|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
749-1335 |
6.40e-173 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 526.27 E-value: 6.40e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 749 WTLIKLIASFNKKEWHMMLVGIFFSAIcgagnptqAVFFAKLISSLSRPIVNEEIRASIKSDASFWCLMYLMLALVQCLA 828
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLL--------SALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 829 FSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTV 908
Cdd:COG1132 78 SYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 909 ALALGWKLALVCIATIPILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQH 988
Cdd:COG1132 156 LFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 989 ASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHEYDM--FTFFIVFSSVIFGA-QSAGSVFSfapDMGKATEAAR 1065
Cdd:COG1132 236 ANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVgdLVAFILYLLRLFGPlRQLANVLN---QLQRALASAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1066 DLKELFDRKPTVDTWSNEGDLiKQVDGTIEFRDVHFRYPtrPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERF 1145
Cdd:COG1132 313 RIFELLDEPPEIPDPPGAVPL-PPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1146 YDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGaNNDVTDEQIKFACQEANIYDFIMSLPDGMNT 1225
Cdd:COG1132 390 YDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYG-RPDATDEEVEEAAKAAQAHEFIEALPDGYDT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1226 LVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFD 1305
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLD 548
|
570 580 590
....*....|....*....|....*....|
gi 164423939 1306 QGRIVEQGTHSELMKKNGRYAELVNLQSLE 1335
Cdd:COG1132 549 DGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
138-672 |
1.07e-151 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 470.42 E-value: 1.07e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 138 TDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGIS 217
Cdd:COG1132 57 LSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 218 EKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAF 297
Cdd:COG1132 137 HGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 298 GTQDRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQGSRFLLSGDTELRKILTVMMSVMIGAFNLGN 377
Cdd:COG1132 217 GREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 378 IAPNLQAFVTALGAAAKIYNTIDRESPIDSSsEEGGKLENVVGTIRLENIKHIYPSRPDVVvmEDVSLVIPAGKTTALVG 457
Cdd:COG1132 297 LANVLNQLQRALASAERIFELLDEPPEIPDP-PGAVPLPPVRGEIEFENVSFSYPGDRPVL--KDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 458 ASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGLIGtkweseseeQQRE 537
Cdd:COG1132 374 PSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD---------ATDE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 538 RIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAE 617
Cdd:COG1132 445 EVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK 524
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 618 GRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLVTAQAIAA 672
Cdd:COG1132 525 GRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
124-1331 |
3.79e-149 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 489.54 E-value: 3.79e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 124 FQNYFAGVTTYDDFTDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKlgagEVTT 203
Cdd:PTZ00265 79 FVSVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDN----NPGS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 204 RITADTNLIQEGISEKVGLTLQALATFIAAFvIGFVsFW------KLTLILlSTVVALTLVMGGGSQFIIKFSKQNIAAY 277
Cdd:PTZ00265 155 KLTSDLDFYLEQVNAGIGTKFITIFTYASAF-LGLY-IWslfknaRLTLCI-TCVFPLIYICGVICNKKVKINKKTSLLY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 278 AEGG-SVADEVISSVRNAIAFGTQDRLARRYDahLTRAEHFGFRLKGS-IGVMVAGMMTVLYL-NYGLAFWQGSRFLLS- 353
Cdd:PTZ00265 232 NNNTmSIIEEALVGIRTVVSYCGEKTILKKFN--LSEKLYSKYILKANfMESLHIGMINGFILaSYAFGFWYGTRIIISd 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 354 -------GDTELRKILTVMMSVMIGAFNLGNIAPNLQAFVTALGAAAKIYNTIDREsPIDSSSEEGGKLENVvGTIRLEN 426
Cdd:PTZ00265 310 lsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRK-PLVENNDDGKKLKDI-KKIQFKN 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDV-DISTLNVRWLRQQIALVSQ 505
Cdd:PTZ00265 388 VRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQ 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 506 EPTLFACTIYDNIRHGLIGTK---WESESEEQQRERIYEAARKANA---------------------------------- 548
Cdd:PTZ00265 468 DPLLFSNSIKNNIKYSLYSLKdleALSNYYNEDGNDSQENKNKRNScrakcagdlndmsnttdsneliemrknyqtikds 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 549 -----------HDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALE--VA 615
Cdd:PTZ00265 548 evvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKG 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 616 AEGRTTITIAHRLSTIKDAHNIVVM-----------------------------------------------AQGRIVEQ 648
Cdd:PTZ00265 628 NENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnAGSYIIEQ 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 649 GTHAELLA-KRGAYYKLVTAQAIAAvnEMTAEEEAALDQQEEAALIRKATRN---SQKEGGAAGYVEDPEDNIAEKLDRS 724
Cdd:PTZ00265 708 GTHDALMKnKNGIYYTMINNQKVSS--KKSSNNDNDKDSDMKSSAYKDSERGydpDEMNGNSKHENESASNKKSCKMSDE 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 725 KSQQSVSSVAIA------ARKKEEPKEygLWTLIKLIASFNKKewhmmLVGIFFSAICGAG-NPTQAVFFAKLISSLSRp 797
Cdd:PTZ00265 786 NASENNAGGKLPflrnlfKRKPKAPNN--LRIVYREIFSYKKD-----VTIIALSILVAGGlYPVFALLYAKYVSTLFD- 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 798 ivneeiRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRDENSAGALTSFL 877
Cdd:PTZ00265 858 ------FANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHI 931
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 878 STETThvagLSGVTLGTIIMVLTTLIAACTVALALGWKLalvCIATIPILLGCGFYRFWMIAHYQRRAKSA--------- 948
Cdd:PTZ00265 932 NRDVH----LLKTGLVNNIVIFTHFIVLFLVSMVMSFYF---CPIVAAVLTGTYFIFMRVFAIRARLTANKdvekkeinq 1004
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 949 YAGSASYAS-------------EAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALG 1015
Cdd:PTZ00265 1005 PGTVFAYNSddeifkdpsfliqEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFA 1084
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1016 FWYGGTLIAKHEYDMFTFFIVFSSVIFGAQSAGSVFSFAPDMGKATEAARDLKELFDRKPTVDTWSNEGDLIKQ---VDG 1092
Cdd:PTZ00265 1085 YWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKG 1164
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYD------------------------- 1147
Cdd:PTZ00265 1165 KIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqg 1244
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1148 -----------------------------PLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGaNNDV 1198
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KEDA 1323
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1199 TDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAAL-- 1276
Cdd:PTZ00265 1324 TREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvd 1403
|
1370 1380 1390 1400 1410 1420
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1277 --DKAAKgrTTIAVAHRLSTIQKADIIYVFDQ----GRIVE-QGTHSELMK-KNGRYAELVNL 1331
Cdd:PTZ00265 1404 ikDKADK--TIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1094-1332 |
1.91e-144 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 437.74 E-value: 1.91e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQGTVRENIILGANnDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPK 1253
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1254 ILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELVNLQ 1332
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
756-1077 |
1.31e-138 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 425.71 E-value: 1.31e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 756 ASFNKKEWHMMLVGIFFSAICGAGNPTQAVFFAKLISSLSRPIVNEeirasIKSDASFWCLMYLMLALVQCLAFSVQGWL 835
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDE-----LRSEANFWALMFLVLAIVAGIAYFLQGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 836 FAKCSERLIHRVRDMAFRSFLRQDVEFFDRDENSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWK 915
Cdd:cd18578 76 FGIAGERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 916 LALVCIATIPILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVL 995
Cdd:cd18578 156 LALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 996 KSSLLFAASNSLMFLAFALGFWYGGTLIAKHEYDMFTFFIVFSSVIFGAQSAGSVFSFAPDMGKATEAARDLKELFDRKP 1075
Cdd:cd18578 236 ISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKP 315
|
..
gi 164423939 1076 TV 1077
Cdd:cd18578 316 EI 317
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
739-1332 |
1.47e-136 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 435.03 E-value: 1.47e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 739 KKEEPKEYGLWTLIKLIASFnKKEWHMMLVGIFFSAICGAGNPtqavFFAKLIssLSRPIVNEEIrasiksdASFW--CL 816
Cdd:COG2274 135 DKRGEKPFGLRWFLRLLRRY-RRLLLQVLLASLLINLLALATP----LFTQVV--IDRVLPNQDL-------STLWvlAI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 817 MYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLStETTHVA-GLSGVTLGTI 895
Cdd:COG2274 201 GLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFES--RSVGDLASRFR-DVESIReFLTGSLLTAL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 896 IMVLTTLIAAcTVALALGWKLALVCIATIPILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDV 975
Cdd:COG2274 278 LDLLFVLIFL-IVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 976 LQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHEY---DMFTFFIVFSSVIfgaQSAGSVFS 1052
Cdd:COG2274 357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLtlgQLIAFNILSGRFL---APVAQLIG 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1053 FAPDMGKATEAARDLKELFDRKPTVDTWSNEGDLiKQVDGTIEFRDVHFRYPTRpEQPVLRGLNLSIQPGQYVALVGASG 1132
Cdd:COG2274 434 LLQRFQDAKIALERLDDILDLPPEREEGRSKLSL-PRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSG 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1133 CGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGaNNDVTDEQIKFACQEANI 1212
Cdd:COG2274 512 SGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLG-DPDATDEEIIEAARLAGL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1213 YDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRL 1292
Cdd:COG2274 591 HDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRL 670
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 164423939 1293 STIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELVNLQ 1332
Cdd:COG2274 671 STIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
422-668 |
1.08e-130 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 401.53 E-value: 1.08e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIA 501
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFACTIYDNIRHGLigtkwesesEEQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIA 581
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGK---------PDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 582 RAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAY 661
Cdd:cd03249 152 RALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVY 231
|
....*..
gi 164423939 662 YKLVTAQ 668
Cdd:cd03249 232 AKLVKAQ 238
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
816-1332 |
1.74e-122 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 392.53 E-value: 1.74e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 816 LMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTI 895
Cdd:TIGR02204 62 AFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDK--NRSGEVVSRLTTDTTLLQSVIGSSLSMA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 896 IMVLTTLIAACTVALALGWKLALVCIATIPILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDV 975
Cdd:TIGR02204 140 LRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 976 LQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTL-----IAKHEYDMFTFFIVFSsvifgAQSAGSV 1050
Cdd:TIGR02204 220 RSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDviagkMSAGTLGQFVFYAVMV-----AGSIGTL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1051 FSFAPDMGKATEAARDLKELFDRKPTVDTWSNEGDLIKQVDGTIEFRDVHFRYPTRPEQPVLRGLNLSIQPGQYVALVGA 1130
Cdd:TIGR02204 295 SEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGP 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1131 SGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGaNNDVTDEQIKFACQEA 1210
Cdd:TIGR02204 375 SGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG-RPDATDEEVEAAARAA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1211 NIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAH 1290
Cdd:TIGR02204 454 HAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAH 533
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 164423939 1291 RLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELVNLQ 1332
Cdd:TIGR02204 534 RLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
736-1329 |
1.97e-116 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 380.99 E-value: 1.97e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 736 AARKKEEPKEYGLWTLIKLIASFNKKEWHMMLVGIFFSAIcgagnptqavffakliSSLSR---PIVNEEIRASIKSDAS 812
Cdd:TIGR00958 133 ASEKEAEQGQSETADLLFRLLGLSGRDWPWLISAFVFLTL----------------SSLGEmfiPFYTGRVIDTLGGDKG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 813 FWCL---MYLM--LALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDrdENSAGALTSFLSTETTHVAGL 887
Cdd:TIGR00958 197 PPALasaIFFMclLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 888 SGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIPIL-LGCGFYRFWmiahYQ---RRAKSAYAGSASYASEAITAM 963
Cdd:TIGR00958 275 LSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVfLAEKVFGKR----YQllsEELQEAVAKANQVAEEALSGM 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 964 RTVASLTREQDVLQHYKDSLAKQQHASLISVLkSSLLFAASNSLMFLAFALG-FWYGGTLIAKHEY---DMFTFfivfss 1039
Cdd:TIGR00958 351 RTVRSFAAEEGEASRFKEALEETLQLNKRKAL-AYAGYLWTTSVLGMLIQVLvLYYGGQLVLTGKVssgNLVSF------ 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1040 VIFGAQSAGSVF---SFAPDMGKATEAARDLKELFDRKPTVdtwSNEGDLI-KQVDGTIEFRDVHFRYPTRPEQPVLRGL 1115
Cdd:TIGR00958 424 LLYQEQLGEAVRvlsYVYSGMMQAVGASEKVFEYLDRKPNI---PLTGTLApLNLEGLIEFQDVSFSYPNRPDVPVLKGL 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1116 NLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGAn 1195
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGL- 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1196 NDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAa 1275
Cdd:TIGR00958 580 TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE- 658
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 164423939 1276 lDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELV 1329
Cdd:TIGR00958 659 -SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
138-668 |
1.37e-114 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 371.34 E-value: 1.37e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 138 TDELARLVLYFVY-------LAIGEFVTMYITTvgfiYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTN 210
Cdd:TIGR02204 51 KDSSGLLNRYFAFllvvalvLALGTAARFYLVT----WLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 211 LIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISS 290
Cdd:TIGR02204 127 LLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 291 VRNAIAFGTQDRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQGSRFLLSGDTELRKILTVMMSVMI 370
Cdd:TIGR02204 207 IRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 371 GAFNLGNIAPNLQAFVTALGAAAKIYNTIDRESPIDSSSEEGGKLENVVGTIRLENIKHIYPSRPDVVVMEDVSLVIPAG 450
Cdd:TIGR02204 287 VAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 451 KTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGligtkwese 530
Cdd:TIGR02204 367 ETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG--------- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 531 SEEQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQA 610
Cdd:TIGR02204 438 RPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQ 517
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 611 ALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLVTAQ 668
Cdd:TIGR02204 518 ALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
110-395 |
3.10e-114 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 359.87 E-value: 3.10e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 110 LPLMTVIFGNLQGTFQNYFAGVTTYDDFTDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQN 189
Cdd:cd18577 15 LPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 190 IGFFDKLGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKF 269
Cdd:cd18577 95 IAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 270 SKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQGSR 349
Cdd:cd18577 175 TKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSR 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 164423939 350 FLLSGDTELRKILTVMMSVMIGAFNLGNIAPNLQAFVTALGAAAKI 395
Cdd:cd18577 255 LVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
151-669 |
1.70e-112 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 369.93 E-value: 1.70e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 151 LAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITaDTNLIQEGISekvGLTLQALA-- 228
Cdd:COG2274 205 ALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLT---GSLLTALLdl 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 229 --TFIAAFVIGFVSfWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRLARR 306
Cdd:COG2274 281 lfVLIFLIVLFFYS-PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRR 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 307 YDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQGSRFLLSGDtelrkiLTV--------MMSVMIGAF-NLGN 377
Cdd:COG2274 360 WENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQ------LTLgqliafniLSGRFLAPVaQLIG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 378 IAPNLQAFVTALGAAAKIYNTiDRESPIDSSSEEGGKLEnvvGTIRLENIKHIYPSRPDVVVmEDVSLVIPAGKTTALVG 457
Cdd:COG2274 434 LLQRFQDAKIALERLDDILDL-PPEREEGRSKLSLPRLK---GDIELENVSFRYPGDSPPVL-DNISLTIKPGERVAIVG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 458 ASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGligtkweseSEEQQRE 537
Cdd:COG2274 509 RSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLG---------DPDATDE 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 538 RIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAE 617
Cdd:COG2274 580 EIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK 659
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 164423939 618 GRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLVTAQA 669
Cdd:COG2274 660 GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
120-665 |
1.67e-108 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 359.04 E-value: 1.67e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 120 LQGTFQNYFAGVTTYDDFTD----ELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDK 195
Cdd:TIGR00958 175 LGEMFIPFYTGRVIDTLGGDkgppALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 196 LGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFVIGFVSFWKL---TLILLSTVVALTLVMGggsQFIIKFSKQ 272
Cdd:TIGR00958 255 NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLtmvTLINLPLVFLAEKVFG---KRYQLLSEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 273 NIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAHLTRAEHFGFR-----LKGSIGVMVAGM-MTVLYLNYGlafwq 346
Cdd:TIGR00958 332 LQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRkalayAGYLWTTSVLGMlIQVLVLYYG----- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 347 gSRFLLSGDTELRKILTVM---MSVMIGAFNLGNIAPNLQafvTALGAAAKIYNTIDRESPIDSSSEEggKLENVVGTIR 423
Cdd:TIGR00958 407 -GQLVLTGKVSSGNLVSFLlyqEQLGEAVRVLSYVYSGMM---QAVGASEKVFEYLDRKPNIPLTGTL--APLNLEGLIE 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 424 LENIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALV 503
Cdd:TIGR00958 481 FQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 504 SQEPTLFACTIYDNIRHGLIGTKweseseeqqRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARA 583
Cdd:TIGR00958 561 GQEPVLFSGSVRENIAYGLTDTP---------DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 584 IVSDPKILLLDEATSALDTKSEGVVQAALEvaAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYK 663
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
..
gi 164423939 664 LV 665
Cdd:TIGR00958 710 LV 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
768-1332 |
6.89e-108 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 352.87 E-value: 6.89e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 768 VGIFFSAICGA-GNPTQAVFFAKLIsslsRPIVNEEIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKCSERLIHR 846
Cdd:TIGR02203 13 KAGLVLAGVAMiLVAATESTLAALL----KPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 847 VRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIPI 926
Cdd:TIGR02203 89 IRVRMFEKLLGLPVSFFDR--QPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 927 LLgcgfyrfWMIAHYQRRAKS-------AYAGSASYASEAITAMRTV------ASLTREQDVLQHYKDSLAKQQhASLIS 993
Cdd:TIGR02203 167 LS-------ILMRRVSKRLRRiskeiqnSMGQVTTVAEETLQGYRVVklfggqAYETRRFDAVSNRNRRLAMKM-TSAGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 994 VLKSSLLFAASNSLMFLAFALGFWYG-GTLIAKheydmfTFFIVFSSVIFGAQSAGSVFSFAPDMGKATEAARDLKELFD 1072
Cdd:TIGR02203 239 ISSPITQLIASLALAVVLFIALFQAQaGSLTAG------DFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1073 RKPTVDTWSNEgdlIKQVDGTIEFRDVHFRYPTRpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGG 1152
Cdd:TIGR02203 313 SPPEKDTGTRA---IERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1153 IFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGANNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGA 1232
Cdd:TIGR02203 389 ILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1233 LLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQ 1312
Cdd:TIGR02203 469 LLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVER 548
|
570 580
....*....|....*....|
gi 164423939 1313 GTHSELMKKNGRYAELVNLQ 1332
Cdd:TIGR02203 549 GTHNELLARNGLYAQLHNMQ 568
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
144-664 |
1.37e-103 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 340.93 E-value: 1.37e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 144 LVLYFVYLAIGEFVTMYITTvgfiYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLT 223
Cdd:TIGR02203 60 VIGLAVLRGICSFVSTYLLS----WVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 224 LQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRL 303
Cdd:TIGR02203 136 VRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 304 ARRYDAHLTRAEHFGFRLK--GSIG------VMVAGMMTVLYLnyglAFWQ-GSRFLLSGDtelrkiLTVMMSVMIGAF- 373
Cdd:TIGR02203 216 TRRFDAVSNRNRRLAMKMTsaGSISspitqlIASLALAVVLFI----ALFQaQAGSLTAGD------FTAFITAMIALIr 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 374 ---NLGNIAPNLQafvTALGAAAKIYNTIDRESPIDssseEGGK-LENVVGTIRLENIKHIYPSRpDVVVMEDVSLVIPA 449
Cdd:TIGR02203 286 plkSLTNVNAPMQ---RGLAAAESLFTLLDSPPEKD----TGTRaIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 450 GKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGLIGTkwes 529
Cdd:TIGR02203 358 GETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQ---- 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 530 eseeQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQ 609
Cdd:TIGR02203 434 ----ADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQ 509
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 610 AALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKL 664
Cdd:TIGR02203 510 AALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1094-1328 |
6.76e-103 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 326.50 E-value: 6.76e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEqPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQGTVRENIILGaNNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPK 1253
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1254 ILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAEL 1328
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
760-1323 |
8.01e-103 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 338.66 E-value: 8.01e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 760 KKEWHMMLVGIFFSAICGAGNPTQAVFFAKLISSLSrpivneeIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKC 839
Cdd:COG4988 13 RGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLI-------IGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 840 SERLIHRVRDMAFRSFLRQDVEFFDRDenSAGALTSFLsteTTHVAGL----SGVTLGTIIMVLTTLIAACTVALaLGWK 915
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGK--STGELATLL---TEGVEALdgyfARYLPQLFLAALVPLLILVAVFP-LDWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 916 LALVCIATIP------ILLGcgfyrfWMIAHYQRRAKSAYAG-SASYAsEAITAMRTVASLTREQDVLQHYKDSlAKQQH 988
Cdd:COG4988 160 SGLILLVTAPliplfmILVG------KGAAKASRRQWRALARlSGHFL-DRLRGLTTLKLFGRAKAEAERIAEA-SEDFR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 989 ASLISVLKSSLL------FAASNSLMFLAFALGFWY-GGTLiakheyDMFT-FFIVFSSVIFgaqsagsvfsFAP--DMG 1058
Cdd:COG4988 232 KRTMKVLRVAFLssavleFFASLSIALVAVYIGFRLlGGSL------TLFAaLFVLLLAPEF----------FLPlrDLG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1059 -------KATEAARDLKELFDRKPTVDTWSNEGDLIKQvDGTIEFRDVHFRYPtrPEQPVLRGLNLSIQPGQYVALVGAS 1131
Cdd:COG4988 296 sfyharaNGIAAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1132 GCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGaNNDVTDEQIKFACQEAN 1211
Cdd:COG4988 373 GAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLG-RPDASDEELEAALEAAG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1212 IYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHR 1291
Cdd:COG4988 452 LDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHR 531
|
570 580 590
....*....|....*....|....*....|..
gi 164423939 1292 LSTIQKADIIYVFDQGRIVEQGTHSELMKKNG 1323
Cdd:COG4988 532 LALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
214-680 |
5.85e-101 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 334.87 E-value: 5.85e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 214 EGISEKVGLTL-QALATFI-AAFVIGFVSF---WKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVAdevI 288
Cdd:COG5265 146 KGIEFLLRFLLfNILPTLLeIALVAGILLVkydWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRA---V 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 289 SSVRNA---IAFGTQDRLARRYDAHLTRAEHFGFRLKGSIG-------VMVAGMMTVLYLNYGLAFWQGSrfllsgdtel 358
Cdd:COG5265 223 DSLLNYetvKYFGNEAREARRYDEALARYERAAVKSQTSLAllnfgqaLIIALGLTAMMLMAAQGVVAGT---------- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 359 rkiLTVMMSVMIGAFNLGNIAP-NLQAFV-----TALGAAAKIYNTIDRESPIdSSSEEGGKLENVVGTIRLENIKHIY- 431
Cdd:COG5265 293 ---MTVGDFVLVNAYLIQLYIPlNFLGFVyreirQALADMERMFDLLDQPPEV-ADAPDAPPLVVGGGEVRFENVSFGYd 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 432 PSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFA 511
Cdd:COG5265 369 PERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFN 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 512 CTIYDNIRHGLIGtkweseseeQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKIL 591
Cdd:COG5265 446 DTIAYNIAYGRPD---------ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPIL 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 592 LLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLVTAQAIA 671
Cdd:COG5265 517 IFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEE 596
|
....*....
gi 164423939 672 AVNEMTAEE 680
Cdd:COG5265 597 EEAEEALAA 605
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1094-1332 |
7.19e-101 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 321.10 E-value: 7.19e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQGTVRENIILGaNNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPK 1253
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1254 ILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELVNLQ 1332
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
422-664 |
3.28e-100 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 319.18 E-value: 3.28e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVVVmEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIA 501
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFACTIYDNIRHGLIGtkweseseeQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIA 581
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPG---------ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 582 RAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAY 661
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
...
gi 164423939 662 YKL 664
Cdd:cd03251 231 AKL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1092-1323 |
1.94e-99 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 316.86 E-value: 1.94e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1092 GTIEFRDVHFRYptRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSF 1171
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1172 IALVSQEPTLYQGTVRENIILGaNNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRD 1251
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1252 PKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNG 1323
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
841-1331 |
3.96e-99 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 328.65 E-value: 3.96e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 841 ERLI-HrvrDMAFR--SFLRqdVEFFDRDE-NSAGALTSF-----LSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALA 911
Cdd:COG4987 75 ERLVsH---DATLRllADLR--VRLYRRLEpLAPAGLARLrsgdlLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 912 LGW---KLALVCIATIPILLGCGFYRFWMIA-HYQRRAKSAYAGSASYASEAITAMRTVASLTReqdvLQHYKDSLAKQQ 987
Cdd:COG4987 150 LAFfspALALVLALGLLLAGLLLPLLAARLGrRAGRRLAAARAALRARLTDLLQGAAELAAYGA----LDRALARLDAAE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 988 HASLISVLKSSLLFAASNSLMFLAFALG----FWYGGTLIAKHEYDmFTFFIVFssvIFGAQSAGSVFSFAPD----MGK 1059
Cdd:COG4987 226 ARLAAAQRRLARLSALAQALLQLAAGLAvvavLWLAAPLVAAGALS-GPLLALL---VLAALALFEALAPLPAaaqhLGR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1060 ATEAARDLKELFDRKPTVDtwSNEGDLIKQVDGTIEFRDVHFRYPTRPeQPVLRGLNLSIQPGQYVALVGASGCGKSTTI 1139
Cdd:COG4987 302 VRAAARRLNELLDAPPAVT--EPAEPAPAPGGPSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1140 ALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILgANNDVTDEQIKFACQEANIYDFIMSL 1219
Cdd:COG4987 379 ALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRL-ARPDATDEELWAALERVGLGDWLAAL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1220 PDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKAD 1299
Cdd:COG4987 458 PDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMD 537
|
490 500 510
....*....|....*....|....*....|..
gi 164423939 1300 IIYVFDQGRIVEQGTHSELMKKNGRYAELVNL 1331
Cdd:COG4987 538 RILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
835-1337 |
2.16e-98 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 327.93 E-value: 2.16e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 835 LFAKCSERLIHRVRDMAFRSFLRQDVEF-FDRdenSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTV-ALAL 912
Cdd:COG5265 101 LFARVTQRAVRRLALEVFRHLHALSLRFhLER---QTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGIlLVKY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 913 GWKLALVCIATIpiLLGCGFYRF---WMIaHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHA 989
Cdd:COG5265 178 DWWFALITLVTV--VLYIAFTVVvteWRT-KFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 990 SLisvlKSSLLFAASNSLMFLAFALG----FWYGGTLIAKHEYDM--F----TFFI-VFSSVIFgaqsAGSVF-----SF 1053
Cdd:COG5265 255 AV----KSQTSLALLNFGQALIIALGltamMLMAAQGVVAGTMTVgdFvlvnAYLIqLYIPLNF----LGFVYreirqAL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1054 ApDMGKateaardLKELFDRKPTVDTWSNEGDLiKQVDGTIEFRDVHFRYptRPEQPVLRGLNLSIQPGQYVALVGASGC 1133
Cdd:COG5265 327 A-DMER-------MFDLLDQPPEVADAPDAPPL-VVGGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGA 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1134 GKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGaNNDVTDEQIKFACQEANIY 1213
Cdd:COG5265 396 GKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG-RPDASEEEVEAAARAAQIH 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1214 DFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLS 1293
Cdd:COG5265 475 DFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLS 554
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 164423939 1294 TIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELVNLQSLEKH 1337
Cdd:COG5265 555 TIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEE 598
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
422-668 |
3.37e-95 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 305.31 E-value: 3.37e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIY-PSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQI 500
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEPTLFACTIYDNIRHGLIGtkweseseeQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAI 580
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPD---------ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 581 ARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGA 660
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
|
....*...
gi 164423939 661 YYKLVTAQ 668
Cdd:cd03253 229 YAEMWKAQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
808-1332 |
3.76e-95 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 318.12 E-value: 3.76e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 808 KSDASFWCLMYLM---LALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDrdENSAGALTSFLSTETTHV 884
Cdd:PRK11176 58 KADRSVLKWMPLVvigLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 885 AGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIPILlgcgfyrFWMIAHYQRRAKSAyagsasyaSEAI-TAM 963
Cdd:PRK11176 136 ASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIV-------SIAIRVVSKRFRNI--------SKNMqNTM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 964 RTVASlTREQdVLQHYKDSLA------------------KQQHASLISVlkSSLL-----FAASNSLMFLAFALGF-WYG 1019
Cdd:PRK11176 201 GQVTT-SAEQ-MLKGHKEVLIfggqevetkrfdkvsnrmRQQGMKMVSA--SSISdpiiqLIASLALAFVLYAASFpSVM 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1020 GTLIAKheydmfTFFIVFSSVIFGAQSAGSVFSFAPDMGKATEAARDLKELFDRKPTVDTWSNEgdlIKQVDGTIEFRDV 1099
Cdd:PRK11176 277 DTLTAG------TITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKRV---IERAKGDIEFRNV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1100 HFRYPTRpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEP 1179
Cdd:PRK11176 348 TFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1180 TLYQGTVRENIILGANNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDE 1259
Cdd:PRK11176 427 HLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1260 ATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELVNLQ 1332
Cdd:PRK11176 507 ATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
886-1334 |
1.04e-89 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 303.04 E-value: 1.04e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 886 GLSGVTLG------TIIMVLTTLIAactVALALGWKLALVCIATIPIllgcgfyrFWMIAHY--------QRRAKSAYAG 951
Cdd:PRK13657 125 ALFGLWLEfmrehlATLVALVVLLP---LALFMNWRLSLVLVVLGIV--------YTLITTLvmrktkdgQAAVEEHYHD 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 952 SASYASEAITAMRTVASLTR---EQDVLQHYKDSLAKQQHA-----SLISVLKSsllfAASNSLMFLAFALGFWYG---- 1019
Cdd:PRK13657 194 LFAHVSDAIGNVSVVQSYNRieaETQALRDIADNLLAAQMPvlswwALASVLNR----AASTITMLAILVLGAALVqkgq 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1020 ---GTLIAkheydmftfFIVFSSVIFG-----AQSAGSVFSFAPDMgkateaaRDLKELFDRKPTVDTWSNEGDLiKQVD 1091
Cdd:PRK13657 270 lrvGEVVA---------FVGFATLLIGrldqvVAFINQVFMAAPKL-------EEFFEVEDAVPDVRDPPGAIDL-GRVK 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1092 GTIEFRDVHFRYPTRPeqPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSF 1171
Cdd:PRK13657 333 GAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1172 IALVSQEPTLYQGTVRENIILGaNNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRD 1251
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRVG-RPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKD 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1252 PKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELVNL 1331
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRA 569
|
...
gi 164423939 1332 QSL 1334
Cdd:PRK13657 570 QGM 572
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
420-659 |
4.87e-87 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 282.19 E-value: 4.87e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 420 GTIRLENIKHIYpsRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQ 499
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEPTLFACTIYDNIRHGligtkweseSEEQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIA 579
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG---------RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 580 IARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRG 659
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
388-659 |
2.35e-86 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 292.82 E-value: 2.35e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 388 ALGAAAKIYNTIDRESPIDSSSEEGGKLENVVgTIRLENIKHIYPSRPDVVvmEDVSLVIPAGKTTALVGASGSGKSTIV 467
Cdd:COG4988 304 GIAAAEKIFALLDAPEPAAPAGTAPLPAAGPP-SIELEDVSFSYPGGRPAL--DGLSLTIPPGERVALVGPSGAGKSTLL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 468 GLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGligtkweseSEEQQRERIYEAARKAN 547
Cdd:COG4988 381 NLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLG---------RPDASDEELEAALEAAG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 548 AHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHR 627
Cdd:COG4988 452 LDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHR 531
|
250 260 270
....*....|....*....|....*....|..
gi 164423939 628 LSTIKDAHNIVVMAQGRIVEQGTHAELLAKRG 659
Cdd:COG4988 532 LALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
165-664 |
1.29e-83 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 285.76 E-value: 1.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 165 GFI--YSGEHISGK----IREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFVIGF 238
Cdd:PRK11176 82 SFIssYCISWVSGKvvmtMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 239 VSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAHLTRAEHFG 318
Cdd:PRK11176 162 YYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 319 FRLKGSIGV------MVA--GMMTVLYLnyglAFWQGSRFLLSGDTelrkiLTVMMSVMIGAF----NLGNIapNLQaFV 386
Cdd:PRK11176 242 MKMVSASSIsdpiiqLIAslALAFVLYA----ASFPSVMDTLTAGT-----ITVVFSSMIALMrplkSLTNV--NAQ-FQ 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 387 TALGAAAKIYNTIDRESPIDSSSEEggkLENVVGTIRLENIKHIYPSRpDVVVMEDVSLVIPAGKTTALVGASGSGKSTI 466
Cdd:PRK11176 310 RGMAACQTLFAILDLEQEKDEGKRV---IERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTI 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 467 VGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGligtkwesESEEQQRERIYEAARKA 546
Cdd:PRK11176 386 ANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYA--------RTEQYSREQIEEAARMA 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 547 NAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAH 626
Cdd:PRK11176 458 YAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
490 500 510
....*....|....*....|....*....|....*...
gi 164423939 627 RLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKL 664
Cdd:PRK11176 538 RLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1094-1308 |
4.08e-81 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 263.47 E-value: 4.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQGTVRENIilganndvtdeqikfacqeaniydfimslpdgmntlvgskgalLSGGQKQRIAIARALIRDPK 1253
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1254 ILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGR 1308
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
139-668 |
5.58e-81 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 281.63 E-value: 5.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 139 DELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNlIQEGISe 218
Cdd:TIGR01846 176 STLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRELEQ-IRNFLT- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 219 kvGLTLQALATFIAAFVIGFVSFW---KLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAI 295
Cdd:TIGR01846 254 --GSALTVVLDLLFVVVFLAVMFFyspTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 296 AFGTQDRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQGSRFLLSGDtelrkiLTVMMSVmigAFNL 375
Cdd:TIGR01846 332 ATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGA------LSPGQLV---AFNM 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 376 --GNI-APNL------QAFVTALGAAAKIYNTIDreSPIDSSSEEGGKLENVVGTIRLENIKHIYpsRPDV-VVMEDVSL 445
Cdd:TIGR01846 403 laGRVtQPVLrlaqlwQDFQQTGIALERLGDILN--SPTEPRSAGLAALPELRGAITFENIRFRY--APDSpEVLSNLNL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 446 VIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGLIGt 525
Cdd:TIGR01846 479 DIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPG- 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 526 kweseseeQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSE 605
Cdd:TIGR01846 558 --------APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESE 629
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 606 GVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLVTAQ 668
Cdd:TIGR01846 630 ALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1088-1309 |
1.07e-80 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 264.33 E-value: 1.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1088 KQVDGTIEFRDVHFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE 1167
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1168 YRSFIALVSQEPTLYQGTVRENIILGANnDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARA 1247
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQ-SCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1248 LIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRI 1309
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1094-1332 |
2.34e-80 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 263.96 E-value: 2.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYptRPEQP-VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFI 1172
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQEPTLYQGTVRENIILgANNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDP 1252
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIAL-ADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1253 KILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELVNLQ 1332
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
422-668 |
3.87e-80 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 263.19 E-value: 3.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYpsRPD-VVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQI 500
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEPTLFACTIYDNIRHGLIGtkweseseeQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAI 580
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG---------MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 581 ARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGA 660
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
....*...
gi 164423939 661 YYKLVTAQ 668
Cdd:cd03252 230 YAYLYQLQ 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
195-664 |
4.17e-79 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 272.41 E-value: 4.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 195 KLGAGEVTTRITADTNLIQegisekvGLTLQALATFIAAFVIGFVSFWKLTLIL--LSTVVALTLVMGGgsqFII----- 267
Cdd:COG4987 108 RLRSGDLLNRLVADVDALD-------NLYLRVLLPLLVALLVILAAVAFLAFFSpaLALVLALGLLLAG---LLLpllaa 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 268 KFSKQNIAAYAEG-GSVADEVISSVRNA---IAFGTQDRLARRYDA---HLTRAEHFGFRLKG---SIGVMVAGMMTVLy 337
Cdd:COG4987 178 RLGRRAGRRLAAArAALRARLTDLLQGAaelAAYGALDRALARLDAaeaRLAAAQRRLARLSAlaqALLQLAAGLAVVA- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 338 lnyglAFWQGSRFLLSGDTELRKILTVMMSVMiGAF-NLGNIAPNLQAFVTALGAAAKIYNTIDRESPIdsSSEEGGKLE 416
Cdd:COG4987 257 -----VLWLAAPLVAAGALSGPLLALLVLAAL-ALFeALAPLPAAAQHLGRVRAAARRLNELLDAPPAV--TEPAEPAPA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 417 NVVGTIRLENIKHIYPSRPDVVVmEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWL 496
Cdd:COG4987 329 PGGPSLELEDVSFRYPGAGRPVL-DGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 497 RQQIALVSQEPTLFACTIYDNIRHGLIGtkweseseeQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQ 576
Cdd:COG4987 408 RRRIAVVPQRPHLFDTTLRENLRLARPD---------ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 577 RIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLA 656
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558
|
....*...
gi 164423939 657 KRGAYYKL 664
Cdd:COG4987 559 QNGRYRQL 566
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
915-1333 |
1.15e-78 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 274.70 E-value: 1.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 915 KLALVCIATIPIllgcgFYRFWMIAH--YQRRAKSAYAGSA---SYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHA 989
Cdd:TIGR01846 279 TLTGVVIGSLVC-----YALLSVFVGpiLRKRVEDKFERSAaatSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAA 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 990 SLiSVLKSSLLFAASNSLMF-LAFALGFWYGGTLIAKHEYDMFTFfIVFSsvIFGAQSAGSVFSFAP---DMGKATEAAR 1065
Cdd:TIGR01846 354 SF-RVTNLGNIAGQAIELIQkLTFAILLWFGAHLVIGGALSPGQL-VAFN--MLAGRVTQPVLRLAQlwqDFQQTGIALE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1066 DLKELFDrKPTVDTWSNEGDLIKqVDGTIEFRDVHFRYptRPEQP-VLRGLNLSIQPGQYVALVGASGCGKSTTIALLER 1144
Cdd:TIGR01846 430 RLGDILN-SPTEPRSAGLAALPE-LRGAITFENIRFRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1145 FYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGaNNDVTDEQIKFACQEANIYDFIMSLPDGMN 1224
Cdd:TIGR01846 506 LYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALC-NPGAPFEHVIHAAKLAGAHDFISELPQGYN 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1225 TLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVF 1304
Cdd:TIGR01846 585 TEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVL 664
|
410 420
....*....|....*....|....*....
gi 164423939 1305 DQGRIVEQGTHSELMKKNGRYAELVNLQS 1333
Cdd:TIGR01846 665 EKGQIAESGRHEELLALQGLYARLWQQQS 693
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
379-691 |
1.55e-78 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 271.45 E-value: 1.55e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 379 APNLQAFVTALGAAAkiyntiDRESPIDSSSeeggkLENVVGTIRLENIKHIYPSRPDVVvmEDVSLVIPAGKTTALVGA 458
Cdd:PRK13657 303 APKLEEFFEVEDAVP------DVRDPPGAID-----LGRVKGAVEFDDVSFSYDNSRQGV--EDVSFEAKPGQTVAIVGP 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 459 SGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGligtkweseSEEQQRER 538
Cdd:PRK13657 370 TGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG---------RPDATDEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 539 IYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEG 618
Cdd:PRK13657 441 MRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKG 520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 619 RTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLVTAQAiaavneMTAEEEAALDQQEEAA 691
Cdd:PRK13657 521 RTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQG------MLQEDERRKQPAAEGA 587
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
856-1329 |
1.03e-77 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 272.59 E-value: 1.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 856 LRQDVEFFDrdENSAGALTSFLSTeTTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIPILLGcgfYRF 935
Cdd:TIGR03796 238 LRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVL---ALQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 936 WMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTR---EQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAF 1012
Cdd:TIGR03796 312 LVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKAsglESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1013 ALGFWYGGTLIAKHEYDMFTFfIVFSSVIFGAQS--------AGSVFSFAPDMGKATEAARDLKELFDRKPTVDTWSNEG 1084
Cdd:TIGR03796 392 ALILVVGGLRVMEGQLTIGML-VAFQSLMSSFLEpvnnlvgfGGTLQELEGDLNRLDDVLRNPVDPLLEEPEGSAATSEP 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1085 DliKQVDGTIEFRDVHFRYpTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLN 1164
Cdd:TIGR03796 471 P--RRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIP 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1165 VNEYRSFIALVSQEPTLYQGTVRENIILgANNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAI 1244
Cdd:TIGR03796 548 REVLANSVAMVDQDIFLFEGTVRDNLTL-WDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEI 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1245 ARALIRDPKILLLDEATSALDSESEHVVQAALDKaaKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGR 1324
Cdd:TIGR03796 627 ARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGA 704
|
....*
gi 164423939 1325 YAELV 1329
Cdd:TIGR03796 705 YARLI 709
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
420-645 |
1.11e-77 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 255.86 E-value: 1.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 420 GTIRLENIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQ 499
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEPTLFACTIYDNIRHGLIGTKweseseeqqRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIA 579
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQSCS---------FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 580 IARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRI 645
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
887-1332 |
6.60e-71 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 252.18 E-value: 6.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 887 LSGVTLGTiimVLTTLIAACTVALAL--GWKLALV----CIATIPILLGCGFYRFwmiaHYQRRAKSAYAGSASYASEAI 960
Cdd:TIGR03797 249 LSGSTLTT---LLSGIFALLNLGLMFyySWKLALVavalALVAIAVTLVLGLLQV----RKERRLLELSGKISGLTVQLI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 961 T-------AMRTVASLTR------EQDVLQhykdsLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYG---GTLIA 1024
Cdd:TIGR03797 322 NgisklrvAGAENRAFARwaklfsRQRKLE-----LSAQRIENLLTVFNAVLPVLTSAALFAAAISLLGGAGlslGSFLA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1025 kheydmftFFIVFSSVIFGA-QSAGSVfsfaPDMGKATEAARDLKELFDRKPTVD-TWSNEGDLIkqvdGTIEFRDVHFR 1102
Cdd:TIGR03797 397 --------FNTAFGSFSGAVtQLSNTL----ISILAVIPLWERAKPILEALPEVDeAKTDPGKLS----GAIEVDRVTFR 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1103 YptRPEQP-VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTL 1181
Cdd:TIGR03797 461 Y--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRL 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1182 YQGTVRENIILGANndVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEAT 1261
Cdd:TIGR03797 539 MSGSIFENIAGGAP--LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEAT 616
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1262 SALDSESEHVVQAALDKAAKGRttIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELVNLQ 1332
Cdd:TIGR03797 617 SALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1092-1314 |
6.96e-71 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 236.24 E-value: 6.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1092 GTIEFRDVHFRYptRPE-QPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRS 1170
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1171 FIALVSQEPTLYQGTVRENiiLGANNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIR 1250
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSN--LDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 1251 DPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGT 1314
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
422-644 |
3.48e-70 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 232.27 E-value: 3.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVVVmEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIA 501
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVL-KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFACTIYDNIrhgligtkweseseeqqreriyeaarkanahdfitslpegyetnvgergflLSGGQKQRIAIA 581
Cdd:cd03228 80 YVPQDPFLFSGTIRENI---------------------------------------------------LSGGQRQRIAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 582 RAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGR 644
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
766-1067 |
6.75e-69 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 233.91 E-value: 6.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 766 MLVGIFFSAICGAGNPTQAVFFAKLISSLSRPIVNEEIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKCSERLIH 845
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 846 RVRDMAFRSFLRQDVEFFDrdENSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIP 925
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 926 ILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASN 1005
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1006 SLMFLAFALGFWYGGTLIAKHEYDMFTFFIVFSSVIFGAQSAGSVFSFAPDMGKATEAARDL 1067
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
983-1328 |
9.38e-69 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 242.81 E-value: 9.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 983 LAKQQHASLISVLKSSLLFAASNslmfLAFALGFWYGGTLIAKHEY-DMFTFFIVFSSV--------IFGA-QSAGSVFS 1052
Cdd:PRK11160 234 LAAQRRQANLTGLSQALMILANG----LTVVLMLWLAAGGVGGNAQpGALIALFVFAALaafealmpVAGAfQHLGQVIA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1053 fapdmgkateAARDLKELFDRKPTVDTWSNEGDLIKQvdGTIEFRDVHFRYPTRPeQPVLRGLNLSIQPGQYVALVGASG 1132
Cdd:PRK11160 310 ----------SARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQP-QPVLKGLSLQIKAGEKVALLGRTG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1133 CGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILgANNDVTDEQIKFACQEANI 1212
Cdd:PRK11160 377 CGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL-AAPNASDEALIEVLQQVGL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1213 yDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRL 1292
Cdd:PRK11160 456 -EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRL 534
|
330 340 350
....*....|....*....|....*....|....*.
gi 164423939 1293 STIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAEL 1328
Cdd:PRK11160 535 TGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
820-1329 |
2.68e-68 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 241.72 E-value: 2.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 820 MLALVQCLAFS--VQGWLFAKCSERLIHRVR----DMAFRSFLRQDVEFFDRDENSAGALTSFLSTETthvagLSGVTLG 893
Cdd:TIGR01192 58 TLALWAGFGVFntIAYVLVAREADRLAHGRRatllTEAFGRIISMPLSWHQQRGTSNALHTLLRATET-----LFGLWLE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 894 TIIMVLTTLIAA---CTVALALGWKLALVciatipiLLGCGFYrFWMIAHY--------QRRAKSAYAGSASYASEAITA 962
Cdd:TIGR01192 133 FMRQHLATFVALfllIPTAFAMDWRLSIV-------LMVLGIL-YILIAKLvmqrtkngQAAVEHHYHNVFKHVSDSISN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 963 MRTVASLTR---EQDVLQHYKDSLAKQQHASL-ISVLKSSLLFAASNSLMFLAFALGfwygGTLIAKHEYDM--FTFFIV 1036
Cdd:TIGR01192 205 VSVVHSYNRieaETSALKQFTNNLLSAQYPVLdWWALASGLNRMASTISMMCILVIG----TVLVIKGELSVgeVIAFIG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1037 FSSVIFGAQSAGSVFsfapdMGKATEAARDLKELFDRKPTVDTWSNEGDL--IKQVDGTIEFRDVHFRYPTRPEQpvLRG 1114
Cdd:TIGR01192 281 FANLLIGRLDQMSGF-----ITQIFEARAKLEDFFDLEDSVFQREEPADApeLPNVKGAVEFRHITFEFANSSQG--VFD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1115 LNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGa 1194
Cdd:TIGR01192 354 VSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLG- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1195 NNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQA 1274
Cdd:TIGR01192 433 REGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKN 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1275 ALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELV 1329
Cdd:TIGR01192 513 AIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
190-665 |
8.26e-68 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 243.70 E-value: 8.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 190 IGFFDKLGAGEVTTRITADTNlIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLIllstVVALTLVMGGGSQFIIKF 269
Cdd:TIGR03796 242 VRFFAQRHAGDIASRVQLNDQ-VAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLI----GIAFAAINVLALQLVSRR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 270 SK-QNIAAYAEGGSVADEVISSVRNaI----AFGTQDRLARR---YDAHLTRAEHFGFRLKGSIGVMVAGMMTvlyLNYG 341
Cdd:TIGR03796 317 RVdANRRLQQDAGKLTGVAISGLQS-IetlkASGLESDFFSRwagYQAKLLNAQQELGVLTQILGVLPTLLTS---LNSA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 342 LAFWQGSRFLLSGDTELRKIL---TVMMSVMIGAFNLGNIAPNLQAFVTALGAAAKIYN-----TIDRESPIDSSSEEGG 413
Cdd:TIGR03796 393 LILVVGGLRVMEGQLTIGMLVafqSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRnpvdpLLEEPEGSAATSEPPR 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 414 KLEnvvGTIRLENIKHIYpSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNV 493
Cdd:TIGR03796 473 RLS---GYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 494 RWLRQQIALVSQEPTLFACTIYDNIrhgligTKWESESEEQQrerIYEAARKANAHDFITSLPEGYETNVGERGFLLSGG 573
Cdd:TIGR03796 549 EVLANSVAMVDQDIFLFEGTVRDNL------TLWDPTIPDAD---LVRACKDAAIHDVITSRPGGYDAELAEGGANLSGG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 574 QKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALevAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAE 653
Cdd:TIGR03796 620 QRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEE 697
|
490
....*....|..
gi 164423939 654 LLAKRGAYYKLV 665
Cdd:TIGR03796 698 LWAVGGAYARLI 709
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
433-1323 |
1.96e-67 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 251.02 E-value: 1.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 433 SRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLddvdistlnvrwlRQQIALVSQEPTLFAC 512
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-------------KGSVAYVPQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 513 TIYDNIRHGligtkweseseEQQRERIYEAARKANA--HDfITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKI 590
Cdd:TIGR00957 714 SLRENILFG-----------KALNEKYYQQVLEACAllPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 591 LLLDEATSALDTKS-----EGVVQAalEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLV 665
Cdd:TIGR00957 782 YLFDDPLSAVDAHVgkhifEHVIGP--EGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 666 TAQAiaavnemTAEEEAALDQQEEAALirkatrnsQKEGGAAGYVEDP---EDNIAEKLDRSKSQQSVSS-------VAI 735
Cdd:TIGR00957 860 RTYA-------PDEQQGHLEDSWTALV--------SGEGKEAKLIENGmlvTDVVGKQLQRQLSASSSDSgdqsrhhGSS 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 736 AARKKEEPKEyGLWTL----------IKLIASFNkkewHMMLVGIFFS-AIC--GAGNPTQAVFFAKLISSLSR-PIVNe 801
Cdd:TIGR00957 925 AELQKAEAKE-ETWKLmeadkaqtgqVELSVYWD----YMKAIGLFITfLSIflFVCNHVSALASNYWLSLWTDdPMVN- 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 802 eiraSIKSDASFWCLMYLMLALVQ-------CLAFSVQGWLFAKC-SERLIHRVrdmafrsfLRQDVEFFDRdeNSAGAL 873
Cdd:TIGR00957 999 ----GTQNNTSLRLSVYGALGILQgfavfgySMAVSIGGIQASRVlHQDLLHNK--------LRSPMSFFER--TPSGNL 1064
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 874 TSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALgwklalVCIATIPIL-LGCGFY---RFWMIAHYQRRAKSAY 949
Cdd:TIGR00957 1065 VNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLA------TPIAAVIIPpLGLLYFfvqRFYVASSRQLKRLESV 1138
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 950 AGSASYA--SEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLL-----FAASNSLMFLA-FALgfwyggt 1021
Cdd:TIGR00957 1139 SRSPVYShfNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLavrleCVGNCIVLFAAlFAV------- 1211
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1022 lIAKHEydmFTFFIVFSSVIFGAQSAGSV---FSFAPDMGKATEAARDLKElFDRKPTVDTWSNEGDLIKQV---DGTIE 1095
Cdd:TIGR00957 1212 -ISRHS---LSAGLVGLSVSYSLQVTFYLnwlVRMSSEMETNIVAVERLKE-YSETEKEAPWQIQETAPPSGwppRGRVE 1286
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1096 FRDVHFRYptRPE-QPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIAL 1174
Cdd:TIGR00957 1287 FRNYCLRY--REDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1175 VSQEPTLYQGTVRENiiLGANNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKI 1254
Cdd:TIGR00957 1365 IPQDPVLFSGSLRMN--LDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKI 1442
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1255 LLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNG 1323
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
818-1332 |
9.47e-67 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 237.31 E-value: 9.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 818 YLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSgVTLGTIIM 897
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDT--QPVGQLISRVTNDTEVIRDLY-VTVVATVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 898 VLTTLIAACTVAL-ALGWKLALVCIATIPILLGCgfyrFWMIAHYQ----RRAKSAYAGSASYASEAITAMrTVASLTRE 972
Cdd:PRK10790 148 RSAALIGAMLVAMfSLDWRMALVAIMIFPAVLVV----MVIYQRYStpivRRVRAYLADINDGFNEVINGM-SVIQQFRQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 973 Q---------DVLQHYkdsLAKQQHASLISVLKSSLLfaasnSLmFLAFALGfwygGTLIakheydMFTFfivfSSVifG 1043
Cdd:PRK10790 223 QarfgermgeASRSHY---MARMQTLRLDGFLLRPLL-----SL-FSALILC----GLLM------LFGF----SAS--G 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1044 AQSAGSVFSFAPDMGKATE-----------------AARDLKELFDRkpTVDTWSNEGDLIKQvdGTIEFRDVHFRYptR 1106
Cdd:PRK10790 278 TIEVGVLYAFISYLGRLNEplielttqqsmlqqavvAGERVFELMDG--PRQQYGNDDRPLQS--GRIDIDNVSFAY--R 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1107 PEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTV 1186
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTF 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 RENIILGanNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDS 1266
Cdd:PRK10790 432 LANVTLG--RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1267 ESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELVNLQ 1332
Cdd:PRK10790 510 GTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1092-1313 |
1.19e-66 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 224.39 E-value: 1.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1092 GTIEFRDVHFRYPTRpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSF 1171
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1172 IALVSQEPTLYQGTVRENIILGANnDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRD 1251
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAP-LADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1252 PKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQG 1313
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
852-1334 |
2.57e-65 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 244.17 E-value: 2.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 852 FRSFLRQDVEFfdRDENSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIPILLGCG 931
Cdd:PTZ00265 137 LKSVFYQDGQF--HDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 932 FYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLA 1011
Cdd:PTZ00265 215 VICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILAS 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1012 FALGFWYGGTLI--------AKHEYDMFTFFIVFSSVIFGAQSAGSVFSFAPDMGKATEAARDLKELFDRKPTVDTwSNE 1083
Cdd:PTZ00265 295 YAFGFWYGTRIIisdlsnqqPNNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN-NDD 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1084 GDLIKQVDgTIEFRDVHFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFI-DGREISS 1162
Cdd:PTZ00265 374 GKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKD 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1163 LNVNEYRSFIALVSQEPTLYQGTVRENI-------------------------------------ILGANNDVT------ 1199
Cdd:PTZ00265 453 INLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyynedgndsqenknkrnscrakCAGDLNDMSnttdsn 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1200 -------------DEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDS 1266
Cdd:PTZ00265 533 eliemrknyqtikDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1267 ESEHVVQAALD--KAAKGRTTIAVAHRLSTIQKADIIYVFDQ-------------------------------------- 1306
Cdd:PTZ00265 613 KSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNrergstvdvdiigedptkdnkennnknnkddnnnnnnn 692
|
570 580 590
....*....|....*....|....*....|....*...
gi 164423939 1307 ---------GRIVEQGTHSELMK-KNGRYAELVNLQSL 1334
Cdd:PTZ00265 693 nnnkinnagSYIIEQGTHDALMKnKNGIYYTMINNQKV 730
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
993-1328 |
2.80e-65 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 232.81 E-value: 2.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 993 SVLK----SS--LLFAASNSLMFLAFALGFWYGGTLIAKHeYDM-FTFFIVFSSVIFGAQsagsvFsFAP--DMG----- 1058
Cdd:PRK11174 241 EVLRmaflSSavLEFFASISIALVAVYFGFSYLGELNFGH-YGTgVTLFAGFFVLILAPE-----F-YQPlrDLGtfyha 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1059 --KATEAARDLKELFDrKPTVDTWSNEGDLIKQVDGTIEFRDVHFrypTRPEQPVLRG-LNLSIQPGQYVALVGASGCGK 1135
Cdd:PRK11174 314 kaQAVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIEAEDLEI---LSPDGKTLAGpLNFTLPAGQRIALVGPSGAGK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1136 STTIALLERFYdPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGaNNDVTDEQIKFACQEANIYDF 1215
Cdd:PRK11174 390 TSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG-NPDASDEQLQQALENAWVSEF 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1216 IMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTI 1295
Cdd:PRK11174 468 LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDL 547
|
330 340 350
....*....|....*....|....*....|...
gi 164423939 1296 QKADIIYVFDQGRIVEQGTHSELMKKNGRYAEL 1328
Cdd:PRK11174 548 AQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
225-683 |
1.84e-64 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 230.55 E-value: 1.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 225 QALATFIAAFVIGFVSF---WKLTLILLSTVVALTLVmgggSQFIIKFSKQNIAAYAEG-GSVADEVISSVRNAIAFGTQ 300
Cdd:TIGR01192 136 QHLATFVALFLLIPTAFamdWRLSIVLMVLGILYILI----AKLVMQRTKNGQAAVEHHyHNVFKHVSDSISNVSVVHSY 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 301 DRLA------RRYDAHLTRAEH---FGFRLKGSIGVMVA--GMMTVLYLnyglafwqGSRFLLSGDTELRKILTVM--MS 367
Cdd:TIGR01192 212 NRIEaetsalKQFTNNLLSAQYpvlDWWALASGLNRMAStiSMMCILVI--------GTVLVIKGELSVGEVIAFIgfAN 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 368 VMIGAFNlgniapNLQAFVT-ALGAAAKIYNTIDRESPIDSSSEEG--GKLENVVGTIRLENIKHIYPSRPDVVvmEDVS 444
Cdd:TIGR01192 284 LLIGRLD------QMSGFITqIFEARAKLEDFFDLEDSVFQREEPAdaPELPNVKGAVEFRHITFEFANSSQGV--FDVS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 445 LVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGLIG 524
Cdd:TIGR01192 356 FEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREG 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 525 TkweseseeqQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKS 604
Cdd:TIGR01192 436 A---------TDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVET 506
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 605 EGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLVTAQAIAAVNEMTAEEEAA 683
Cdd:TIGR01192 507 EARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRSGLLTNQPATKPLRKA 585
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
198-1323 |
2.77e-64 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 241.03 E-value: 2.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 198 AGEVTTRITADTNLIQEgISEKVGLTLQALATFIAAFVI-----GFVS-FWKLTLILLSTVVALTLvmgggsQFIIKFSK 271
Cdd:PLN03232 397 SGKVTNMITTDANALQQ-IAEQLHGLWSAPFRIIVSMVLlyqqlGVASlFGSLILFLLIPLQTLIV------RKMRKLTK 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 272 QNIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAhlTRAEHFGFRLKGSI-----GVMVAGMMTVLYLnygLAFwq 346
Cdd:PLN03232 470 EGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQG--IRNEELSWFRKAQLlsafnSFILNSIPVVVTL---VSF-- 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 347 GSRFLLSGDTELRKILTVMMSVMIGAFNLgNIAPNL-QAFVTALGAAAKIYNTIDRESPIDSSSEeggKLENVVGTIRLE 425
Cdd:PLN03232 543 GVFVLLGGDLTPARAFTSLSLFAVLRSPL-NMLPNLlSQVVNANVSLQRIEELLLSEERILAQNP---PLQPGAPAISIK 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 426 NIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKvyldDVDIstlnvrwlRQQIALVSQ 505
Cdd:PLN03232 619 NGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS----SVVI--------RGSVAYVPQ 686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 506 EPTLFACTIYDNIrhgLIGTKweseseeqqreriYEAARKANAHDfITSLPEGYE-------TNVGERGFLLSGGQKQRI 578
Cdd:PLN03232 687 VSWIFNATVRENI---LFGSD-------------FESERYWRAID-VTALQHDLDllpgrdlTEIGERGVNISGGQKQRV 749
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 579 AIARAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAK 657
Cdd:PLN03232 750 SMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 658 RGAYYKLVtaqaiaavnemtaEEEAALDQQEEaalIRKATRNSQKEGGAAgyvedpEDNIAEkldRSKSQQSVSSVAIAA 737
Cdd:PLN03232 830 GSLFKKLM-------------ENAGKMDATQE---VNTNDENILKLGPTV------TIDVSE---RNLGSTKQGKRGRSV 884
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 738 RKKEEPKEYGL--WTLIkliASFNKKEWHMMLVGIFFsaICgagnptqavffaKLISSLSRpiVNEEIRASIKSDAS--- 812
Cdd:PLN03232 885 LVKQEERETGIisWNVL---MRYNKAVGGLWVVMILL--VC------------YLTTEVLR--VSSSTWLSIWTDQStpk 945
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 813 -----FWCLMYLMLALVQ-CLAFSVQGWLFAKcSERLIHRVRDMAFRSFLRQDVEFFDrdENSAGALTSFLSTET----T 882
Cdd:PLN03232 946 syspgFYIVVYALLGFGQvAVTFTNSFWLISS-SLHAAKRLHDAMLNSILRAPMLFFH--TNPTGRVINRFSKDIgdidR 1022
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 883 HVAGLSGVTLGTIIMVLTTLIAACTVALALGWklalvciATIPILLGcgFYRFWMiaHYQ------RRAKSAyAGSASYA 956
Cdd:PLN03232 1023 NVANLMNMFMNQLWQLLSTFALIGTVSTISLW-------AIMPLLIL--FYAAYL--YYQstsrevRRLDSV-TRSPIYA 1090
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 957 --SEAITAMRTVASltreqdvlqhYK--DSLAKQQHASLISVLKSSLLFAASNSLMFLAFALgfwYGGTLIakheydmft 1032
Cdd:PLN03232 1091 qfGEALNGLSSIRA----------YKayDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLET---LGGVMI--------- 1148
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1033 fFIVFSSVIFGAQSAGSVFSFAPDMG------------------KATEAARDLKELFDRKPTVDTWSNEGDLIKQ----- 1089
Cdd:PLN03232 1149 -WLTATFAVLRNGNAENQAGFASTMGlllsytlnittllsgvlrQASKAENSLNSVERVGNYIDLPSEATAIIENnrpvs 1227
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1090 ---VDGTIEFRDVHFRYptRPE-QPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNV 1165
Cdd:PLN03232 1228 gwpSRGSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGL 1305
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1166 NEYRSFIALVSQEPTLYQGTVRENIilGANNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIA 1245
Cdd:PLN03232 1306 TDLRRVLSIIPQSPVLFSGTVRFNI--DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLA 1383
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1246 RALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNG 1323
Cdd:PLN03232 1384 RALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
817-1335 |
2.79e-64 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 229.60 E-value: 2.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 817 MYLMLALVQCLAFSVQGWLFAkCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHV---AGLSGVTL- 892
Cdd:PRK10789 42 MVLIAVVVYLLRYVWRVLLFG-ASYQLAVELREDFYRQLSRQHPEFYLR--HRTGDLMARATNDVDRVvfaAGEGVLTLv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 893 GTIIMVLTTLIAACTvalALGWKLALVCIATIPILLgcgfyrfWMIAHY----QRRAKSAYAGSAS---YASEAITAMRT 965
Cdd:PRK10789 119 DSLVMGCAVLIVMST---QISWQLTLLALLPMPVMA-------IMIKRYgdqlHERFKLAQAAFSSlndRTQESLTSIRM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 966 VASLTREQDVLQHY----KDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYggtliakheydmftffivfssVI 1041
Cdd:PRK10789 189 IKAFGLEDRQSALFaadaEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGGGSWM---------------------VV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1042 FGAQSAGSVFSFAPDMG-----------------KATEAARDLKELFDRKPTVdtwsNEGDL-IKQVDGTIEFRDVHFRY 1103
Cdd:PRK10789 248 NGSLTLGQLTSFVMYLGlmiwpmlalawmfniveRGSAAYSRIRAMLAEAPVV----KDGSEpVPEGRGELDVNIRQFTY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1104 PTRpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQ 1183
Cdd:PRK10789 324 PQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1184 GTVRENIILGaNNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSA 1263
Cdd:PRK10789 403 DTVANNIALG-RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1264 LDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELVNLQSLE 1335
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLE 553
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
142-692 |
8.34e-64 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 228.83 E-value: 8.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 142 ARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVG 221
Cdd:PRK10790 65 AGLAAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 222 LTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQF---IIKFSKQNIAAYAEGgsvADEVIS--SV----R 292
Cdd:PRK10790 145 TVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYstpIVRRVRAYLADINDG---FNEVINgmSViqqfR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 293 NAIAFGT-------QDRLAR----RYDAHLTRA--------------EHFGFRLKGSIGVmvagmmTVLY--LNYglafw 345
Cdd:PRK10790 222 QQARFGErmgeasrSHYMARmqtlRLDGFLLRPllslfsalilcgllMLFGFSASGTIEV------GVLYafISY----- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 346 qgsrflLSGDTELRKILTVMMSVMigafnlgniapnLQAFVtalgAAAKIYNTIDResPIDSSSEEGGKLENvvGTIRLE 425
Cdd:PRK10790 291 ------LGRLNEPLIELTTQQSML------------QQAVV----AGERVFELMDG--PRQQYGNDDRPLQS--GRIDID 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 426 NIKHIYpsRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQ 505
Cdd:PRK10790 345 NVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQ 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 506 EPTLFACTIYDNIRHGligtkwesesEEQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIV 585
Cdd:PRK10790 423 DPVVLADTFLANVTLG----------RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 586 SDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLV 665
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY 572
|
570 580
....*....|....*....|....*..
gi 164423939 666 TAQaiaavneMTAEEEAALDQQEEAAL 692
Cdd:PRK10790 573 QLQ-------LAGEELAASVREEESLS 592
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1060-1303 |
1.36e-62 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 223.32 E-value: 1.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1060 ATEAARDLKELFDRKPTVDtwSNEGDLIKQVDGTIEFRDVHFRYPTRPeqPVLRGLNLSIQPGQYVALVGASGCGKSTTI 1139
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRPL--AGKAPVTAAPASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1140 ALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGANnDVTDEQIKFACQEANIYDFIMSL 1219
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARP-DASDAEIREALERAGLDEFVAAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1220 PDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKAD 1299
Cdd:TIGR02857 445 PQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALAD 524
|
....
gi 164423939 1300 IIYV 1303
Cdd:TIGR02857 525 RIVV 528
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
186-668 |
2.09e-61 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 224.07 E-value: 2.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 186 MRQNIGFFDKLGAGEVTTRITAdTNLIQEGISekvGLTL-QALATFIAAFVIG--FVSFWKLTLILLSTVVALTLVMGGG 262
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASRAMG-ISQIRRILS---GSTLtTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLVL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 263 SQFIIKFSKQNIAAYAEGGSVADEVISSV---RNAiafGTQDRLARRYDAHLTRAEHFGFRlKGSIGVMVAGMMTVL-YL 338
Cdd:TIGR03797 296 GLLQVRKERRLLELSGKISGLTVQLINGIsklRVA---GAENRAFARWAKLFSRQRKLELS-AQRIENLLTVFNAVLpVL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 339 NYGLAFWQGSRFLLSGDTELRKILtvmmsvmigAFNlgniapnlQAFVTALGAAAKIYNTI----------DRESPI--- 405
Cdd:TIGR03797 372 TSAALFAAAISLLGGAGLSLGSFL---------AFN--------TAFGSFSGAVTQLSNTLisilaviplwERAKPIlea 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 406 ----DSSSEEGGKLEnvvGTIRLENIKHIYpsRPD-VVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGK 480
Cdd:TIGR03797 435 lpevDEAKTDPGKLS---GAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGS 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 481 VYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGLIGTkweseseeqqRERIYEAARKANAHDFITSLPEGYE 560
Cdd:TIGR03797 510 VFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLT----------LDEAWEAARMAGLAEDIRAMPMGMH 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 561 TNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEvaAEGRTTITIAHRLSTIKDAHNIVVM 640
Cdd:TIGR03797 580 TVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLE--RLKVTRIVIAHRLSTIRNADRIYVL 657
|
490 500
....*....|....*....|....*...
gi 164423939 641 AQGRIVEQGTHAELLAKRGAYYKLVTAQ 668
Cdd:TIGR03797 658 DAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
816-1292 |
8.17e-60 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 215.30 E-value: 8.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 816 LMYLMLALVQCLAFSVQGWLFAKCsERLI-HrvrDMAFRSFLRQDVEFFDRDENSAGALTS------FLSTETTHVAGLS 888
Cdd:TIGR02868 49 VLYLSVAAVAVRAFGIGRAVFRYL-ERLVgH---DAALRSLGALRVRVYERLARQALAGRRrlrrgdLLGRLGADVDALQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 889 GVTLGTIIMVLTTLIAACTVALALGW-----KLALVCIATIPILLGCGFYRFWMIAHYQRRAksayAGSASYASEAITAM 963
Cdd:TIGR02868 125 DLYVRVIVPAGVALVVGAAAVAAIAVlsvpaALILAAGLLLAGFVAPLVSLRAARAAEQALA----RLRGELAAQLTDAL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 964 RTVASLT---REQDVLQHYKDSlAKQQHASLISVLKSSLLFAASNSL-MFLAFALGFWYGGTLIAKHEYDMfTFFIVFSS 1039
Cdd:TIGR02868 201 DGAAELVasgALPAALAQVEEA-DRELTRAERRAAAATALGAALTLLaAGLAVLGALWAGGPAVADGRLAP-VTLAVLVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1040 VIFGAQSAGSVFSFAPD-MGKATEAARDLKELFDRKPTVDTWSNEGDLIKQVDG-TIEFRDVHFRYPtrPEQPVLRGLNL 1117
Cdd:TIGR02868 279 LPLAAFEAFAALPAAAQqLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYP--GAPPVLDGVSL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1118 SIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIILGANnD 1197
Cdd:TIGR02868 357 DLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARP-D 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1198 VTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALD 1277
Cdd:TIGR02868 436 ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL 515
|
490
....*....|....*
gi 164423939 1278 KAAKGRTTIAVAHRL 1292
Cdd:TIGR02868 516 AALSGRTVVLITHHL 530
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
440-1323 |
1.85e-59 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 225.77 E-value: 1.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 440 MEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLddvdistlnvrwLRQQIALVSQEPTLFACTIYDNIr 519
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNI- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 520 hgLIGTKWESESeeqqreriYEAARKANA--HDfITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEAT 597
Cdd:PLN03130 700 --LFGSPFDPER--------YERAIDVTAlqHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 598 SALDTK-SEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLVtaqaiaavnem 676
Cdd:PLN03130 769 SALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLM----------- 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 677 taEEEAALDQQEEAALIRKATRNSQKeggaagyveDPEDNIAEKLDRSKSQQSVSSVAIAARKKEEPKEYGLWTLiKLIA 756
Cdd:PLN03130 838 --ENAGKMEEYVEENGEEEDDQTSSK---------PVANGNANNLKKDSSSKKKSKEGKSVLIKQEERETGVVSW-KVLE 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 757 SFNKKEWHMMLVGIFFsaICGAGNPTQAVFFAKLISSLSRPIVNEEIRASiksdasFWCLMYLMLALVQ-CLAFSVQGWL 835
Cdd:PLN03130 906 RYKNALGGAWVVMILF--LCYVLTEVFRVSSSTWLSEWTDQGTPKTHGPL------FYNLIYALLSFGQvLVTLLNSYWL 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 836 FAKcSERLIHRVRDMAFRSFLRQDVEFFDrdENSAGALTSFLSTETT----HVAGLSGVTLGTIIMVLTTLIAACTVALA 911
Cdd:PLN03130 978 IMS-SLYAAKRLHDAMLGSILRAPMSFFH--TNPLGRIINRFAKDLGdidrNVAVFVNMFLGQIFQLLSTFVLIGIVSTI 1054
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 912 LGWklalvciATIPILLGcgFYRFWMiaHYQRRAKS-----AYAGSASYA--SEAITAMRTVASltreqdvlqhYK--DS 982
Cdd:PLN03130 1055 SLW-------AIMPLLVL--FYGAYL--YYQSTAREvkrldSITRSPVYAqfGEALNGLSTIRA----------YKayDR 1113
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 983 LAKQQHASLISVLKSSLLFAASNSlmFLAFALGFwYGGTLIakheydmftfFIVFSSVIFGAQSAGSVFSFAPDMGKATE 1062
Cdd:PLN03130 1114 MAEINGRSMDNNIRFTLVNMSSNR--WLAIRLET-LGGLMI----------WLTASFAVMQNGRAENQAAFASTMGLLLS 1180
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1063 AARDLKEL--------------FDRKPTVDTW---SNEGDLIKQVD---------GTIEFRDVHFRYptRPE-QPVLRGL 1115
Cdd:PLN03130 1181 YALNITSLltavlrlaslaensLNAVERVGTYidlPSEAPLVIENNrpppgwpssGSIKFEDVVLRY--RPElPPVLHGL 1258
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1116 NLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENiiLGAN 1195
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN--LDPF 1336
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1196 NDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAA 1275
Cdd:PLN03130 1337 NEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKT 1416
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 164423939 1276 LDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNG 1323
Cdd:PLN03130 1417 IREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
130-690 |
8.78e-59 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 213.42 E-value: 8.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 130 GVTTYDDFTDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADT 209
Cdd:PRK10789 24 GVTEQHMTTGQILMWIGTMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 210 NLIQEGISEKVgLTL-QALATFIAAFVIGFVSF-WKLTLI-LLSTVVALTLVMGGGSQFIIKFsKQNIAAYAEGGSVADE 286
Cdd:PRK10789 104 DRVVFAAGEGV-LTLvDSLVMGCAVLIVMSTQIsWQLTLLaLLPMPVMAIMIKRYGDQLHERF-KLAQAAFSSLNDRTQE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 287 VISSVRNAIAFGTQDRLARRYDA----------HLTRAEHfgfRLKGSIGVMVAgmMTVLylnygLAFWQGSRFllsgdt 356
Cdd:PRK10789 182 SLTSIRMIKAFGLEDRQSALFAAdaedtgkknmRVARIDA---RFDPTIYIAIG--MANL-----LAIGGGSWM------ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 357 elrkiltvmmsVMIGAFNLGNiapnLQAFVTALG-------AAAKIYNTIDRESP----IDSSSEEGGKLENvvGTIRLE 425
Cdd:PRK10789 246 -----------VVNGSLTLGQ----LTSFVMYLGlmiwpmlALAWMFNIVERGSAaysrIRAMLAEAPVVKD--GSEPVP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 426 --------NIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLR 497
Cdd:PRK10789 309 egrgeldvNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 QQIALVSQEPTLFACTIYDNIRHGligtkweseSEEQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQR 577
Cdd:PRK10789 389 SRLAVVSQTPFLFSDTVANNIALG---------RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQR 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 578 IAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAK 657
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
570 580 590
....*....|....*....|....*....|...
gi 164423939 658 RGAYYKLVTAQAIaavnemtaeeEAALDQQEEA 690
Cdd:PRK10789 540 SGWYRDMYRYQQL----------EAALDDAPEI 562
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
420-649 |
3.40e-58 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 200.12 E-value: 3.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 420 GTIRLENIKHIYPSRPDVVVmEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQ 499
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEPTLFACTIYDNIRHGligtkweseSEEQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIA 579
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLG---------APLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 580 IARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQG 649
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
144-667 |
5.56e-58 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 214.22 E-value: 5.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 144 LVLYFVYLAIGEFVTMYITTVgfiySGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITaDTNLIQEGI-SEKVGL 222
Cdd:TIGR01193 202 LIIAYIIQQILSYIQIFLLNV----LGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALaSTILSL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 223 TLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMgggsQFIIKFSKQNIAAYAEGGSVADEVISSVrNAI----AFG 298
Cdd:TIGR01193 277 FLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIII----LFKRTFNKLNHDAMQANAVLNSSIIEDL-NGIetikSLT 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 299 TQDRLARRYDAHLTRAEHFGFRL-KGSIGVMVAGMMTVLYLNYgLAFWQGSRFLLSGDTELRKILTvmMSVMIGAFN--L 375
Cdd:TIGR01193 352 SEAERYSKIDSEFGDYLNKSFKYqKADQGQQAIKAVTKLILNV-VILWTGAYLVMRGKLTLGQLIT--FNALLSYFLtpL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 376 GNIApNLQafvTALGAAAKIYNTIDRESPIDSSSEEGGK---LENVVGTIRLENIKHIYPSRPDVvvMEDVSLVIPAGKT 452
Cdd:TIGR01193 429 ENII-NLQ---PKLQAARVANNRLNEVYLVDSEFINKKKrteLNNLNGDIVINDVSYSYGYGSNI--LSDISLTIKMNSK 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 453 TALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIrhgLIGTKwesesE 532
Cdd:TIGR01193 503 TTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENL---LLGAK-----E 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 533 EQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL 612
Cdd:TIGR01193 575 NVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL 654
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 613 eVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLVTA 667
Cdd:TIGR01193 655 -LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
911-1321 |
2.18e-57 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 209.22 E-value: 2.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 911 ALGWkLALVCIAtipILLGCGFYRFWMIAHYQRRAKSAYAGSASYA------SEAITAMRTVASLTREQdvLQHYKDSLA 984
Cdd:COG4618 156 LLGL-LALVGAL---VLVALALLNERLTRKPLKEANEAAIRANAFAeaalrnAEVIEAMGMLPALRRRW--QRANARALA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 985 KQQHASLISvlksSLLFAASNSL-MFL---AFALGFWY-------GGTLIAkheydmftffivfSSVIFG-A-----QSA 1047
Cdd:COG4618 230 LQARASDRA----GGFSALSKFLrLLLqsaVLGLGAYLviqgeitPGAMIA-------------ASILMGrAlapieQAI 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1048 GSVFSFApdmgKATEAARDLKELFDRKPTVDtwsnEGDLIKQVDGTIEFRDVHFRYPTRpEQPVLRGLNLSIQPGQYVAL 1127
Cdd:COG4618 293 GGWKQFV----SARQAYRRLNELLAAVPAEP----ERMPLPRPKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1128 VGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGTVRENIilgAN-NDVTDEQIKFA 1206
Cdd:COG4618 364 IGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI---ARfGDADPEKVVAA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1207 CQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKA-AKGRTT 1285
Cdd:COG4618 441 AKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATV 520
|
410 420 430
....*....|....*....|....*....|....*.
gi 164423939 1286 IAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKK 1321
Cdd:COG4618 521 VVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
871-1330 |
2.99e-57 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 211.91 E-value: 2.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 871 GALTSFLSTETTHVAGLSGVTLgTIIMVLTTLIAACTVALALGWKLALVCIATIP--ILLGCGFYR-FWMIAHYQRRAKS 947
Cdd:TIGR01193 253 GEIVSRFTDASSIIDALASTIL-SLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPvyAVIIILFKRtFNKLNHDAMQANA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 948 AYAGSASyasEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHE 1027
Cdd:TIGR01193 332 VLNSSII---EDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGK 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1028 YDMFTFfIVFSSVI-FGAQSAGSVFSFAPDMGKATEAARDLKELFdrkpTVDTWSNEG---DLIKQVDGTIEFRDVHFRY 1103
Cdd:TIGR01193 409 LTLGQL-ITFNALLsYFLTPLENIINLQPKLQAARVANNRLNEVY----LVDSEFINKkkrTELNNLNGDIVINDVSYSY 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1104 PTrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQ 1183
Cdd:TIGR01193 484 GY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFS 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1184 GTVRENIILGANNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSA 1263
Cdd:TIGR01193 562 GSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSN 641
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1264 LDSESEHVVQAALDKaAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELVN 1330
Cdd:TIGR01193 642 LDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
387-640 |
1.32e-56 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 205.98 E-value: 1.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 387 TALGAAAKIYNTIDRESPIDSSSEEggKLENVVGTIRLENIKHIYPSRPDVVvmEDVSLVIPAGKTTALVGASGSGKSTI 466
Cdd:TIGR02857 289 DGVAAAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGPSGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 467 VGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGLIGTKweseseeqqRERIYEAARKA 546
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDAS---------DAEIREALERA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 547 NAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAH 626
Cdd:TIGR02857 436 GLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
250
....*....|....
gi 164423939 627 RLSTIKDAHNIVVM 640
Cdd:TIGR02857 516 RLALAALADRIVVL 529
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
111-405 |
2.12e-56 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 198.44 E-value: 2.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 111 PLMTVIFGNLQGTFQNyfagvTTYDDFTDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNI 190
Cdd:cd18578 26 PVFAILFSKLISVFSL-----PDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 191 GFFDKLG--AGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIK 268
Cdd:cd18578 101 AWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 269 FSKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAHLTRAEHFGFR--LKGSIGVMVAGMMTvlYLNYGLAFWQ 346
Cdd:cd18578 181 FEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRraLISGLGFGLSQSLT--FFAYALAFWY 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 347 GSRFLLSGDTELRKILTVMMSVMIGAFNLGNIAPNLQAFVTALGAAAKIYNTIDRESPI 405
Cdd:cd18578 259 GGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
438-1330 |
2.18e-56 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 215.80 E-value: 2.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 438 VVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVylddvdistlnvrWLRQQIALVSQEPTLFACTIYDN 517
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 518 IrhgligtkweseseeqqreRIYEAARKANAHDFI---------TSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDP 588
Cdd:PTZ00243 741 I-------------------LFFDEEDAARLADAVrvsqleadlAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANR 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 589 KILLLDEATSALDTK-SEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLakRGAYYKLVTA 667
Cdd:PTZ00243 802 DVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM--RTSLYATLAA 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 668 QAIAAVNEMTAEEEAALDQQEEAalirkatrnsqkEGGAagyvEDPEDNIAEKLDRSKSQQSVSSVAIAAR-KKEEPKEY 746
Cdd:PTZ00243 880 ELKENKDSKEGDADAEVAEVDAA------------PGGA----VDHEPPVAKQEGNAEGGDGAALDAAAGRlMTREEKAS 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 747 GL--W-TLIKLIASFNKKEWHMMLVGIFFSaicgagnpTQAVFFAKLISsLSRPIVNEEirasiKSDASFWCLMYLMLAL 823
Cdd:PTZ00243 944 GSvpWsTYVAYLRFCGGLHAAGFVLATFAV--------TELVTVSSGVW-LSMWSTRSF-----KLSAATYLYVYLGIVL 1009
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 824 VQCLAFSVQgwlFAKCSERLIHRVRDM---AFRSFLRQDVEFFDRDensagALTSFLSTETTHVAGLSGVTLGTIIMVLT 900
Cdd:PTZ00243 1010 LGTFSVPLR---FFLSYEAMRRGSRNMhrdLLRSVSRGTMSFFDTT-----PLGRILNRFSRDIDILDNTLPMSYLYLLQ 1081
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 901 TLIAACTVALALGWKLALVCIATIPillgCGFYRFWMIAHYQ------RRAKS-AYAGSASYASEAITAMRTVASLTREQ 973
Cdd:PTZ00243 1082 CLFSICSSILVTSASQPFVLVALVP----CGYLYYRLMQFYNsanreiRRIKSvAKSPVFTLLEEALQGSATITAYGKAH 1157
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 974 DVLQhykDSLAKqqhasLISVLKSSLLFAASN-----------SLMFLAFALGFWYGGTLIAKHEydmfTFFIVFSSVIF 1042
Cdd:PTZ00243 1158 LVMQ---EALRR-----LDVVYSCSYLENVANrwlgvrveflsNIVVTVIALIGVIGTMLRATSQ----EIGLVSLSLTM 1225
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1043 GAQSAGS-------VFSFAPDMGKA-----------TEAARDLKELfdrkptVDTWSNEGDLIKQVDGTI---------- 1094
Cdd:PTZ00243 1226 AMQTTATlnwlvrqVATVEADMNSVerllyytdevpHEDMPELDEE------VDALERRTGMAADVTGTVviepasptsa 1299
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1095 ----------EFRDVHFRYptRPEQP-VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSL 1163
Cdd:PTZ00243 1300 aphpvqagslVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY 1377
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1164 NVNEYRSFIALVSQEPTLYQGTVRENI--ILGAnndvTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQR 1241
Cdd:PTZ00243 1378 GLRELRRQFSMIPQDPVLFDGTVRQNVdpFLEA----SSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQL 1453
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1242 IAIARALI-RDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSEL-M 1319
Cdd:PTZ00243 1454 MCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvM 1533
|
970
....*....|.
gi 164423939 1320 KKNGRYAELVN 1330
Cdd:PTZ00243 1534 NRQSIFHSMVE 1544
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
84-663 |
7.77e-56 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 213.74 E-value: 7.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 84 LYR--YATRNDLLIIAVSaicaiaagaalplmTVIFGNLQGTFQNYFAG-VTTYDDFTDELA---RLVLYFVYLAIGEFV 157
Cdd:PTZ00265 816 VYReiFSYKKDVTIIALS--------------ILVAGGLYPVFALLYAKyVSTLFDFANLEAnsnKYSLYILVIAIAMFI 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 158 TMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFD--KLGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFV 235
Cdd:PTZ00265 882 SETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMV 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 236 IGF------VSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYA---------EGGSVADEVISSVRNAIAFGTQ 300
Cdd:PTZ00265 962 MSFyfcpivAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVFAynsddeifkDPSFLIQEAFYNMNTVIIYGLE 1041
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 301 DRLARRYDAHLTRAEHfGFRLKGSIGVMVAGMM--TVLYLNyGLAFWQGSRFLLSGDTELRKILTVMMSVMIGAFNLGNI 378
Cdd:PTZ00265 1042 DYFCNLIEKAIDYSNK-GQKRKTLVNSMLWGFSqsAQLFIN-SFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKL 1119
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 379 APNLQAFVTALGAAAKIYNTIDRESPIDSSSEEGGKLEN---VVGTIRLENIKHIYPSRPDVVVMEDVSLVIPAGKTTAL 455
Cdd:PTZ00265 1120 MSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAI 1199
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 456 VGASGSGKSTIVGLVERFY----------------------------------KPI--------------------EGKV 481
Cdd:PTZ00265 1200 VGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneqdyqgdeeqnvgmKNVnefsltkeggsgedstvfknSGKI 1279
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 482 YLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGligtkweseSEEQQRERIYEAARKANAHDFITSLPEGYET 561
Cdd:PTZ00265 1280 LLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG---------KEDATREDVKRACKFAAIDEFIESLPNKYDT 1350
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 562 NVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEG-RTTITIAHRLSTIKDAHNIVV 639
Cdd:PTZ00265 1351 NVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvDIKDKAdKTIITIAHRIASIKRSDKIVV 1430
|
650 660
....*....|....*....|....*....
gi 164423939 640 MAQ----GRIVE-QGTHAELLAKRGAYYK 663
Cdd:PTZ00265 1431 FNNpdrtGSFVQaHGTHEELLSVQDGVYK 1459
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
420-650 |
8.21e-55 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 190.40 E-value: 8.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 420 GTIRLENIKHIYpsRPD-VVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQ 498
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 499 QIALVSQEPTLFACTIYDNI----RHgligtkweseseeqQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQ 574
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdpfgEY--------------SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGT 650
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
420-657 |
1.08e-54 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 201.13 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 420 GTIRLENIKHIYPSRpDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLNVRW 495
Cdd:COG4618 329 GRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTlarlLVGVW----PPTAGSVRLDGADLSQWDREE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 LRQQIALVSQEPTLFACTIYDNI-RHGligtkweseseEQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQ 574
Cdd:COG4618 404 LGRHIGYLPQDVELFDGTIAENIaRFG-----------DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQ 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAE 653
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIrALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDE 552
|
....
gi 164423939 654 LLAK 657
Cdd:COG4618 553 VLAR 556
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
766-1044 |
2.87e-54 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 190.93 E-value: 2.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 766 MLVGIFFSAICGAGNPTQAVFFAKLISSLSrpivneEIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKCSERLIH 845
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLL------PDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 846 RVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIP 925
Cdd:pfam00664 75 RLRRKLFKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 926 ILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASN 1005
Cdd:pfam00664 153 LYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 164423939 1006 SLMFLAFALGFWYGGTLIAKHEYDM--FTFFIVFSSVIFGA 1044
Cdd:pfam00664 233 FIGYLSYALALWFGAYLVISGELSVgdLVAFLSLFAQLFGP 273
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
175-628 |
5.66e-52 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 192.19 E-value: 5.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 175 GKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEgisekvgLTLQALATFIAAFVIGFVS-------FWKLTLI 247
Cdd:TIGR02868 86 GALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQD-------LYVRVIVPAGVALVVGAAAvaaiavlSVPAALI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 248 LLSTVVALTLVMGGGSQFIIKFSKQNIAAYAegGSVADEVISSVRNA---IAFGTQDRLARRY---DAHLTRAEHFGFRL 321
Cdd:TIGR02868 159 LAAGLLLAGFVAPLVSLRAARAAEQALARLR--GELAAQLTDALDGAaelVASGALPAALAQVeeaDRELTRAERRAAAA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 322 KG---SIGVMVAGMMTVLYLnyglafWQGSRFLLSGDTELRkILTVMMSVMIGAFN-LGNIAPNLQAFVTALGAAAKIYN 397
Cdd:TIGR02868 237 TAlgaALTLLAAGLAVLGAL------WAGGPAVADGRLAPV-TLAVLVLLPLAAFEaFAALPAAAQQLTRVRAAAERIVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 398 TIDRESPI-DSSSEEGGKLENVVGTIRLENIKHIYPsrPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKP 476
Cdd:TIGR02868 310 VLDAAGPVaEGSAPAAGAVGLGKPTLELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 477 IEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGligtkweseSEEQQRERIYEAARKANAHDFITSLP 556
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA---------RPDATDEELWAALERVGLADWLRALP 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 557 EGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRL 628
Cdd:TIGR02868 459 DGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
110-395 |
1.50e-51 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 184.40 E-value: 1.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 110 LPLMTVIFGNLQGTFQNYFAGVTT------------YDDFTDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKI 177
Cdd:cd18558 15 LPAFMVIFGDMTDSFTNGGMTNITgnssglnssagpFEKLEEEMTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 178 REHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTL 257
Cdd:cd18558 95 RYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 258 VMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLY 337
Cdd:cd18558 175 SAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIY 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 338 LNYGLAFWQGSRFLLSGDTELRKILTVMMSVMIGAFNLGNIAPNLQAFVTALGAAAKI 395
Cdd:cd18558 255 ASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
443-668 |
2.93e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 191.60 E-value: 2.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 443 VSLVIPAGKTTALVGASGSGKSTIVGLVERFYkPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGl 522
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 523 igtkweseSEEQQRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDT 602
Cdd:PRK11174 447 --------NPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 603 KSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLVTAQ 668
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
950-1321 |
2.48e-49 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 184.86 E-value: 2.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 950 AGSASYASEAITAMRTVASLTREQDVLqHYKdSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWyggtLIAKHEyd 1029
Cdd:TIGR01842 183 ADSALRNAEVIEAMGMMGNLTKRWGRF-HSK-YLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAY----LAIDGE-- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1030 MFTFFIVFSSVIFGAqsagsvfSFAP---------DMGKATEAARDLKELFDRKPtvdtwSNEGDL-IKQVDGTIEFRDV 1099
Cdd:TIGR01842 255 ITPGMMIAGSILVGR-------ALAPidgaiggwkQFSGARQAYKRLNELLANYP-----SRDPAMpLPEPEGHLSVENV 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1100 HFRyPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEP 1179
Cdd:TIGR01842 323 TIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDV 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1180 TLYQGTVRENIILGANNdVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDE 1259
Cdd:TIGR01842 402 ELFPGTVAENIARFGEN-ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDE 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1260 ATSALDSESEHVVQAALDKA-AKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKK 1321
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1094-1309 |
4.01e-49 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 172.02 E-value: 4.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQGTVRENIilganndvtdeqikfacqeaniydfimslpdgmntlvgskgalLSGGQKQRIAIARALIRDPK 1253
Cdd:cd03246 80 YLPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1254 ILLLDEATSALDSESEHVVQAALDKA-AKGRTTIAVAHRLSTIQKADIIYVFDQGRI 1309
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1094-1309 |
1.19e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 172.31 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:COG4619 1 LELEGLSFRVG---GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQGTVRENIILGANNdvtdEQIKFacQEANIYDFIMSL---PDGMNTLVGSkgalLSGGQKQRIAIARALIR 1250
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQL----RERKF--DRERALELLERLglpPDILDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1251 DPKILLLDEATSALDSESEHVVQAALDK--AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRI 1309
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
391-664 |
1.51e-48 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 183.10 E-value: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 391 AAAKIYNTIDRESPIDSSSEEGGKLENvvGTIRLENIKHIYPSRPDVVvMEDVSLVIPAGKTTALVGASGSGKSTIVGLV 470
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQPV-LKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 471 ERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHgligtkweseseeqqreriyeAARKANAHD 550
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL---------------------AAPNASDEA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 551 FITSL-----------PEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGR 619
Cdd:PRK11160 446 LIEVLqqvgleklledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK 525
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 164423939 620 TTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKL 664
Cdd:PRK11160 526 TVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1094-1321 |
5.14e-48 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 171.36 E-value: 5.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPT--LYQGTVRENIILG-ANNDVTDEQIKFACQEA----NIYDFIMSLPdgmntlvgskgALLSGGQKQRIAIAR 1246
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpENLGLPREEIRERVEEAlelvGLEHLADRPP-----------HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1247 ALIRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELMKK 1321
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
385-657 |
5.93e-48 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 180.62 E-value: 5.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 385 FVTALGAAAKIyNTIDRESPidsSSEEGGKLENVVGTIRLENIkHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKS 464
Cdd:TIGR01842 284 FSGARQAYKRL-NELLANYP---SRDPAMPLPEPEGHLSVENV-TIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKS 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 465 TIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNI-RHGligtkwesesEEQQRERIYEAA 543
Cdd:TIGR01842 359 TLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFG----------ENADPEKIIEAA 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 544 RKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSE-GVVQAALEVAAEGRTTI 622
Cdd:TIGR01842 429 KLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEqALANAIKALKARGITVV 508
|
250 260 270
....*....|....*....|....*....|....*
gi 164423939 623 TIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAK 657
Cdd:TIGR01842 509 VITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1094-1313 |
1.10e-47 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 168.26 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNvNEYRSFIA 1173
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQGTVRENIilganndvtdeqikfacqeaniydfimslpdgmntlvgskGALLSGGQKQRIAIARALIRDPK 1253
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1254 ILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQG 1313
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1091-1314 |
1.12e-47 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 169.52 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1091 DGTIEFRDVHFRYptRPEQP-VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYR 1169
Cdd:cd03369 4 HGEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SFIALVSQEPTLYQGTVRENiiLGANNDVTDEQIKFACQeaniydfimslpdgmntlVGSKGALLSGGQKQRIAIARALI 1249
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSN--LDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1250 RDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGT 1314
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1095-1308 |
1.46e-47 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 169.18 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1095 EFRDVHFRYPTRpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIAL 1174
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1175 VSQEPT--LYQGTVRENIILGANN-----DVTDEQIKFACQEANIYDFIMSLPDgmntlvgskgaLLSGGQKQRIAIARA 1247
Cdd:cd03225 80 VFQNPDdqFFGPTVEEEVAFGLENlglpeEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1248 LIRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTI-QKADIIYVFDQGR 1308
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
422-673 |
2.40e-47 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 178.17 E-value: 2.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRP--DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN---VRWL 496
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 497 RQQIALVSQEPT--LFAC-TIYDNIRHGLIgtkweseseeqqrerIYEAARKANAHDFITSLPE--GYETNVGER-GFLL 570
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAEPLR---------------LHGLLSRAERRERVAELLErvGLPPDLADRyPHEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 571 SGGQKQRIAIARAIVSDPKILLLDEATSALDTksegVVQAAL-----EVAAE-GRTTITIAHRLSTIKD-AHNIVVMAQG 643
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQIlnllrDLQRElGLTYLFISHDLAVVRYiADRVAVMYDG 481
|
250 260 270
....*....|....*....|....*....|
gi 164423939 644 RIVEQGTHAELLAKRGAYYklvTAQAIAAV 673
Cdd:COG1123 482 RIVEDGPTEEVFANPQHPY---TRALLAAV 508
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1094-1308 |
3.44e-47 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 168.03 E-value: 3.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQ--PVLRGLNLSIQPGQYVALVGASGCGKSTTI-ALL-ErfYDPLSGGIFIDGReisslnvneyr 1169
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLsALLgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 sfIALVSQEPTLYQGTVRENIILGA--NNDVTDEQIKfACQ-EAniyDFIMsLPDGMNTLVGSKGALLSGGQKQRIAIAR 1246
Cdd:cd03250 68 --IAYVSQEPWIQNGTIRENILFGKpfDEERYEKVIK-ACAlEP---DLEI-LPDGDLTEIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1247 ALIRDPKILLLDEATSALDSES-----EHVVQAALdkaAKGRTTIAVAHRLSTIQKADIIYVFDQGR 1308
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1094-1312 |
7.61e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 167.91 E-value: 7.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQ-PVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREISSLNVNE-- 1167
Cdd:COG1136 5 LELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSEREla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1168 -YR-SFIALVSQE----PTLyqgTVRENIIL-----GANNDVTDEQIKFACQEANIYDFIMSLPdgmntlvgskgALLSG 1236
Cdd:COG1136 82 rLRrRHIGFVFQFfnllPEL---TALENVALplllaGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1237 GQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQKADIIYVFDQGRIVEQ 1312
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1094-1318 |
2.13e-46 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 166.59 E-value: 2.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYD-----PLSGGIFIDGREISSL--NVN 1166
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1167 EYRSFIALVSQEPTLYQGTVRENIILG------ANNDVTDEQIKFACQEANIYDfimslpDGMNTLVGSKgalLSGGQKQ 1240
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEALRKAALWD------EVKDRLHALG---LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1241 RIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1094-1321 |
4.69e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 162.93 E-value: 4.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlNVNEYRSFIA 1173
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQG-TVRENIIL-----GANNDVTDEQIKFACQEANIYDFimslpdgMNTLVGSkgalLSGGQKQRIAIARA 1247
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfarlyGLPRKEARERIDELLELFGLTDA-------ADRKVGT----LSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1248 LIRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELMKK 1321
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
422-649 |
1.37e-44 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 161.19 E-value: 1.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYK-----PIEGKVYLDDVDISTLNVR-- 494
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 495 WLRQQIALVSQEPTLFACTIYDNIRHG--LIGTKWESESEEQqrerIYEAARKANAHDfitslpegyetNVGER--GFLL 570
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrLHGIKLKEELDER----VEEALRKAALWD-----------EVKDRlhALGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 571 SGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQG 649
Cdd:cd03260 143 SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
422-658 |
2.85e-44 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 160.58 E-value: 2.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrPDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLNVRWLR 497
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTllrlLNGLL----KPTSGEVLVDGKDITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 QQIALVSQEPT--LFACTIYDNI-----RHGLigtkweseSEEQQRERIYEAARKANAHDFITSLPegyetnvgergFLL 570
Cdd:COG1122 75 RKVGLVFQNPDdqLFAPTVEEDVafgpeNLGL--------PREEIRERVEEALELVGLEHLADRPP-----------HEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 571 SGGQKQRIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQ 648
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGrRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVAD 215
|
250
....*....|
gi 164423939 649 GTHAELLAKR 658
Cdd:COG1122 216 GTPREVFSDY 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
422-645 |
3.24e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 159.60 E-value: 3.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIA 501
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFACTIYDNIRHGligtkWESESEEQQRERIYEAARKANahdfitsLPEGY-ETNVGErgflLSGGQKQRIAI 580
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFP-----FQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 581 ARAIVSDPKILLLDEATSALDTKSEGVVQAALE--VAAEGRTTITIAH------RLstikdAHNIVVMAQGRI 645
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLReyLAEEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
766-1064 |
1.22e-43 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 161.68 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 766 MLVGIFFSAICGAGNPTQAVFFAKLISSL------------SRPIVNEEIRASIKSDASFWCLMYLMLALVQCLAFSVQG 833
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnggmtnitgnsSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 834 WLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALG 913
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 914 WKLALVCIATIPILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLIS 993
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 994 VLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHEYDMF-TFFIVFSSVIFGAQSAGSVFSFAPdMGKATEAA 1064
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGeVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAA 309
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
422-657 |
1.69e-43 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 158.51 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRP-DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN---VRWLR 497
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 QQIALVSQEPTLFAC-TIYDNIRHGLIGTKWEseseeqqreriyEAARKANAHDFI-----TSLPEGYETNvgergflLS 571
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVP------------KAEIEERVLELLelvglEDKADAYPAQ-------LS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 572 GGQKQRIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAE-GRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQ 648
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETtQSILALLRDINRElGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
....*....
gi 164423939 649 GTHAELLAK 657
Cdd:cd03258 223 GTVEEVFAN 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1094-1313 |
3.07e-43 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 157.28 E-value: 3.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRP-EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLN---VNEYR 1169
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SFIALVSQE------PTLyqgTVRENI--ILGANNDVTDEQIKfacqEANIYDFIMSLPDgmntlvgSKGAL------LS 1235
Cdd:cd03257 82 KEIQMVFQDpmsslnPRM---TIGEQIaePLRIHGKLSKKEAR----KEAVLLLLVGVGL-------PEEVLnrypheLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1236 GGQKQRIAIARALIRDPKILLLDEATSALDSesehVVQAA-LD-----KAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGR 1308
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDV----SVQAQiLDllkklQEELGLTLLFITHDLGVVAKiADRVAVMYAGK 223
|
....*
gi 164423939 1309 IVEQG 1313
Cdd:cd03257 224 IVEEG 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1094-1319 |
1.08e-42 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 156.74 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQG-TVRENIILG--------ANNDVTDEQI-KFACQEANIYDFImslpdgmNTLVGSkgalLSGGQKQRIA 1243
Cdd:COG1120 79 YVPQEPPAPFGlTVRELVALGryphlglfGRPSAEDREAvEEALERTGLEHLA-------DRPVDE----LSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1244 IARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLS-TIQKADIIYVFDQGRIVEQGTHSELM 1319
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
422-649 |
1.22e-42 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 155.74 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVV-VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWL---R 497
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 QQIALVSQEPtlFAC-----TIYDNIRHGLIGTKWESESEEQQRERIYEAARKANAHDFITSLPegYEtnvgergflLSG 572
Cdd:cd03257 82 KEIQMVFQDP--MSSlnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYP--HE---------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 573 GQKQRIAIARAIVSDPKILLLDEATSALDTksegVVQAA-----LEVAAE-GRTTITIAHRLSTIKD-AHNIVVMAQGRI 645
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDV----SVQAQildllKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
....
gi 164423939 646 VEQG 649
Cdd:cd03257 225 VEEG 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1094-1318 |
1.24e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 155.92 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREI--SSLNVNEY 1168
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTITVDGEDLtdSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1169 RSFIALVSQEPTLYQG-TVRENIILGanndvtdeQIKF-------ACQEAniydfiMSLPD--GMNTLVGSKGALLSGGQ 1238
Cdd:COG1126 76 RRKVGMVFQQFNLFPHlTVLENVTLA--------PIKVkkmskaeAEERA------MELLErvGLADKADAYPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1239 KQRIAIARALIRDPKILLLDEATSALDSE--SEhVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTH 1315
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALDPElvGE-VLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPP 220
|
...
gi 164423939 1316 SEL 1318
Cdd:COG1126 221 EEF 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1094-1309 |
1.48e-42 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 154.96 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQ-PVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREISSLNVNEYR 1169
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SF----IALVSQE----PTLyqgTVRENIIL-----GANNDVTDEQIKFACQEaniydfiMSLPDGMNTLVGSkgalLSG 1236
Cdd:cd03255 78 AFrrrhIGFVFQSfnllPDL---TALENVELplllaGVPKKERRERAEELLER-------VGLGDRLNHYPSE----LSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1237 GQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQKADIIYVFDQGRI 1309
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1094-1320 |
1.64e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 156.12 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPE-QPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREISSLNVNEYR 1169
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTllrALAGLER---PWSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SFIALVSQEPTLY---QGTVRENI-----ILGanNDVTDEQIKFACQEANiydfimsLPDGmntLVGSKGALLSGGQKQR 1241
Cdd:COG1124 79 RRVQMVFQDPYASlhpRHTVDRILaeplrIHG--LPDREERIAELLEQVG-------LPPS---FLDRYPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1242 IAIARALIRDPKILLLDEATSALDSesehVVQAA-LD-----KAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGT 1314
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDV----SVQAEiLNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELT 222
|
....*.
gi 164423939 1315 HSELMK 1320
Cdd:COG1124 223 VADLLA 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1094-1323 |
2.22e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 156.44 E-value: 2.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSL-NVNEYRSFI 1172
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQEPT--LYQGTVRENIILG-ANNDVTDEQIKFACQEA----NIYDFIMSLPdgmntlvgskgALLSGGQKQRIAIA 1245
Cdd:TIGR04520 80 GMVFQNPDnqFVGATVEDDVAFGlENLGVPREEMRKRVDEAlklvGMEDFRDREP-----------HLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1246 RALIRDPKILLLDEATSALDSES-EHVVQAALD-KAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGT------HSE 1317
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTpreifsQVE 228
|
....*.
gi 164423939 1318 LMKKNG 1323
Cdd:TIGR04520 229 LLKEIG 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
422-657 |
3.78e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 157.93 E-value: 3.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRP-DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN---VRWLR 497
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 QQIALVSQEPTLF-ACTIYDNIRHGLIGTKWEseseeqqreriyEAARKANAHDFItSLpegyetnVGergfL------- 569
Cdd:COG1135 82 RKIGMIFQHFNLLsSRTVAENVALPLEIAGVP------------KAEIRKRVAELL-EL-------VG----Lsdkaday 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 ---LSGGQKQRIAIARAIVSDPKILLLDEATSALD---TKSegVVQAALEVAAE-GRTTITIAHRLSTIKD-AHNIVVMA 641
Cdd:COG1135 138 psqLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTRS--ILDLLKDINRElGLTIVLITHEMDVVRRiCDRVAVLE 215
|
250
....*....|....*.
gi 164423939 642 QGRIVEQGTHAELLAK 657
Cdd:COG1135 216 NGRIVEQGPVLDVFAN 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
422-673 |
4.03e-42 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 155.20 E-value: 4.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIA 501
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTL-FACTIYDNIRHGLIG-TKWESESEEQQRERIYEAARKANAHDFItslpegyETNVGErgflLSGGQKQRIA 579
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRYPhLGLFGRPSAEDREAVEEALERTGLEHLA-------DRPVDE----LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 580 IARAIVSDPKILLLDEATSALDtksegvVQAALEV--------AAEGRTTITIAHRLS-TIKDAHNIVVMAQGRIVEQGT 650
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLD------LAHQLEVlellrrlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
250 260
....*....|....*....|...
gi 164423939 651 HAELLakrgayyklvTAQAIAAV 673
Cdd:COG1120 222 PEEVL----------TPELLEEV 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1094-1319 |
4.80e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 162.38 E-value: 4.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRP--EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLN---VNEY 1168
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1169 RSFIALVSQEPtlYQG-----TVRENII--LGANNDVTDEQIKFACQEAniydfimsLpdgmnTLVG-SKGAL------L 1234
Cdd:COG1123 341 RRRVQMVFQDP--YSSlnprmTVGDIIAepLRLHGLLSRAERRERVAEL--------L-----ERVGlPPDLAdrypheL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1235 SGGQKQRIAIARALIRDPKILLLDEATSALDSesehVVQAA-LD-----KAAKGRTTIAVAHRLSTIQK-ADIIYVFDQG 1307
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDG 481
|
250
....*....|..
gi 164423939 1308 RIVEQGTHSELM 1319
Cdd:COG1123 482 RIVEDGPTEEVF 493
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
422-648 |
8.46e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 153.28 E-value: 8.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPS-RPDVVVMEDVSLVIPAGKTTALVGASGSGKST---IVGLVERfykPIEGKVYLDDVDISTLN----V 493
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 494 RWLRQQIALVSQEPTLFAC-TIYDNIRHGLIGTKWESeseeqqreriyeAARKANAHDFITSLpegyetNVGERGFL--- 569
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVALPLLLAGVSR------------KERRERARELLERV------GLGDRLDHrps 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 -LSGGQKQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAE-GRTTITIAHRLSTIKDAHNIVVMAQGRIV 646
Cdd:COG1136 144 qLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKtGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
..
gi 164423939 647 EQ 648
Cdd:COG1136 224 SD 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
422-645 |
8.88e-42 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 151.21 E-value: 8.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYP--SRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQ 499
Cdd:cd03246 1 LEVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEPTLFACTIYDNIrhgligtkweseseeqqreriyeaarkanahdfitslpegyetnvgergflLSGGQKQRIA 579
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI---------------------------------------------------LSGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 580 IARAIVSDPKILLLDEATSALDTKSEGVVQAALE-VAAEGRTTITIAHRLSTIKDAHNIVVMAQGRI 645
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAaLKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
124-373 |
1.82e-41 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 153.95 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 124 FQNYFAGVTTYDDF-TDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVT 202
Cdd:pfam00664 22 LGRILDVLLPDGDPeTQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 203 TRITADTNLIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGS 282
Cdd:pfam00664 102 SRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 283 VADEVISSVRNAIAFGTQDRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQGSRFLLSGDTELRKIL 362
Cdd:pfam00664 182 VAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLV 261
|
250
....*....|...
gi 164423939 363 T--VMMSVMIGAF 373
Cdd:pfam00664 262 AflSLFAQLFGPL 274
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1094-1318 |
2.03e-41 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 152.35 E-value: 2.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRP-EQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREISSLNVNEYR 1169
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SF---IALVSQEPTLYQG-TVRENI-----ILGANNDVTDEQIKFACQEANIYDFIMSLPdgmntlvgskgALLSGGQKQ 1240
Cdd:cd03258 79 KArrrIGMIFQHFNLLSSrTVFENValpleIAGVPKAEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1241 RIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSE 1317
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
.
gi 164423939 1318 L 1318
Cdd:cd03258 228 V 228
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1092-1329 |
2.86e-41 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 152.76 E-value: 2.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1092 GTIEFRDVHFRYPTRPeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSF 1171
Cdd:cd03288 18 GEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1172 IALVSQEPTLYQGTVRENiiLGANNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRD 1251
Cdd:cd03288 97 LSIILQDPILFSGSIRFN--LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1252 PKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELM-KKNGRYAELV 1329
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1094-1333 |
3.04e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 153.22 E-value: 3.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEP-TLYQG-TVRENIILG-ANNDVTDEQIKfacqeANIYDFimSLPDGMNTLVGSKGALLSGGQKQRIAIARALIR 1250
Cdd:PRK13632 87 IIFQNPdNQFIGaTVEDDIAFGlENKKVPPKKMK-----DIIDDL--AKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1251 DPKILLLDEATSALDSESEH-VVQAALDKAAKG-RTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMkKNGRYAEL 1328
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKReIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL-NNKEILEK 238
|
....*
gi 164423939 1329 VNLQS 1333
Cdd:PRK13632 239 AKIDS 243
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1094-1320 |
3.57e-41 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 151.89 E-value: 3.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREISSLNVNEYRS 1170
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTllrLIVGLLR---PDSGEVLIDGEDISGLSEAELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1171 F---IALVSQEPTLYQG-TVRENIILGANNdvtdeqiKFACQEANIYDFIMS-LpdgmnTLVGSKGAL------LSGGQK 1239
Cdd:cd03261 75 LrrrMGMLFQSGALFDSlTVFENVAFPLRE-------HTRLSEEEIREIVLEkL-----EAVGLRGAEdlypaeLSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1240 QRIAIARALIRDPKILLLDEATSALDSESEHVVQA-ALD-KAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHS 1316
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDlIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPE 222
|
....
gi 164423939 1317 ELMK 1320
Cdd:cd03261 223 ELRA 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
420-650 |
5.32e-41 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 150.26 E-value: 5.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 420 GTIRLENIKHIYpsRPDVV-VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQ 498
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 499 QIALVSQEPTLFACTIYDNIrhgligtkweSESEEQQRERIYEAARkanahdfitslpegyetnVGERGFLLSGGQKQRI 578
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL----------DPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 579 AIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGT 650
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1094-1312 |
1.36e-40 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 149.54 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPT-RPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNeyrsfI 1172
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQEPTLYQ-GTVRENIILGAN-NDVTDEQIKfacQEAniydfimslpDGMNTLVGSKGAL------LSGGQKQRIAI 1244
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElQGVPKAEAR---ERA----------EELLELVGLSGFEnayphqLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1245 ARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLS-TIQKADIIYVFDQ--GRIVEQ 1312
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1094-1313 |
2.14e-40 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 148.82 E-value: 2.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRsfIA 1173
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQG-TVRENIILG-ANNDVTDEQIKFACQEANiydFIMSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRD 1251
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlKLRGVPKAEIRARVRELL---ELVGLEGLLNRYPHE----LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1252 PKILLLDEATSALDSESEHVVQAALDK--AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1112-1262 |
2.42e-40 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 146.25 E-value: 2.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQG-TVRENI 1190
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1191 ILGAN-----NDVTDEQIKFACQEANIYDFImslpdgmNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATS 1262
Cdd:pfam00005 81 RLGLLlkglsKREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1094-1311 |
3.05e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.85 E-value: 3.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRP-EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNeyrsfI 1172
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQEPTLYQ-GTVRENIILGAN-NDVTDEQIKfacqeANIYDFImslpdgmnTLVGSKGAL------LSGGQKQRIAI 1244
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLElRGVPKAERR-----ERARELL--------ELVGLAGFEdayphqLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1245 ARALIRDPKILLLDEATSALDSESEHVVQAALDK--AAKGRTTIAVAH------RLstiqkADIIYVFDQ--GRIVE 1311
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1094-1324 |
6.42e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 148.47 E-value: 6.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNvNEYRSFIA 1173
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQG-TVRENI-ILGANNDVTDEQIKFACQEAnIYDFIMSlpDGMNTLVGSkgalLSGGQKQRIAIARALIRD 1251
Cdd:COG4555 78 VLPDERGLYDRlTVRENIrYFAELYGLFDEELKKRIEEL-IELLGLE--EFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1252 PKILLLDEATSALDSESEHVVQAALDKAAK-GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELMKKNGR 1324
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
422-645 |
7.46e-40 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 147.25 E-value: 7.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPD-VVVMEDVSLVIPAGKTTALVGASGSGKST---IVGLVERfykPIEGKVYLDDVDISTLNVRWL- 496
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 497 ---RQQIALVSQE----PTLfacTIYDNIRHGLIGTKweseseeqqrerIYEAARKANAHDFITS--LPEGYETNVGErg 567
Cdd:cd03255 78 afrRRHIGFVFQSfnllPDL---TALENVELPLLLAG------------VPKKERRERAEELLERvgLGDRLNHYPSE-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 568 flLSGGQKQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAEGRTTITIA-HRLSTIKDAHNIVVMAQGRI 645
Cdd:cd03255 141 --LSGGQQQRVAIARALANDPKIILADEPTGNLDSEtGKEVMELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1094-1308 |
1.09e-39 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 145.41 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVN--EYRSF 1171
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1172 IALVSQEPTLYQG-TVRENIILGanndvtdeqikfacqeaniydfimslpdgmntlvgskgalLSGGQKQRIAIARALIR 1250
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1251 DPKILLLDEATSALDSESEHVVQAALD--KAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGR 1308
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
422-656 |
1.63e-39 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 147.26 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRP-DVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLNVRWL 496
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTllraLAGLE----RPWSGEVTFDGRPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 497 RQQIALVSQEPTLfAC----TIYDNIR-----HGLIGTKweseseeqqrERIYEAARKANahdfitsLPEGyetnvgerg 567
Cdd:COG1124 78 RRRVQMVFQDPYA-SLhprhTVDRILAeplriHGLPDRE----------ERIAELLEQVG-------LPPS--------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 568 FL------LSGGQKQRIAIARAIVSDPKILLLDEATSALDTksegVVQAA-LEV-----AAEGRTTITIAHRLSTIkdAH 635
Cdd:COG1124 131 FLdryphqLSGGQRQRVAIARALILEPELLLLDEPTSALDV----SVQAEiLNLlkdlrEERGLTYLFVSHDLAVV--AH 204
|
250 260
....*....|....*....|....
gi 164423939 636 ---NIVVMAQGRIVEQGTHAELLA 656
Cdd:COG1124 205 lcdRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
423-644 |
1.73e-39 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 146.07 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 423 RLENIKHIYPSRpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIAL 502
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 503 VSQEPT--LFACTIYDNIRHGLIGTKWeseseeqQRERIYEAARKANAHDFITSLPEgyetnvgERGFLLSGGQKQRIAI 580
Cdd:cd03225 80 VFQNPDdqFFGPTVEEEVAFGLENLGL-------PEEEIEERVEEALELVGLEGLRD-------RSPFTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 581 ARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGR 644
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLkKLKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1095-1308 |
2.50e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 143.54 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1095 EFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIAL 1174
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1175 VSQeptlyqgtvreniilganndvtdeqikfacqeaniydfimslpdgmntlvgskgalLSGGQKQRIAIARALIRDPKI 1254
Cdd:cd00267 78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1255 LLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQKA-DIIYVFDQGR 1308
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1094-1309 |
1.53e-38 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 141.77 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlNVNEYRSFIA 1173
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQG-TVRENIilganndvtdeqikfacqeaniydfimslpdgmntlvgskgaLLSGGQKQRIAIARALIRDP 1252
Cdd:cd03230 77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1253 KILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRI 1309
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1094-1319 |
1.78e-38 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 144.37 E-value: 1.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRpeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:cd03295 1 IEFENVTKRYGGG--KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLY-QGTVRENI-ILGANNDVTDEQIKfacqeANIYDFI--MSLPDGmnTLVGSKGALLSGGQKQRIAIARALI 1249
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIaLVPKLLKWPKEKIR-----ERADELLalVGLDPA--EFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1250 RDPKILLLDEATSALDSesehVVQAALDKAAK------GRTTIAVAHRL-STIQKADIIYVFDQGRIVEQGTHSELM 1319
Cdd:cd03295 152 ADPPLLLMDEPFGALDP----ITRDQLQEEFKrlqqelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1094-1319 |
1.87e-38 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 151.59 E-value: 1.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEqPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDP---LSGGIFIDGREISSLNVNEYRS 1170
Cdd:COG1123 5 LEVRDLSVRYPGGDV-PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1171 FIALVSQEPT--LYQGTVRENIILG-ANNDVTDEQIKFACQEAniYDFImslpdGMNTLVGSKGALLSGGQKQRIAIARA 1247
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEAlENLGLSRAEARARVLEL--LEAV-----GLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1248 LIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTI-QKADIIYVFDQGRIVEQGTHSELM 1319
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
441-598 |
1.99e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 140.86 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 441 EDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLF-ACTIYDNIR 519
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 520 HGLIGTKWeseseeqqreriYEAARKANAHDFITSLPEGY--ETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEAT 597
Cdd:pfam00005 82 LGLLLKGL------------SKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 164423939 598 S 598
Cdd:pfam00005 150 A 150
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
427-656 |
2.05e-38 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 143.97 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLNVR---WLRQQ 499
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVllklIIGLL----RPDSGEILVDGQDITGLSEKelyELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEPTLF-ACTIYDNI-----RHGLIGTKweseseeqqreRIYEAAR-KANAhdfitslpegyetnVGERGFL--- 569
Cdd:COG1127 84 IGMLFQGGALFdSLTVFENVafplrEHTDLSEA-----------EIRELVLeKLEL--------------VGLPGAAdkm 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 ---LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVV-------QAALevaaeGRTTITIAHRLSTIKD-AHNIV 638
Cdd:COG1127 139 pseLSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIdelirelRDEL-----GLTSVVVTHDLDSAFAiADRVA 213
|
250
....*....|....*...
gi 164423939 639 VMAQGRIVEQGTHAELLA 656
Cdd:COG1127 214 VLADGKIIAEGTPEELLA 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
422-644 |
3.97e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 140.79 E-value: 3.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN--VRWLRQQ 499
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEPTLFA-CTIYDNIRHGligtkweseseeqqreriyeaarkanahdfitslpegyetnvgergflLSGGQKQRI 578
Cdd:cd03229 78 IGMVFQDFALFPhLTVLENIALG------------------------------------------------LSGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 579 AIARAIVSDPKILLLDEATSALDTKSEGVVQAALE--VAAEGRTTITIAHRLS-TIKDAHNIVVMAQGR 644
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
422-649 |
4.52e-38 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 141.89 E-value: 4.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSrpdVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRwlRQQIA 501
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFA-CTIYDNIRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIAI 580
Cdd:cd03259 76 MVFQDYALFPhLTVAENIAFGL---KLRGVPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 581 ARAIVSDPKILLLDEATSALDTKSEGVVQAALE--VAAEGRTTITIAHRLS---TIkdAHNIVVMAQGRIVEQG 649
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKelQRELGITTIYVTHDQEealAL--ADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
422-656 |
4.89e-38 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 150.44 E-value: 4.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVVVmEDVSLVIPAGKTTALVGASGSGKST----IVGLVERFYKpIEGKVYLDDVDISTLNVRWLR 497
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTlalaLMGLLPHGGR-ISGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 QQIALVSQEPT--LFACTIYDNIRHGLIGTKWESESEEQQrerIYEAARKANAHDFITSLPegyetnvgergFLLSGGQK 575
Cdd:COG1123 83 RRIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARAR---VLELLEAVGLERRLDRYP-----------HQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 576 QRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALE--VAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHA 652
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPE 228
|
....
gi 164423939 653 ELLA 656
Cdd:COG1123 229 EILA 232
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1094-1320 |
5.74e-38 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 142.81 E-value: 5.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREISSLNVNEYRS 1170
Cdd:COG1127 6 IEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVllkLIIGLLR---PDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1171 FIALVSqepTLYQG-------TVRENIILG--ANNDVTDEQIKfacQEANiydfiMSLpdgmnTLVGSKGAL------LS 1235
Cdd:COG1127 80 LRRRIG---MLFQGgalfdslTVFENVAFPlrEHTDLSEAEIR---ELVL-----EKL-----ELVGLPGAAdkmpseLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1236 GGQKQRIAIARALIRDPKILLLDEATSALDSESehvvQAALD------KAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGR 1308
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPIT----SAVIDelirelRDELGLTSVVVTHDLDSAFAiADRVAVLADGK 219
|
250
....*....|..
gi 164423939 1309 IVEQGTHSELMK 1320
Cdd:COG1127 220 IIAEGTPEELLA 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
422-657 |
6.24e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 143.34 E-value: 6.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRW-LRQQI 500
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEPT--LFACTIYDNIRHGL--IGTKwesesEEQQRERIYEAARKANAHDFITSLPegyetnvgergFLLSGGQKQ 576
Cdd:TIGR04520 80 GMVFQNPDnqFVGATVEDDVAFGLenLGVP-----REEMRKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 577 RIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAE-GRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAEL 654
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGrKEVLETIRKLNKEeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREI 223
|
...
gi 164423939 655 LAK 657
Cdd:TIGR04520 224 FSQ 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
422-656 |
6.77e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 142.44 E-value: 6.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVErfykPIEGKVYLDDVDI--STLNVRW 495
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrcINLLEE----PDSGTITVDGEDLtdSKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 LRQQIALVSQEPTLFA-CTIYDNIRHGLI---GTKWEseseeqqreriyEAARKANAH-------DFITSLPEGyetnvg 564
Cdd:COG1126 75 LRRKVGMVFQQFNLFPhLTVLENVTLAPIkvkKMSKA------------EAEERAMELlervglaDKADAYPAQ------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 565 ergflLSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMA 641
Cdd:COG1126 137 -----LSGGQQQRVAIARALAMEPKVMLFDEPTSALDpeLVGE-VLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMD 210
|
250
....*....|....*
gi 164423939 642 QGRIVEQGTHAELLA 656
Cdd:COG1126 211 GGRIVEEGPPEEFFE 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
422-649 |
6.81e-38 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 140.14 E-value: 6.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNvRWLRQQIA 501
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFACTIYDNIrhgligtkweseseeqqreriyeaarkanahdfitslpegyetnvGERgflLSGGQKQRIAIA 581
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------------GRR---FSGGERQRLALA 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 582 RAIVSDPKILLLDEATSALDTKSEgvvQAALEV---AAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQG 649
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLDPITE---RQLLSLifeVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
148-665 |
1.26e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 154.75 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 148 FVY--LAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLTL- 224
Cdd:PLN03232 954 VVYalLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMn 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 225 ---QALATFIAAFVIGFVSFWKLtLILLSTVVALTLVMGGGSQFIIKF-SKQNIAAYAEGGSvADEVISSVRnaiAFGTQ 300
Cdd:PLN03232 1034 qlwQLLSTFALIGTVSTISLWAI-MPLLILFYAAYLYYQSTSREVRRLdSVTRSPIYAQFGE-ALNGLSSIR---AYKAY 1108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 301 DRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVlylnYGLAFWQGSRF--LLSGDTELRKILTVMMSVMIgAFNLgNI 378
Cdd:PLN03232 1109 DRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETL----GGVMIWLTATFavLRNGNAENQAGFASTMGLLL-SYTL-NI 1182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 379 APNLQAFVTALGAAAKIYNTIDRESP-IDSSSEEGGKLEN--------VVGTIRLENIKHIYpsRPDVV-VMEDVSLVIP 448
Cdd:PLN03232 1183 TTLLSGVLRQASKAENSLNSVERVGNyIDLPSEATAIIENnrpvsgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVS 1260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 449 AGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNI----RHGLIG 524
Cdd:PLN03232 1261 PSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdpfsEHNDAD 1340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 525 tkweseseeqqrerIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKS 604
Cdd:PLN03232 1341 --------------LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 605 EGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRG-AYYKLV 665
Cdd:PLN03232 1407 DSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMV 1468
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1094-1314 |
1.30e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 144.84 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQ-PVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREISSLNVNEYR 1169
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SF---IALVSQEPTLYQG-TVRENI-----ILGANNDVTDEQIKfacqeaniydfimSLPDgmntLVGSKG------ALL 1234
Cdd:COG1135 79 AArrkIGMIFQHFNLLSSrTVAENValpleIAGVPKAEIRKRVA-------------ELLE----LVGLSDkadaypSQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1235 SGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVE 1311
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 164423939 1312 QGT 1314
Cdd:COG1135 222 QGP 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1094-1318 |
2.37e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 144.47 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTT---IALLERfydPLSGGIFIDGREISSLNVNEyRs 1170
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLlrmIAGFET---PDSGRILLDGRDVTGLPPEK-R- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1171 FIALVSQE----PTLyqgTVRENI-----ILGANNDVTDEQIkfacQEAniydfiMSLPdGMNTLVGSKGALLSGGQKQR 1241
Cdd:COG3842 78 NVGMVFQDyalfPHL---TVAENVafglrMRGVPKAEIRARV----AEL------LELV-GLEGLADRYPHQLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1242 IAIARALIRDPKILLLDEATSALDSESEHVVQAALDK--AAKGRTTIAVAHRLS---TIqkADIIYVFDQGRIVEQGTHS 1316
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPE 221
|
..
gi 164423939 1317 EL 1318
Cdd:COG3842 222 EI 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1092-1318 |
6.58e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 143.29 E-value: 6.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1092 GTIEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTT---IALLErfyDPLSGGIFIDGREISSLNVNEy 1168
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmIAGLE---DPTSGEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1169 RSfIALVSQEPTLY-QGTVRENI-----ILGANNDVTDEQIKFACQEANIYDFIMSLPDGmntlvgskgalLSGGQKQRI 1242
Cdd:COG3839 75 RN-IAMVFQSYALYpHMTVYENIafplkLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQ-----------LSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1243 AIARALIRDPKILLLDEATSALDSESEHVVQAALDK--AAKGRTTIAVAHRLS---TIqkADIIYVFDQGRIVEQGTHSE 1317
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRlhRRLGTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGTPEE 220
|
.
gi 164423939 1318 L 1318
Cdd:COG3839 221 L 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
422-647 |
1.11e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.45 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRP-DVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLnvrwl 496
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTllrlIAGLE----KPTSGEVLVDGKPVTGP----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 497 RQQIALVSQEPTLFA-CTIYDNIRHGLIGTKWEseseeqqreriyEAARKANAHDFITSlpegyetnVGERGFL------ 569
Cdd:COG1116 79 GPDRGVVFQEPALLPwLTVLDNVALGLELRGVP------------KAERRERARELLEL--------VGLAGFEdayphq 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 LSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgvVQAALE--VAAEGRTTITIAH------RLstikdAHNIVV 639
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDalTRER--LQDELLrlWQETGKTVLFVTHdvdeavFL-----ADRVVV 211
|
250
....*....|
gi 164423939 640 MAQ--GRIVE 647
Cdd:COG1116 212 LSArpGRIVE 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
182-664 |
1.40e-36 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 151.25 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 182 LESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVmgg 261
Cdd:TIGR00957 1045 LHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFV--- 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 262 gSQFIIKFSKQ----NIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAHL-------------TRAEHFGFRLKGS 324
Cdd:TIGR00957 1122 -QRFYVASSRQlkrlESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVdenqkayypsivaNRWLAVRLECVGN 1200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 325 IGVMVAGMMTVL---YLNYGLAFwqgsrflLSGDTELRkiLTVMMSVMIgafnlgNIAPNLQAFVTALgAAAKIYNTIDR 401
Cdd:TIGR00957 1201 CIVLFAALFAVIsrhSLSAGLVG-------LSVSYSLQ--VTFYLNWLV------RMSSEMETNIVAV-ERLKEYSETEK 1264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 402 ESP--IDSSSEEGGKLEnvVGTIRLENIKHIYpsRPDV-VVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIE 478
Cdd:TIGR00957 1265 EAPwqIQETAPPSGWPP--RGRVEFRNYCLRY--REDLdLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAE 1340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 479 GKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIrhgligtkweSESEEQQRERIYEAARKANAHDFITSLPEG 558
Cdd:TIGR00957 1341 GEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL----------DPFSQYSDEEVWWALELAHLKTFVSALPDK 1410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 559 YETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIV 638
Cdd:TIGR00957 1411 LDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVI 1490
|
490 500
....*....|....*....|....*.
gi 164423939 639 VMAQGRIVEQGTHAELLAKRGAYYKL 664
Cdd:TIGR00957 1491 VLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1094-1318 |
1.50e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.04 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRpeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLN---VNEYRS 1170
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1171 FIALVSQEPTL-YQGTVRENIILGANNDV----------TDEQIKFACQ---EANIYDFIMSLPDgmntlvgskgaLLSG 1236
Cdd:COG3638 81 RIGMIFQQFNLvPRLSVLTNVLAGRLGRTstwrsllglfPPEDRERALEaleRVGLADKAYQRAD-----------QLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1237 GQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGRVVFDG 229
|
....*
gi 164423939 1314 THSEL 1318
Cdd:COG3638 230 PPAEL 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
422-659 |
1.54e-36 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 138.84 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSrpdVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNvRWLRQQIA 501
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFA-CTIYDNIR-----HGLIGTKweseseeqQRERIYEAARKANahdfitsLPEGYETNVGErgflLSGGQK 575
Cdd:COG4555 78 VLPDERGLYDrLTVRENIRyfaelYGLFDEE--------LKKRIEELIELLG-------LEEFLDRRVGE----LSTGMK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 576 QRIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAE 653
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVMArRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDE 218
|
....*.
gi 164423939 654 LLAKRG 659
Cdd:COG4555 219 LREEIG 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
422-657 |
2.04e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 137.89 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWlRQQIA 501
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFA-CTIYDNIRH--GLIGTKweseseeqqreriyEAARKANAHDFI--TSLPEGYETNVGErgflLSGGQKQ 576
Cdd:COG1131 77 YVPQEPALYPdLTVRENLRFfaRLYGLP--------------RKEARERIDELLelFGLTDAADRKVGT----LSGGMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 577 RIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAEL 654
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEArRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDEL 218
|
...
gi 164423939 655 LAK 657
Cdd:COG1131 219 KAR 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
422-655 |
2.91e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.97 E-value: 2.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIA 501
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEP--TLFACTIYDNIRHGLIGTKwesESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIA 579
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKK---VPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 580 IARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEG-RTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELL 655
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGkREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1094-1309 |
3.16e-36 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 136.89 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREI--SSLNVNEY 1168
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTIIIDGLKLtdDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1169 RSFIALVSQEPTLY-QGTVRENIIL------GANNDVTDEQIKFACQEANIYDFIMSLPdgmntlvgskgALLSGGQKQR 1241
Cdd:cd03262 75 RQKVGMVFQQFNLFpHLTVLENITLapikvkGMSKAEAEERALELLEKVGLADKADAYP-----------AQLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1242 IAIARALIRDPKILLLDEATSALDSE-SEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRI 1309
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPElVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1094-1318 |
5.36e-36 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 136.93 E-value: 5.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSL---NVNEYRS 1170
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1171 FIALVSQEPTLY-QGTVRENIILGANNDVT------------DEQIKFACQEANiydfimslpdGMNTLVGSKGALLSGG 1237
Cdd:cd03256 79 QIGMIFQQFNLIeRLSVLENVLSGRLGRRStwrslfglfpkeEKQRALAALERV----------GLLDKAYQRADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1238 QKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAA--KGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGT 1314
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGP 228
|
....
gi 164423939 1315 HSEL 1318
Cdd:cd03256 229 PAEL 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
423-644 |
1.12e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 133.14 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 423 RLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIAL 502
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 503 VSQeptlfactiydnirhgligtkweseseeqqreriyeaarkanahdfitslpegyetnvgergflLSGGQKQRIAIAR 582
Cdd:cd00267 78 VPQ----------------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 583 AIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEGRTTITIAHRLSTIKDA-HNIVVMAQGR 644
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASrERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1094-1328 |
1.88e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 136.68 E-value: 1.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:PRK13635 6 IRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEP--TLYQGTVRENIILGANN-----DVTDEQIKFACQEANIYDFIMSLPdgmntlvgskgALLSGGQKQRIAIAR 1246
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENigvprEEMVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1247 ALIRDPKILLLDEATSALDSES-EHVVQAALD-KAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGR 1324
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGrREVLETVRQlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
....
gi 164423939 1325 YAEL 1328
Cdd:PRK13635 234 LQEI 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
427-656 |
2.26e-35 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 134.94 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLNV---RWLRQQ 499
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTllrlIVGLL----RPDSGEVLIDGEDISGLSEaelYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEPTLF-ACTIYDNIRHGLigtkweseseeqqreriYEaarkanaHdfiTSLPEGYETN--------VGERGFL- 569
Cdd:cd03261 79 MGMLFQSGALFdSLTVFENVAFPL-----------------RE-------H---TRLSEEEIREivlekleaVGLRGAEd 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 -----LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQA-ALEVAAE-GRTTITIAHRLSTIKD-AHNIVVMA 641
Cdd:cd03261 132 lypaeLSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDlIRSLKKElGLTSIMVTHDLDTAFAiADRIAVLY 211
|
250
....*....|....*
gi 164423939 642 QGRIVEQGTHAELLA 656
Cdd:cd03261 212 DGKIVAEGTPEELRA 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
422-648 |
2.27e-35 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 134.52 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPS-RPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRwlrqqI 500
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEPTLFA-CTIYDNIRHGLIGTKWEseseeqqreriyEAARKANAHDFITSlpegyetnVGERGFL------LSGG 573
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVP------------KAEARERAEELLEL--------VGLSGFEnayphqLSGG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 574 QKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALE--VAAEGRTTITIAHRLS-TIKDAHNIVVMAQ--GRIVEQ 648
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLdiWRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
422-654 |
2.78e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.18 E-value: 2.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSrpDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVErfykPIEGKVYLDDVDISTLN---VR 494
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTllrcLNGLVE----PTSGEILVDGQDVTALRgraLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 495 WLRQQIALVSQEPTLFA-CTIYDNIRHGLIGTK--WESESEeqqrerIYEAARKANAHDFITSlpegyetnVGERGFL-- 569
Cdd:COG3638 77 RLRRRIGMIFQQFNLVPrLSVLTNVLAGRLGRTstWRSLLG------LFPPEDRERALEALER--------VGLADKAyq 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 ----LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAE-GRTTITIAHRLSTIKD-AHNIVVMAQ 642
Cdd:COG3638 143 radqLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRD 222
|
250
....*....|..
gi 164423939 643 GRIVEQGTHAEL 654
Cdd:COG3638 223 GRVVFDGPPAEL 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
421-655 |
4.07e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 137.97 E-value: 4.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDIST-LNVRw 495
Cdd:COG1118 2 SIEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTllriIAGLE----TPDSGRIVLNGRDLFTnLPPR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 lRQQIALVSQEPTLFA-CTIYDNIRHGLIGTKWEseseeqqreriyEAARKANAHDFItSLpegyetnVGERGFL----- 569
Cdd:COG1118 74 -ERRVGFVFQHYALFPhMTVAENIAFGLRVRPPS------------KAEIRARVEELL-EL-------VQLEGLAdryps 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 -LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKsegvVQAALE------VAAEGRTTITIAH------RLstikdAHN 636
Cdd:COG1118 133 qLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK----VRKELRrwlrrlHDELGGTTVFVTHdqeealEL-----ADR 203
|
250
....*....|....*....
gi 164423939 637 IVVMAQGRIVEQGTHAELL 655
Cdd:COG1118 204 VVVMNQGRIEQVGTPDEVY 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1094-1309 |
4.60e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.45 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGReisslNVNEYRSFIA 1173
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQG---TVRENIILGANNDV--------TD-EQIKFACQEANIYDFImslpdgmNTLVGSkgalLSGGQKQR 1241
Cdd:COG1121 79 YVPQRAEVDWDfpiTVRDVVLMGRYGRRglfrrpsrADrEAVDEALERVGLEDLA-------DRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1242 IAIARALIRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRI 1309
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
422-656 |
5.94e-35 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 136.34 E-value: 5.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVV-VMEDVSLVIPAGKTTALVGASGSGKST----IVGLVERFYKpIEGKVYLDDVDISTLN---V 493
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTlaraILGLLPPPGI-TSGEILFDGEDLLKLSekeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 494 RWLR-QQIALVSQEPtlFAC-----TIYDNI-----RHGLIGTKweseseeqqreriyEAARKA----------NAHDFI 552
Cdd:COG0444 81 RKIRgREIQMIFQDP--MTSlnpvmTVGDQIaeplrIHGGLSKA--------------EARERAiellervglpDPERRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 553 TSLPegyetnvgergFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTksegVVQAA-----LEVAAE-GRTTITIAH 626
Cdd:COG0444 145 DRYP-----------HELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQilnllKDLQRElGLAILFITH 209
|
250 260 270
....*....|....*....|....*....|.
gi 164423939 627 RLSTIKD-AHNIVVMAQGRIVEQGTHAELLA 656
Cdd:COG0444 210 DLGVVAEiADRVAVMYAGRIVEEGPVEELFE 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
422-657 |
6.15e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 137.24 E-value: 6.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYP-SRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWL---R 497
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 QQIALVSQEPTLFAC-TIYDNIRHGLIGTKWESESEEQQRERIYEAARKANAHDFitslpegYETNvgergflLSGGQKQ 576
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADR-------YPAQ-------LSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 577 RIAIARAIVSDPKILLLDEATSALDTKSegvVQAALEVAAE-----GRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGT 650
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPAT---TRSILELLKDinrelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
....*..
gi 164423939 651 HAELLAK 657
Cdd:PRK11153 225 VSEVFSH 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1095-1313 |
6.33e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 131.79 E-value: 6.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1095 EFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIAL 1174
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1175 VSQeptlyqgtvreniilganndvtdeqikfACQEANIYDFIMSlpdGMNTLvgskgallSGGQKQRIAIARALIRDPKI 1254
Cdd:cd03214 78 VPQ----------------------------ALELLGLAHLADR---PFNEL--------SGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1255 LLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLS-TIQKADIIYVFDQGRIVEQG 1313
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
422-656 |
7.27e-35 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 133.97 E-value: 7.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVVvmEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIA 501
Cdd:cd03295 1 IEFENVTKRYGGGKKAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFA-CTIYDNIrhGLIGT--KWEseseeqqreriyEAARKANAHDFITSLpegyetNVGERGFL------LSG 572
Cdd:cd03295 79 YVIQQIGLFPhMTVEENI--ALVPKllKWP------------KEKIRERADELLALV------GLDPAEFAdrypheLSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 573 GQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAE--GRTTITIAHRL-STIKDAHNIVVMAQGRIVEQG 649
Cdd:cd03295 139 GQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVG 218
|
....*..
gi 164423939 650 THAELLA 656
Cdd:cd03295 219 TPDEILR 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
422-644 |
1.03e-34 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 132.21 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDV--VVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVERfykpIEGKVYLDDvdistlnvrw 495
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSllsaLLGELEK----LSGSVSVPG---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 lrqQIALVSQEPTLFACTIYDNIrhgLIGTKWESESeeqqreriYEAARKANA-HDFITSLPEGYETNVGERGFLLSGGQ 574
Cdd:cd03250 67 ---SIAYVSQEPWIQNGTIRENI---LFGKPFDEER--------YEKVIKACAlEPDLEILPDGDLTEIGEKGINLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALDTKS-----EGVVQAALevaAEGRTTITIAHRLSTIKDAHNIVVMAQGR 644
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1110-1319 |
1.09e-34 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 132.56 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1110 PVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE-YRSFIALVSQE----PTLyqg 1184
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGrrifPEL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 TVRENIILGANNDVTDeqiKFACQEANIYDFIMSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKILLLDEATSAL 1264
Cdd:cd03224 91 TVEENLLLGAYARRRA---KRKARLERVYELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1265 D-SESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELM 1319
Cdd:cd03224 164 ApKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
422-654 |
2.17e-34 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 132.31 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTL---NVRWLRQ 498
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 499 QIALVSQEPTLFA-CTIYDNIRHGLIGTK--WESESEEQQRERIYEAARKANAHDfitsLPEGYETNVGErgflLSGGQK 575
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGRRstWRSLFGLFPKEEKQRALAALERVG----LLDKAYQRADQ----LSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 576 QRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAE-GRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHA 652
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPAsSRQVMDLLKRINREeGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPA 230
|
..
gi 164423939 653 EL 654
Cdd:cd03256 231 EL 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
422-654 |
6.64e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 133.70 E-value: 6.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYP------SRPDVVV--MEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN- 492
Cdd:COG4608 8 LEVRDLKKHFPvrgglfGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 493 --VRWLRQQIALVSQEPtlFAC-----TIYDNIRHGL----IGTKweseseeqqreriyeAARKANAHDFITSL---PEG 558
Cdd:COG4608 88 reLRPLRRRMQMVFQDP--YASlnprmTVGDIIAEPLrihgLASK---------------AERRERVAELLELVglrPEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 559 YETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALDtKSegvVQAA-----LEVAAE-GRTTITIAHRLSTIK 632
Cdd:COG4608 151 ADRYPHE----FSGGQRQRIGIARALALNPKLIVCDEPVSALD-VS---IQAQvlnllEDLQDElGLTYLFISHDLSVVR 222
|
250 260
....*....|....*....|...
gi 164423939 633 D-AHNIVVMAQGRIVEQGTHAEL 654
Cdd:COG4608 223 HiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
422-655 |
1.11e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDistlnVRWLR 497
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTllkaILGLL----PPTSGTVRLFGKP-----PRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 QQIALVSQEPTL---FACTIYDNIRHGLIGTK-WESESEEQQRERIYEAARKANAHDFItslpegyETNVGErgflLSGG 573
Cdd:COG1121 75 RRIGYVPQRAEVdwdFPITVRDVVLMGRYGRRgLFRRPSRADREAVDEALERVGLEDLA-------DRPIGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 574 QKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEqGTH 651
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLrELRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPP 222
|
....
gi 164423939 652 AELL 655
Cdd:COG1121 223 EEVL 226
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
769-1065 |
1.44e-33 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 131.53 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 769 GIFFSAICGAGNPTQAVFFAKLISSLsrpivneeIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKCSERLIHRVR 848
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTI--------IKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 849 DMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIPILL 928
Cdd:cd18557 73 RDLFSSLLRQEIAFFDK--HKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 929 GCG-FYRFWMIAHYqRRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSL 1007
Cdd:cd18557 151 IASkIYGRYIRKLS-KEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1008 MFLAFALGFWYGGTLIAKHEY---DMFTfFIVFSSVIfgAQSAGSVFSFAPDMGKATEAAR 1065
Cdd:cd18557 230 IYLSLLLVLWYGGYLVLSGQLtvgELTS-FILYTIMV--ASSVGGLSSLLADIMKALGASE 287
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
427-649 |
2.16e-33 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 127.55 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQe 506
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 ptlfactiydnirhgligtkweseseeqqreriyeAARKANAHDFItslpegyetnvgERGFL-LSGGQKQRIAIARAIV 585
Cdd:cd03214 81 -----------------------------------ALELLGLAHLA------------DRPFNeLSGGERQRVLLARALA 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 586 SDPKILLLDEATSALDTKSegvvQAAL------EVAAEGRTTITIAHRLS-TIKDAHNIVVMAQGRIVEQG 649
Cdd:cd03214 114 QEPPILLLDEPTSHLDIAH----QIELlellrrLARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1094-1322 |
2.75e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 128.72 E-value: 2.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeqpvLRgLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEyRSfIA 1173
Cdd:COG3840 2 LRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP-VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLY-QGTVRENIILGAN-----NDVTDEQIKFACQEANIYDFIMSLPdgmntlvgskgALLSGGQKQRIAIARA 1247
Cdd:COG3840 75 MLFQENNLFpHLTVAQNIGLGLRpglklTAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1248 LIRDPKILLLDEATSALD----SESEHVVQAALDKaaKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELMKKN 1322
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
112-395 |
8.02e-33 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 129.60 E-value: 8.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 112 LMTVIFGNLQGTFQNYFAG----VTTYDDFTDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMR 187
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGrlidTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 188 QNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFII 267
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 268 KFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQG 347
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 164423939 348 SRFLLSGDTELRKILTVMMSVMIGAFNLGNIAPNLQAFVTALGAAAKI 395
Cdd:cd18557 242 GYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
422-658 |
1.09e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.18 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvvMEdVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRwlRQQIA 501
Cdd:COG3840 2 LRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFA-CTIYDNIRHGL-IGTKweseSEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIA 579
Cdd:COG3840 75 MLFQENNLFPhLTVAQNIGLGLrPGLK----LTAEQRAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 580 IARAIVSDPKILLLDEATSALDT--KSEGVvqaAL--EVAAE-GRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAE 653
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPalRQEML---DLvdELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
....*
gi 164423939 654 LLAKR 658
Cdd:COG3840 217 LLDGE 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1094-1313 |
1.66e-32 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 126.22 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEyRSfIA 1173
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLY-QGTVRENIILG-----ANNDVTDEQIKFACQEANIydfimslpdgmNTLVGSKGALLSGGQKQRIAIARA 1247
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlklrkVPKDEIDERVREVAELLQI-----------EHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1248 LIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAH-RLSTIQKADIIYVFDQGRIVEQG 1313
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
423-649 |
1.77e-32 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 126.11 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 423 RLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDvdistLNVRWLRQ 498
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTllkaILGLL----KPTSGSIRVFG-----KPLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 499 QIALVSQEPTL---FACTIYDNIRHGLIGTKWESEseeqqrerIYEAARKA---NAHDFitslpegyetnVGERGFL--- 569
Cdd:cd03235 69 RIGYVPQRRSIdrdFPISVRDVVLMGLYGHKGLFR--------RLSKADKAkvdEALER-----------VGLSELAdrq 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 ---LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSE-GVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRI 645
Cdd:cd03235 130 igeLSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQeDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
....
gi 164423939 646 VEQG 649
Cdd:cd03235 210 VASG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
436-649 |
1.86e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.46 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 DVVVMEDVSLVIPAGKTTALVGASGSGKST-------IVGLVERFYkpIEGKVYLDDVDI--STLNVRWLRQQIALVSQE 506
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTllrclnrMNDLIPGAR--VEGEILLDGEDIydPDVDVVELRRRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 PTLFACTIYDNIRHGLigtkweseseeqqreRIYEAARKANAHDFI-TSLpegyeTNVG----------ERGFLLSGGQK 575
Cdd:COG1117 101 PNPFPKSIYDNVAYGL---------------RLHGIKSKSELDEIVeESL-----RKAAlwdevkdrlkKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 576 QRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEgRTTITI-------AHRLStikdaHNIVVMAQGRIVEQ 648
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEF 234
|
.
gi 164423939 649 G 649
Cdd:COG1117 235 G 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1111-1320 |
1.93e-32 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 126.78 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEY------RSFialvsQEPTLYQG 1184
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlgigRTF-----QIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 -TVRENIILGANND--VTDEQIKFACQEANIYDFIMS------LPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKIL 1255
Cdd:cd03219 90 lTVLENVMVAAQARtgSGLLLARARREEREARERAEEllervgLADLADRPAGE----LSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1256 LLDEATSAL-DSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELMK 1320
Cdd:cd03219 166 LLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1094-1311 |
1.99e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.94 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrPEQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREISSLNVNE--- 1167
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTllkLLYGEER---PTSGQVLVNGQDLSRLKRREipy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1168 YRSFIALVSQE-PTLYQGTVRENI-----ILGANNDVTDEQIKFACQEANIYDFIMSLPDgmntlvgskgaLLSGGQKQR 1241
Cdd:COG2884 77 LRRRIGVVFQDfRLLPDRTVYENValplrVTGKSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1242 IAIARALIRDPKILLLDEATSALDSE-SEHVVQaALDKAAKGRTTIAVA-HRLSTIQKADI-IYVFDQGRIVE 1311
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPEtSWEIME-LLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
405-667 |
2.10e-32 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 127.33 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 405 IDSSSEEGgkLENVVGTIRLENIKHIYPS--RPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVY 482
Cdd:cd03288 5 ISGSSNSG--LVGLGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 483 LDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGLIGTKweseseeqqrERIYEAARKANAHDFITSLPEGYETN 562
Cdd:cd03288 80 IDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTD----------DRLWEALEIAQLKNMVKSLPGGLDAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 563 VGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQ 642
Cdd:cd03288 150 VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSR 229
|
250 260
....*....|....*....|....*.
gi 164423939 643 GRIVEQGTHAELLAKR-GAYYKLVTA 667
Cdd:cd03288 230 GILVECDTPENLLAQEdGVFASLVRT 255
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
422-654 |
2.30e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.83 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGlverFYKPIEGKVYLDDVDISTLNVRwlR 497
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTllrmIAG----FETPDSGRILLDGRDVTGLPPE--K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 QQIALVSQEPTLFA-CTIYDNIRHGLigtkweseseeqQRERIYEAARKANAHDFI--TSLpEGYET-NVGErgflLSGG 573
Cdd:COG3842 77 RNVGMVFQDYALFPhLTVAENVAFGL------------RMRGVPKAEIRARVAELLelVGL-EGLADrYPHQ----LSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 574 QKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQaaLEVAA----EGRTTITIAHRLS---TIkdAHNIVVMAQGRIV 646
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMR--EELRRlqreLGITFIYVTHDQEealAL--ADRIAVMNDGRIE 215
|
....*...
gi 164423939 647 EQGTHAEL 654
Cdd:COG3842 216 QVGTPEEI 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
427-645 |
2.36e-32 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 125.72 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDI--STLNVRWLRQQIALVS 504
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 505 QEPTLFA-CTIYDNIRHGLIGTKWESESeeqqreriyEAARKANAH-------DFITSLPegyetnvGErgflLSGGQKQ 576
Cdd:cd03262 83 QQFNLFPhLTVLENITLAPIKVKGMSKA---------EAEERALELlekvglaDKADAYP-------AQ----LSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 577 RIAIARAIVSDPKILLLDEATSALDTKsegVVQAALEV----AAEGRTTITIAHRLSTIKD-AHNIVVMAQGRI 645
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
420-654 |
2.61e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.81 E-value: 2.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 420 GTIRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLverfYKPIEGKVYLDDVDISTLNVRw 495
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrmIAGL----EDPTSGEILIGGRDVTDLPPK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 lRQQIALVSQEPTLF-ACTIYDNIRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQ 574
Cdd:COG3839 74 -DRNIAMVFQSYALYpHMTVYENIAFPL---KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQ-----------LSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALDTKSEgvVQAALEVAA----EGRTTI----------TIAHRlstikdahnIVVM 640
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAKLR--VEMRAEIKRlhrrLGTTTIyvthdqveamTLADR---------IAVM 207
|
250
....*....|....
gi 164423939 641 AQGRIVEQGTHAEL 654
Cdd:COG3839 208 NDGRIQQVGTPEEL 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1094-1317 |
2.89e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 129.15 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPT-RPEQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREISSLNVNEYR 1169
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SF---IALVSQEPTLYQG-TVRENIILG---ANndVTDEQIKFACQEaniydfimsLPDgmntLVG------SKGALLSG 1236
Cdd:PRK11153 79 KArrqIGMIFQHFNLLSSrTVFDNVALPlelAG--TPKAEIKARVTE---------LLE----LVGlsdkadRYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1237 GQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTI-QKADIIYVFDQGRIVEQG 1313
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQG 223
|
....
gi 164423939 1314 THSE 1317
Cdd:PRK11153 224 TVSE 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1094-1313 |
3.77e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 126.30 E-value: 3.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYD--P---LSGGIFIDGREI--SSLNVN 1166
Cdd:COG1117 12 IEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1167 EYRSFIALVSQEPTLYQGTVRENIILGA------NNDVTDEQIKFACQEANIYDfimSLPDGMNtlvgSKGALLSGGQKQ 1240
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgikSKSELDEIVEESLRKAALWD---EVKDRLK----KSALGLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1241 RIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLstiQKA----DIIYVFDQGRIVEQG 1313
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNM---QQAarvsDYTAFFYLGELVEFG 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1094-1320 |
5.05e-32 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 127.86 E-value: 5.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQ-PVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPL---SGGIFIDGREISSLNVNEYR 1169
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SF----IALVSQEPT-----LYqgTVRENII--LGANNDVTDEQIKfacQEAniydfimslpDGMNTLVGSKGAL----- 1233
Cdd:COG0444 82 KIrgreIQMIFQDPMtslnpVM--TVGDQIAepLRIHGGLSKAEAR---ERA----------IELLERVGLPDPErrldr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1234 ----LSGGQKQRIAIARALIRDPKILLLDEATSALDsesehV-VQAA-LD-----KAAKGRTTIAVAHRLSTIQK-ADII 1301
Cdd:COG0444 147 ypheLSGGMRQRVMIARALALEPKLLIADEPTTALD-----VtIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRV 221
|
250
....*....|....*....
gi 164423939 1302 YVFDQGRIVEQGTHSELMK 1320
Cdd:COG0444 222 AVMYAGRIVEEGPVEELFE 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
422-653 |
6.93e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.39 E-value: 6.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN---VRWLRQ 498
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 499 QIALVSQE----PTLfacTIYDNIRHGL--IGTKWEseseeqqreriyEAARKANA-------HDFITSLPEgyetnvgE 565
Cdd:COG2884 80 RIGVVFQDfrllPDR---TVYENVALPLrvTGKSRK------------EIRRRVREvldlvglSDKAKALPH-------E 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 566 rgflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAEGrTTITIA-HRLSTIKDA-HNIVVMAQ 642
Cdd:COG2884 138 ----LSGGEQQRVAIARALVNRPELLLADEPTGNLDPEtSWEIMELLEEINRRG-TTVLIAtHDLELVDRMpKRVLELED 212
|
250
....*....|.
gi 164423939 643 GRIVEQGTHAE 653
Cdd:COG2884 213 GRLVRDEARGV 223
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
766-1027 |
8.00e-32 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 126.51 E-value: 8.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 766 MLVGIFFSAIcgagnptqAVFFAKLISSLSRPIVNEEIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKCSERLIH 845
Cdd:cd07346 1 LLLALLLLLL--------ATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 846 RVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIP 925
Cdd:cd07346 73 DLRRDLFRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 926 ILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASN 1005
Cdd:cd07346 151 LYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIG 230
|
250 260
....*....|....*....|..
gi 164423939 1006 SLMFLAFALGFWYGGTLIAKHE 1027
Cdd:cd07346 231 LLTALGTALVLLYGGYLVLQGS 252
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
148-687 |
8.08e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 136.02 E-value: 8.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 148 FVY--LAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLTLQ 225
Cdd:PLN03130 957 LIYalLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLG 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 226 ALATFIAAFV-IGFV---SFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSvADEVISSVRnaiAFGTQD 301
Cdd:PLN03130 1037 QIFQLLSTFVlIGIVstiSLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGE-ALNGLSTIR---AYKAYD 1112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 302 RLAR----------RYD-AHLTRAEHFGFRLKGSIGVMVagmmtvlYLNYGLAFWQGSRfllsgdTELRKILTVMMSVMI 370
Cdd:PLN03130 1113 RMAEingrsmdnniRFTlVNMSSNRWLAIRLETLGGLMI-------WLTASFAVMQNGR------AENQAAFASTMGLLL 1179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 371 gAFNLgNIAPNLQAFVTALGAAAKIYNTIDR-ESPIDSSSEEGGKLEN--------VVGTIRLENIKHIYpsRPDVV-VM 440
Cdd:PLN03130 1180 -SYAL-NITSLLTAVLRLASLAENSLNAVERvGTYIDLPSEAPLVIENnrpppgwpSSGSIKFEDVVLRY--RPELPpVL 1255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 441 EDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNI-- 518
Cdd:PLN03130 1256 HGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLdp 1335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 519 --RHGligtkweseseeqqRERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEA 596
Cdd:PLN03130 1336 fnEHN--------------DADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 597 TSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAK-RGAYYKLV--TAQAIA-- 671
Cdd:PLN03130 1402 TAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNeGSAFSKMVqsTGAANAqy 1481
|
570 580
....*....|....*....|....
gi 164423939 672 --------AVNEMTAEEEAALDQQ 687
Cdd:PLN03130 1482 lrslvfggDEDRLAREESKALDGQ 1505
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
439-657 |
1.25e-31 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 124.37 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRwlRQQIALVSQEPTLFA-CTIYDN 517
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 518 IRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLPEgyetnvgergfLLSGGQKQRIAIARAIVSDPKILLLDEAT 597
Cdd:cd03299 92 IAYGL---KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 598 SALDTKSEGVVQAALEVAAE--GRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAELLAK 657
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1094-1318 |
1.40e-31 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 123.89 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTrpeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREIssLNVNEYRSFIA 1173
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLY-QGTVRENIILGANNDVTDEQ-IKFACQEAniYDFImslpdGMNTLVGSKGALLSGGQKQRIAIARALIRD 1251
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAFGLRLKKLPKAeIKERVAEA--LDLV-----QLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1252 PKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLS-TIQKADIIYVFDQGRIVEQGTHSEL 1318
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
437-657 |
1.51e-31 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 125.06 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 437 VVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQ----QIALVSQEPTLFA- 511
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPh 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 512 CTIYDNIRHGLigtkweseseeqQRERIYEAARKANA---------HDFITSLPegyetnvGErgflLSGGQKQRIAIAR 582
Cdd:cd03294 117 RTVLENVAFGL------------EVQGVPRAEREERAaealelvglEGWEHKYP-------DE----LSGGMQQRVGLAR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 583 AIVSDPKILLLDEATSALDTKSEGVVQAALE--VAAEGRTTITIAHRLS-TIKDAHNIVVMAQGRIVEQGTHAELLAK 657
Cdd:cd03294 174 ALAVDPDILLMDEAFSALDPLIRREMQDELLrlQAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
422-645 |
1.72e-31 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 121.74 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTlNVRWLRQQIA 501
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFA-CTIYDNIRhgligtkweseseeqqreriyeaarkanahdfitslpegyetnvgergflLSGGQKQRIAI 580
Cdd:cd03230 77 YLPEEPSLYEnLTVRENLK--------------------------------------------------LSGGMKQRLAL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 581 ARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRI 645
Cdd:cd03230 107 AQALLHDPELLILDEPTSGLDPESrREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1094-1301 |
1.78e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 122.97 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRyptRPEQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREISSlNVNEYRS 1170
Cdd:COG4133 3 LEAENLSCR---RGERLLFSGLSFTLAAGEALALTGPNGSGKTTllrILAGLLP---PSAGEVLWNGEPIRD-AREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1171 FIALVSQEPTLYQG-TVRENIILGA---NNDVTDEQIKFACQEaniydfiMSLPDGMNTLVGSkgalLSGGQKQRIAIAR 1246
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRFWAalyGLRADREAIDEALEA-------VGLAGLADLPVRQ----LSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1247 ALIRDPKILLLDEATSALDSESEHVVQAAL-DKAAKGRTTIAVAHRLSTIQKADII 1301
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1094-1318 |
2.35e-31 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 123.00 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlNVNEYRSFIA 1173
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQG-TVRENIIL-----GanndVTDEQIKfacQEANIYDFIMSLPDGMNTLVGSkgalLSGGQKQRIAIARA 1247
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkG----LPKSEIK---EEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1248 LIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHrlsTIQKADI----IYVFDQGRIVEQGTHSEL 1318
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH---SMDEAEAlcdrIAIMSDGKLRCIGSPQEL 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1095-1319 |
2.83e-31 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 123.17 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1095 EFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEY-RSFIA 1173
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQE----PTLyqgTVRENIILGANNDVTDEQIKFACQEanIYDFimsLPDgMNTLVGSKGALLSGGQKQRIAIARALI 1249
Cdd:COG0410 82 YVPEGrrifPSL---TVEENLLLGAYARRDRAEVRADLER--VYEL---FPR-LKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1250 RDPKILLLDEATSALdseSEHVVQ---AALDKAAKGRTTIAV----AHRLSTIqkADIIYVFDQGRIVEQGTHSELM 1319
Cdd:COG0410 153 SRPKLLLLDEPSLGL---APLIVEeifEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELL 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1061-1329 |
2.97e-31 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 133.92 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1061 TEAARDLKEL--FDRKPTVDTWSNEGDLIKQVDG-TIEFRDVHFRYpTRPEQPVLRGLNLSIQPGQYVALVGASGCGKST 1137
Cdd:TIGR00957 601 VQASVSLKRLriFLSHEELEPDSIERRTIKPGEGnSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1138 TIALLERFYDPLSGGIFIDGReisslnvneyrsfIALVSQEPTLYQGTVRENIILG-ANNDVTDEQIKFACqeANIYDFI 1216
Cdd:TIGR00957 680 LLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGkALNEKYYQQVLEAC--ALLPDLE 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1217 MsLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSeseHVVQAALDKAA------KGRTTIAVAH 1290
Cdd:TIGR00957 745 I-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA---HVGKHIFEHVIgpegvlKNKTRILVTH 820
|
250 260 270
....*....|....*....|....*....|....*....
gi 164423939 1291 RLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELV 1329
Cdd:TIGR00957 821 GISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1094-1331 |
3.33e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 124.46 E-value: 3.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEP--TLYQGTVRENIILGANND-VTDEQIKFACQEAniYDFImslpdGMNTLVGSKGALLSGGQKQRIAIARALIR 1250
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKgIPHEEMKERVNEA--LELV-----GMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1251 DPKILLLDEATSALDSESE----HVVQAALDKaaKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMkknGRYA 1326
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF---SRGN 232
|
....*
gi 164423939 1327 ELVNL 1331
Cdd:PRK13650 233 DLLQL 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1094-1313 |
3.43e-31 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 122.30 E-value: 3.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYvALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlNVNEYRSFIA 1173
Cdd:cd03264 1 LQLENLTKRYG---KKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQG-TVRENI-ILGANNDVTDEQIKFACQEA----NIYDFimslpdgMNTLVGSkgalLSGGQKQRIAIARA 1247
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLdYIAWLKGIPSKEVKARVDEVlelvNLGDR-------AKKKIGS----LSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1248 LIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1093-1318 |
6.97e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 125.26 E-value: 6.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTT---IALLERfydPLSGGIFIDGREI-SSLNVNEY 1168
Cdd:COG1118 2 SIEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLlriIAGLET---PDSGRIVLNGRDLfTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1169 RsfIALVSQE----PTLyqgTVRENIILG---------ANNDVTDEQIKfacqeaniydfIMSLPDgmntLVGSKGALLS 1235
Cdd:COG1118 76 R--VGFVFQHyalfPHM---TVAENIAFGlrvrppskaEIRARVEELLE-----------LVQLEG----LADRYPSQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1236 GGQKQRIAIARALIRDPKILLLDEATSALDSesehvvqaaldKAAK-------------GRTTIAVAH------RLstiq 1296
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDEPFGALDA-----------KVRKelrrwlrrlhdelGGTTVFVTHdqeealEL---- 200
|
250 260
....*....|....*....|..
gi 164423939 1297 kADIIYVFDQGRIVEQGTHSEL 1318
Cdd:COG1118 201 -ADRVVVMNQGRIEQVGTPDEV 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
421-653 |
7.08e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 123.62 E-value: 7.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIY-PSRP-DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDIS--TLNVRWL 496
Cdd:PRK13637 2 SIKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 497 RQQIALVSQEP--TLFACTIYDNIRHGLIGtkwesesEEQQRERIYEAARKANAhdfITSLPegYETNVGERGFLLSGGQ 574
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIEKDIAFGPIN-------LGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAE--GRTTITIAHRLSTI-KDAHNIVVMAQGRIVEQGTH 651
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTP 229
|
..
gi 164423939 652 AE 653
Cdd:PRK13637 230 RE 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1094-1310 |
7.52e-31 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 119.46 E-value: 7.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTrpeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSF-I 1172
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQeptlyqgtvreniilganndvtdeqikfacqeaniydfimslpdgmntlvgskgalLSGGQKQRIAIARALIRDP 1252
Cdd:cd03216 78 AMVYQ--------------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1253 KILLLDEATSAL-DSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIV 1310
Cdd:cd03216 102 RLLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
421-654 |
9.38e-31 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 121.68 E-value: 9.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRwlRQQI 500
Cdd:cd03296 2 SIEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEPTLFA-CTIYDNIRHGLigtkweseSEEQQRERIYEAARKANAHDFI-----TSLPEGYETNvgergflLSGGQ 574
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGL--------RVKPRSERPPEAEIRAKVHELLklvqlDWLADRYPAQ-------LSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAE-GRTTITIAHRLS-TIKDAHNIVVMAQGRIVEQGTH 651
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLrRLHDElHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTP 221
|
...
gi 164423939 652 AEL 654
Cdd:cd03296 222 DEV 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
436-656 |
9.93e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 121.00 E-value: 9.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 DVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLNV-RWLRQQIALVSQEPTLF 510
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTllktIMGLL----PPRSGSIRFDGRDITGLPPhERARAGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 511 A-CTIYDNIRHGLigtkweseseeqqreriyEAARKANAHDfitSLPEGYET--NVGER----GFLLSGGQKQRIAIARA 583
Cdd:cd03224 88 PeLTVEENLLLGA------------------YARRRAKRKA---RLERVYELfpRLKERrkqlAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 584 IVSDPKILLLDEATSALDTK-SEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAELLA 656
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKiVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1111-1329 |
1.04e-30 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 121.67 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRsfIALVSQEPTLY-QGTVREN 1189
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1190 IILGANNdVTDEQIKFACQEANIYDFImslpdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESE 1269
Cdd:cd03299 92 IAYGLKK-RKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1270 HVVQAALDKAAK--GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELMKK--NGRYAELV 1329
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKpkNEFVAEFL 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1094-1313 |
3.34e-30 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 119.52 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQpvlrgLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEyRSfIA 1173
Cdd:cd03298 1 VRLDKIRFSYGEQPMH-----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-RP-VS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQG-TVRENIILGAN-----NDVTDEQIKFACQEANIYDFIMSLPDGmntlvgskgalLSGGQKQRIAIARA 1247
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLSpglklTAEDRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1248 LIRDPKILLLDEATSALDSESEHVVQAALDK--AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
437-673 |
3.35e-30 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 127.11 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 437 VVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfykPIEGKVYLDDVDISTLN---VRWLRQQIALVSQEPtl 509
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 510 FAC-----TIYDNIRHGL----IGTKweseseeqqreriyEAARKANAhdfITSLPEgyetnVG-ERGFL------LSGG 573
Cdd:COG4172 372 FGSlsprmTVGQIIAEGLrvhgPGLS--------------AAERRARV---AEALEE-----VGlDPAARhrypheFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 574 QKQRIAIARAIVSDPKILLLDEATSALDtKSegvVQAA-LEVAAE-----GRTTITIAHRLSTIKD-AHNIVVMAQGRIV 646
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALD-VS---VQAQiLDLLRDlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVV 505
|
250 260
....*....|....*....|....*...
gi 164423939 647 EQGTHAELLAK-RGAYyklvTAQAIAAV 673
Cdd:COG4172 506 EQGPTEQVFDApQHPY----TRALLAAA 529
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1094-1319 |
4.67e-30 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 120.19 E-value: 4.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGG-IFIDGREISSLNVNEYRSFI 1172
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQEPTLY---QGTVRENII------LGANNDVTDEQIKFACQEANIYdfimslpdGMNTLVGSKGALLSGGQKQRIA 1243
Cdd:COG1119 81 GLVSPALQLRfprDETVLDVVLsgffdsIGLYREPTDEQRERARELLELL--------GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1244 IARALIRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIA-VAHRLStiqkaDII------YVFDQGRIVEQGTH 1315
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPpgithvLLLKDGRVVAAGPK 227
|
....
gi 164423939 1316 SELM 1319
Cdd:COG1119 228 EEVL 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1094-1299 |
6.96e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 119.05 E-value: 6.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQGTVRENIILganndvtDEQI-KFACQEANIYDFIM--SLPDgmNTLVGSKGAlLSGGQKQRIAIARALIR 1250
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIF-------PWQIrNQQPDPAIFLDDLErfALPD--TILTKNIAE-LSGGEKQRISLIRNLQF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1251 DPKILLLDEATSALDSESEHVVQAALDKAA--KGRTTIAVAHRLSTIQKAD 1299
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHAD 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
422-656 |
9.69e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.12 E-value: 9.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYP--SRPDVvvmEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQ 499
Cdd:PRK13635 6 IRVEHISFRYPdaATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEP--TLFACTIYDNIRHGL--IGTKwesesEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQK 575
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLenIGVP-----REEMVERVDQALRQVGMEDFLNREPHR-----------LSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 576 QRIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEGR-TTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAE 653
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGrREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
...
gi 164423939 654 LLA 656
Cdd:PRK13635 227 IFK 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
437-656 |
1.69e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 117.92 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 437 VVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWL-RQQIALVSQEPTLFA-CTI 514
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPeLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 515 YDNIRHGLIGTKWESESEEQQRERIYEAARKANAH-DFITsLPEGYETNVGErgflLSGGQKQRIAIARAIVSDPKILLL 593
Cdd:cd03219 93 LENVMVAAQARTGSGLLLARARREEREARERAEELlERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 594 DEATSAL-DTKSEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAELLA 656
Cdd:cd03219 168 DEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
422-654 |
2.39e-29 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 117.72 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDIstLNVRWLRQQIA 501
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFA-CTIYDNIRHGLigtkweseseeqQRERIYEAARKANAHDFI--TSLpEGYETNVGERgflLSGGQKQRI 578
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGL------------RLKKLPKAEIKERVAEALdlVQL-EGYANRKPSQ---LSGGQQQRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 579 AIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAE-GRTTITIAHRLS---TIKDahNIVVMAQGRIVEQGTHAE 653
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQLELkRLQKElGITFVFVTHDQEealTMSD--RIAVMNKGKIQQIGTPEE 217
|
.
gi 164423939 654 L 654
Cdd:cd03300 218 I 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
427-649 |
2.42e-29 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 116.97 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDIStlNVRWLRQQIALVSQE 506
Cdd:cd03301 3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 PTLFA-CTIYDNIRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIAIARAIV 585
Cdd:cd03301 81 YALYPhMTVYDNIAFGL---KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 586 SDPKILLLDEATSALDTKSEgvVQAALEV----AAEGRTTITIAH-RLSTIKDAHNIVVMAQGRIVEQG 649
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLR--VQMRAELkrlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1090-1321 |
2.66e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 119.13 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1090 VDGTIEFRDVHFRYPTRPEqPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGG---IFIDGREISSLNVN 1166
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1167 EYRSFIALVSQEP--TLYQGTVRENIILG-ANNDVTDEQIKFACQEAniydfimsLPD-GMNTLVGSKGALLSGGQKQRI 1242
Cdd:PRK13640 81 DIREKVGIVFQNPdnQFVGATVGDDVAFGlENRAVPRPEMIKIVRDV--------LADvGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1243 AIARALIRDPKILLLDEATSALDSES-EHVVQAALD-KAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMK 1320
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGkEQILKLIRKlKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
.
gi 164423939 1321 K 1321
Cdd:PRK13640 233 K 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1093-1318 |
6.62e-29 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 116.67 E-value: 6.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREISSLNVNEYR 1169
Cdd:cd03296 2 SIEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTllrLIAGLER---PDSGTILFGGEDATDVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 sfIALVSQEPTLYQG-TVRENIILGanndVTDEQIKFACQEANIYDFIMSLPD--GMNTLVGSKGALLSGGQKQRIAIAR 1246
Cdd:cd03296 76 --VGFVFQHYALFRHmTVFDNVAFG----LRVKPRSERPPEAEIRAKVHELLKlvQLDWLADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1247 ALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLS-TIQKADIIYVFDQGRIVEQGTHSEL 1318
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1108-1319 |
8.34e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 116.65 E-value: 8.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQG-TV 1186
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 RENIILGANNDVT--------DEQ-IKFACQEANIydfimslpdgmNTLVGSKGALLSGGQKQRIAIARALIRDPKILLL 1257
Cdd:PRK11231 94 RELVAYGRSPWLSlwgrlsaeDNArVNQAMEQTRI-----------NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1258 DEATSALDseSEHvvQAALDK-----AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELM 1319
Cdd:PRK11231 163 DEPTTYLD--INH--QVELMRlmrelNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1091-1296 |
8.66e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 123.38 E-value: 8.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1091 DGTIEFRDVHFRYPTrpEQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERFYdplSGGIFI-DGREIsslnvn 1166
Cdd:COG4178 360 DGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKSTllrAIAGLWPYG---SGRIARpAGARV------ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1167 eyrsfiALVSQEPTLYQGTVRENIIL-GANNDVTDEQIKFACQEANIYDFIMSLPDGMNTlvgskGALLSGGQKQRIAIA 1245
Cdd:COG4178 429 ------LFLPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERLDEEADW-----DQVLSLGEQQRLAFA 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1246 RALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQ 1296
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAA 548
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1094-1289 |
1.56e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 114.81 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE---YRS 1170
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1171 FIALVSQE-PTLYQGTVRENI-----ILGANNDVTDEQIKFACQEANIYDFIMSLPDGmntlvgskgalLSGGQKQRIAI 1244
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVafaleVTGVPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 164423939 1245 ARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVA 1289
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1090-1322 |
3.20e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.60 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1090 VDGTIEFRDVHFRYPTRPEqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYR 1169
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SFIALVSQEP--TLYQGTVRENIILGANN-----DVTDEQIKFACQEANIYDFIMSLPDGmntlvgskgalLSGGQKQRI 1242
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGPVNmgldkDEVERRVEEALKAVRMWDFRDKPPYH-----------LSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1243 AIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVA-HRLS-TIQKADIIYVFDQGRIVEQGTHSELMK 1320
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
..
gi 164423939 1321 KN 1322
Cdd:PRK13647 228 ED 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1094-1319 |
3.42e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.42 E-value: 3.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE--YRSF 1171
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1172 IALVSQEPTLY-QGTVRENIILGAnndvtdEQIKFAC-QEANiyDFIMSLPD--GMNTLVGSKGALLSGGQKQRIAIARA 1247
Cdd:PRK09493 79 AGMVFQQFYLFpHLTALENVMFGP------LRVRGASkEEAE--KQARELLAkvGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 1248 LIRDPKILLLDEATSALDSESEH-VVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVF-DQGRIVEQGTHSELM 1319
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHeVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFiDKGRIAEDGDPQVLI 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1094-1318 |
4.28e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.12 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTrpeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSF-I 1172
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQEPTLYQG-TVRENIILG---ANNDVTD--EQIKFACQEANIYDFIMSLpdgmNTLVGSkgalLSGGQKQRIAIAR 1246
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGrepRRGGLIDwrAMRRRARELLARLGLDIDP----DTPVGD----LSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 1247 ALIRDPKILLLDEATSAL-DSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:COG1129 154 ALSRDARVLILDEPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
117-1292 |
4.58e-28 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 123.48 E-value: 4.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 117 FGNLQGTFQNYFAG--VTTYDDFTDElARLVLYfvYLAIGE---FVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIG 191
Cdd:TIGR01271 91 FGEATKAVQPLLLGriIASYDPFNAP-EREIAY--YLALGLcllFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 192 F----FDKLGAGEVTTRITADTNLIQEGIsekvgltlqALATFI------AAFVIGFVsfWKLTLIL----LSTVVALTL 257
Cdd:TIGR01271 168 LssrvLDKISTGQLVSLLSNNLNKFDEGL---------ALAHFVwiaplqVILLMGLI--WELLEVNgfcgLGFLILLAL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 258 VMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRLA------RRYDAHLTRAEHFgFRLKGSIGVMVAG 331
Cdd:TIGR01271 237 FQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEkiikniRQDELKLTRKIAY-LRYFYSSAFFFSG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 332 MMTVLYLNYGLAFWQGsrfllsgdTELRKILTVMMSVMIGAFNLGNIAP-NLQAFVTALGAAAKI-------------YN 397
Cdd:TIGR01271 316 FFVVFLSVVPYALIKG--------IILRRIFTTISYCIVLRMTVTRQFPgAIQTWYDSLGAITKIqdflckeeyktleYN 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 398 TIDRE---SPIDSSSEEG-GKLenvVGTIRLENIKHIYPSRPDVV-----------VMEDVSLVIPAGKTTALVGASGSG 462
Cdd:TIGR01271 388 LTTTEvemVNVTASWDEGiGEL---FEKIKQNNKARKQPNGDDGLffsnfslyvtpVLKNISFKLEKGQLLAVAGSTGSG 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 463 KSTIVGLVERFYKPIEGKVYLDDvdistlnvrwlrqQIALVSQEPTLFACTIYDNIRHGLIGTKWEseseeqqreriYEA 542
Cdd:TIGR01271 465 KSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFGLSYDEYR-----------YTS 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 543 ARKA-NAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEG-VVQAALEVAAEGRT 620
Cdd:TIGR01271 521 VIKAcQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKT 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 621 TITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLVTAqaIAAVNEMTAEEEAAL--------DQQEEAAL 692
Cdd:TIGR01271 601 RILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLG--LEAFDNFSAERRNSIltetlrrvSIDGDSTV 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 693 IR---------KATRNSQKEGGAAGYVEDP----------------------EDNIAEKLDRSKSQQSVSSVAIAARKKE 741
Cdd:TIGR01271 679 FSgpetikqsfKQPPPEFAEKRKQSIILNPiasarkfsfvqmgpqkaqattiEDAVREPSERKFSLVPEDEQGEESLPRG 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 742 EPKEYGL-------WTLIKLIASFNKKEWHMMLVGIFFSAICGAgnpTQAVFFAKLISSLSRPI-------VNEEI---- 803
Cdd:TIGR01271 759 NQYHHGLqhqaqrrQSVLQLMTHSNRGENRREQLQTSFRKKSSI---TQQNELASELDIYSRRLskdsvyeISEEIneed 835
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 804 -------RASIKSDASFWC--LMY------LMLALVQCL-------AFSVQG-WLFAKCSER------------------ 842
Cdd:TIGR01271 836 lkecfadERENVFETTTWNtyLRYittnrnLVFVLIFCLviflaevAASLLGlWLITDNPSApnyvdqqhanasspdvqk 915
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 843 ---------------------------------LIH-------RVRDMAFRSFLRQDVEFFDRDEnsAGALTSFLSTETT 882
Cdd:TIGR01271 916 pviitptsayyifyiyvgtadsvlalgffrglpLVHtlltvskRLHEQMLHSVLQAPMAVLNTMK--AGRILNRFTKDMA 993
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 883 HVAGLSGVTLGTIIMVLTTLIAA-CTVALALGWKLalvcIATIPILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAIT 961
Cdd:TIGR01271 994 IIDDMLPLTLFDFIQLTLIVLGAiFVVSVLQPYIF----IAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLIT 1069
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 962 AMR---TVASLTReqdvlQHYKDSL---AKQQHASLISVLKSSL-LFAASNSLMFLAF--ALGFWYGGT----------L 1022
Cdd:TIGR01271 1070 SLKglwTIRAFGR-----QSYFETLfhkALNLHTANWFLYLSTLrWFQMRIDIIFVFFfiAVTFIAIGTnqdgegevgiI 1144
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1023 IAKHEYDMFTF-FIVFSSVIFGA--QSAGSVFSFApDM----------GKATEAARDLkeLFDRKPTVDTWSNEGDLIKQ 1089
Cdd:TIGR01271 1145 LTLAMNILSTLqWAVNSSIDVDGlmRSVSRVFKFI-DLpqeeprpsggGGKYQLSTVL--VIENPHAQKCWPSGGQMDVQ 1221
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1090 vdgtiefrDVHFRYpTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPlSGGIFIDGREISSLNVNEYR 1169
Cdd:TIGR01271 1222 --------GLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWR 1291
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SFIALVSQEPTLYQGTVRENiiLGANNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALI 1249
Cdd:TIGR01271 1292 KAFGVIPQKVFIFSGTFRKN--LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSIL 1369
|
1370 1380 1390 1400
....*....|....*....|....*....|....*....|...
gi 164423939 1250 RDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRL 1292
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1108-1320 |
5.03e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.53 E-value: 5.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVN--EYRSFIALVSQEP--TLYQ 1183
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIRKKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1184 GTVRENIILGANN-DVTDEQIKFACQEAniydfimslpdgMNTLVGSKGAL-------LSGGQKQRIAIARALIRDPKIL 1255
Cdd:PRK13637 99 ETIEKDIAFGPINlGLSEEEIENRVKRA------------MNIVGLDYEDYkdkspfeLSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1256 LLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELMK 1320
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
422-646 |
8.03e-28 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 110.60 E-value: 8.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSrpdVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRwlrqqia 501
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 lvsqeptlfactiyDNIRHGlIGTkweseseeqqrerIYEaarkanahdfitslpegyetnvgergflLSGGQKQRIAIA 581
Cdd:cd03216 71 --------------DARRAG-IAM-------------VYQ----------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 582 RAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIV 646
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAeVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
422-649 |
9.55e-28 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 112.20 E-value: 9.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvvmEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRwlRQQIA 501
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFA-CTIYDNIRHGLI-GTKweseSEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIA 579
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSpGLK----LTAEDRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 580 IARAIVSDPKILLLDEATSALD-TKSEGVVQAALEVAAE-GRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQG 649
Cdd:cd03298 139 LARVLVRDKPVLLLDEPFAALDpALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1112-1319 |
1.34e-27 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 113.51 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSF----IALVSQEPTLY-QGTV 1186
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 RENI-----ILGANNDVTDEQIKFACQEANIYDFIMSLPDGmntlvgskgalLSGGQKQRIAIARALIRDPKILLLDEAT 1261
Cdd:cd03294 120 LENVafgleVQGVPRAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1262 SALDSESEHVVQAALDK--AAKGRTTIAVAHRLS-TIQKADIIYVFDQGRIVEQGTHSELM 1319
Cdd:cd03294 189 SALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1095-1313 |
1.41e-27 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.86 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1095 EFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISslnvnEYRSFIAL 1174
Cdd:cd03235 1 EVEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1175 VSQEPTL---YQGTVRENIILGANNDV---------TDEQIKFACQEANIYDFImslpdgmNTLVGSkgalLSGGQKQRI 1242
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGHKglfrrlskaDKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1243 AIARALIRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQK-ADIIYVFDqGRIVEQG 1313
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLN-RTVVASG 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1115-1313 |
1.71e-27 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 111.62 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1115 LNLSIQ-PGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREI--SSLNVN--EYRSFIALVSQEPTLY-QGT 1185
Cdd:cd03297 15 LKIDFDlNEEVTGIFGASGAGKSTllrCIAGLEK---PDGGTIVLNGTVLfdSRKKINlpPQQRKIGLVFQQYALFpHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1186 VRENIILGANNDvTDEQIKFACQEaniydfiMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALD 1265
Cdd:cd03297 92 VRENLAFGLKRK-RNREDRISVDE-------LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1266 SESEHVVQAALDKAAK--GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:cd03297 164 RALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1093-1313 |
2.97e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 110.33 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHF---RYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALL--ERFYDPLSGGIFIDGREISSlnvNE 1167
Cdd:cd03213 3 TLSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1168 YRSFIALVSQEPTLY-QGTVRENIilganndvtdeqiKFAcqeANIydfimslpdgmntlvgsKGalLSGGQKQRIAIAR 1246
Cdd:cd03213 80 FRKIIGYVPQDDILHpTLTVRETL-------------MFA---AKL-----------------RG--LSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1247 ALIRDPKILLLDEATSALDSESEHVVQAALDKAAK-GRTTIAVAHRLST--IQKADIIYVFDQGRIVEQG 1313
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
423-646 |
4.22e-27 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 110.04 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 423 RLENIKHIYPSRPDVVvmEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTlnvRWLRQQIAL 502
Cdd:cd03226 1 RIENISFSYKKGTEIL--DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 503 VSQEPT--LFACTIYDNIRHGLigtkwesESEEQQRERIYEAARKANAHDFITSLPegyetnvgergFLLSGGQKQRIAI 580
Cdd:cd03226 76 VMQDVDyqLFTDSVREELLLGL-------KELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 581 ARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIV 646
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1093-1328 |
5.47e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.57 E-value: 5.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYP--TRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEY-- 1168
Cdd:PRK13646 2 TIRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1169 --RSFIALVSQ--EPTLYQGTVRENIILGANNDVTD-EQIKfacqeANIYDFIMSLpdGMNTLVGSKGAL-LSGGQKQRI 1242
Cdd:PRK13646 82 pvRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNlDEVK-----NYAHRLLMDL--GFSRDVMSQSPFqMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1243 AIARALIRDPKILLLDEATSALDSESEHVVQAALDK--AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELM 1319
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF 234
|
....*....
gi 164423939 1320 KKNGRYAEL 1328
Cdd:PRK13646 235 KDKKKLADW 243
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1094-1331 |
5.54e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 114.66 E-value: 5.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTrpeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSL-----NVNey 1168
Cdd:PRK09452 15 VELRGISKSFDG---KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaenrHVN-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1169 rsfialvsqepTLYQG-------TVRENIILGAN-NDVTDEQIKFACQEAniydFIMSLPDGMntlVGSKGALLSGGQKQ 1240
Cdd:PRK09452 90 -----------TVFQSyalfphmTVFENVAFGLRmQKTPAAEITPRVMEA----LRMVQLEEF---AQRKPHQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1241 RIAIARALIRDPKILLLDEATSALDSESEHVVQAALdKAAK---GRTTIAVAH-RLSTIQKADIIYVFDQGRIVEQGTHS 1316
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNEL-KALQrklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPR 230
|
250
....*....|....*
gi 164423939 1317 ELmkkngrYAELVNL 1331
Cdd:PRK09452 231 EI------YEEPKNL 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1114-1319 |
8.01e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 112.90 E-value: 8.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1114 GLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE---YRSFIALVSQEPtlyQG------ 1184
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrpLRRRMQMVFQDP---YAslnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 TVREniILGA----NNDVTDEQIKFACQEaniydfimslpdgMNTLVGskgaL-----------LSGGQKQRIAIARALI 1249
Cdd:COG4608 113 TVGD--IIAEplriHGLASKAERRERVAE-------------LLELVG----LrpehadrypheFSGGQRQRIGIARALA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1250 RDPKILLLDEATSALD-SesehvVQAA-----LD-KAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELM 1319
Cdd:COG4608 174 LNPKLIVCDEPVSALDvS-----IQAQvlnllEDlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELY 246
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
422-649 |
9.11e-27 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 109.59 E-value: 9.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRpdvVVMEDVSLVIPAGkTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTlNVRWLRQQIA 501
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFA-CTIYDNIRH-----GLIGTKweseseeqQRERIYEAARKANAHDFitslpegYETNVGErgflLSGGQK 575
Cdd:cd03264 76 YLPQEFGVYPnFTVREFLDYiawlkGIPSKE--------VKARVDEVLELVNLGDR-------AKKKIGS----LSGGMR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 576 QRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQG 649
Cdd:cd03264 137 RRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
438-656 |
9.78e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 110.61 E-value: 9.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 438 VVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDIST---LN-----VRWLRQQIALVSQEPTL 509
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarsLSqqkglIRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 510 FAC-TIYDNIRHGLIGTKWESESeeqqreriyEAARKANAHDFITSLpEGYETNVGERgflLSGGQKQRIAIARAIVSDP 588
Cdd:PRK11264 97 FPHrTVLENIIEGPVIVKGEPKE---------EATARARELLAKVGL-AGKETSYPRR---LSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 589 KILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAELLA 656
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIrQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1098-1310 |
1.17e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 108.88 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1098 DVHFRYPTRPEqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlnvNEYRSFIALVSQ 1177
Cdd:cd03226 4 NISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1178 EPT--LYQGTVRENIILGANN-DVTDEQIKFACQEANIYDFIMSLPdgmntlvgskgALLSGGQKQRIAIARALIRDPKI 1254
Cdd:cd03226 79 DVDyqLFTDSVREELLLGLKElDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1255 LLLDEATSALDSES-EHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIV 1310
Cdd:cd03226 148 LIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1093-1319 |
1.32e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.25 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFI 1172
Cdd:PRK13548 2 MLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQEPTL-YQGTVRENIILGA----NNDVTDEQIkfaCQEAniydfiMSLPDgmntLVGSKGAL---LSGGQKQRIAI 1244
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMGRaphgLSRAEDDAL---VAAA------LAQVD----LAHLAGRDypqLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1245 ARALIR------DPKILLLDEATSALD-SESEHVVQAALDKAAK-GRTTIAVAHRLS-TIQKADIIYVFDQGRIVEQGTH 1315
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTP 225
|
....
gi 164423939 1316 SELM 1319
Cdd:PRK13548 226 AEVL 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1111-1314 |
1.39e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 110.13 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEY------RSFialvsQEPTLYQG 1184
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlgiaRTF-----QNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 -TVRENIILGANN-------DVTDEQIKFACQEANIYDFIMS------LPDGMNTLVGSkgalLSGGQKQRIAIARALIR 1250
Cdd:COG0411 94 lTVLENVLVAAHArlgrgllAALLRLPRARREEREARERAEEllervgLADRADEPAGN----LSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1251 DPKILLLDEATSAL-DSESEHVVQAALD-KAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGT 1314
Cdd:COG0411 170 EPKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1093-1316 |
1.43e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 109.72 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYPTrpeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDG------REISSLNVN 1166
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1167 EYRSFIALVSQEPTLY-QGTVRENII------LGANNDVTDEQIKFACQEANIYDFIMSLPdgmntlvgskgALLSGGQK 1239
Cdd:COG4161 79 LLRQKVGMVFQQYNLWpHLTVMENLIeapckvLGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1240 QRIAIARALIRDPKILLLDEATSALDSE-SEHVVQAALDKAAKGRTTIAVAHRLSTIQK--ADIIYVfDQGRIVEQGTHS 1316
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvaSQVVYM-EKGRIIEQGDAS 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1094-1312 |
2.61e-26 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 109.89 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPT------RPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE 1167
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1168 YRSF---IALVSQE-PTLY--QGTVREnIILGANNDVTDeqIKFACQEANIYDFI--MSLPDgmnTLVGSKGALLSGGQK 1239
Cdd:TIGR02769 83 RRAFrrdVQLVFQDsPSAVnpRMTVRQ-IIGEPLRHLTS--LDESEQKARIAELLdmVGLRS---EDADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1240 QRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDK--AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQ 1312
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
437-656 |
2.62e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 115.17 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 437 VVVMEDVSLVIPAGKTTALVGASGSGKS----TIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQ----QIALVSQEPT 508
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 509 -----LFacTIYDNIRHGLIgtkweseseeqqrerIYEAARKANAHDFI------TSLPEGyETNVGERGFLLSGGQKQR 577
Cdd:COG4172 103 tslnpLH--TIGKQIAEVLR---------------LHRGLSGAAARARAlellerVGIPDP-ERRLDAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 578 IAIARAIVSDPKILLLDEATSALDTksegVVQAA-LE-----VAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGT 650
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDV----TVQAQiLDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGP 240
|
....*.
gi 164423939 651 HAELLA 656
Cdd:COG4172 241 TAELFA 246
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1093-1266 |
2.84e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.57 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYP-TRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEyrsf 1171
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1172 iALVSQEPTLYQG-TVRENIILG---------ANNDVTDEQIKfacqeaniydfimslpdgmntLVGSKGAL------LS 1235
Cdd:COG4525 79 -GVVFQKDALLPWlNVLDNVAFGlrlrgvpkaERRARAEELLA---------------------LVGLADFArrriwqLS 136
|
170 180 190
....*....|....*....|....*....|.
gi 164423939 1236 GGQKQRIAIARALIRDPKILLLDEATSALDS 1266
Cdd:COG4525 137 GGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
808-1027 |
4.36e-26 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 109.94 E-value: 4.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 808 KSDASFW--CLMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDrdENSAGALTSFLSTETTHVA 885
Cdd:cd18572 30 GSREAFYraVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKVS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 886 GLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIP-ILLGCGFYrfwmiAHYQRRA----KSAYAGSASYASEAI 960
Cdd:cd18572 108 DPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPvIALITKVY-----GRYYRKLskeiQDALAEANQVAEEAL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 961 TAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHE 1027
Cdd:cd18572 183 SNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGR 249
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1094-1318 |
5.09e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.40 E-value: 5.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVN--EYRSF 1171
Cdd:PRK13639 2 LETRDLKYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1172 IALVSQEP--TLYQGTVRENII-----LGANNDVTDEQIKFACQEANIYDFIMSLPDGmntlvgskgalLSGGQKQRIAI 1244
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAfgplnLGLSKEEVEKRVKEALKAVGMEGFENKPPHH-----------LSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1245 ARALIRDPKILLLDEATSALDSE-SEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1094-1323 |
6.53e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 116.38 E-value: 6.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIdgreisslnvneYRSFIA 1173
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQGTVRENIILGANNDvtDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPK 1253
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFGSPFD--PERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 1254 ILLLDEATSALDSeseHVVQAALDKAAK----GRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMkKNG 1323
Cdd:PLN03130 761 VYIFDDPLSALDA---HVGRQVFDKCIKdelrGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS-NNG 830
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
166-395 |
7.42e-26 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 109.17 E-value: 7.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 166 FIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLT 245
Cdd:cd18572 60 FSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 246 LILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAHLTRAEHFGFRLKGSI 325
Cdd:cd18572 140 LLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAY 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 326 GVMVAGMMTVLYLNYGLAFWQGSRFLLSGDTELRKILTVMM--SVMIGAFN-LGNIAPNLQAfvtALGAAAKI 395
Cdd:cd18572 220 AGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLyqQQLGEAFQsLGDVFSSLMQ---AVGAAEKV 289
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1111-1318 |
7.78e-26 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 107.23 E-value: 7.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE-YRSFIALVSQE----PTLyqgT 1185
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHErARAGIAYVPQGreifPRL---T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1186 VRENIILGANNdvtdeqikFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALD 1265
Cdd:TIGR03410 92 VEENLLTGLAA--------LPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1266 SESEHVVQAALDK--AAKGRTTIAVAHRLS-TIQKADIIYVFDQGRIVEQGTHSEL 1318
Cdd:TIGR03410 164 PSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1097-1318 |
8.02e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 108.62 E-value: 8.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1097 RDVHFRYPT------RPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRS 1170
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1171 F---IALVSQEPTLY---QGTVREnIILGANNDVTDeqIKFACQEANIYDFI--MSLPDgmnTLVGSKGALLSGGQKQRI 1242
Cdd:PRK10419 87 FrrdIQMVFQDSISAvnpRKTVRE-IIREPLRHLLS--LDKAERLARASEMLraVDLDD---SVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1243 AIARALIRDPKILLLDEATSALDSesehVVQA---ALDKAAKGRTTIA---VAHRLSTIQK-ADIIYVFDQGRIVEQGTH 1315
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDL----VLQAgviRLLKKLQQQFGTAclfITHDLRLVERfCQRVMVMDNGQIVETQPV 236
|
...
gi 164423939 1316 SEL 1318
Cdd:PRK10419 237 GDK 239
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1094-1310 |
8.37e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 108.25 E-value: 8.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVH--FRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNvnEYR-- 1169
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP--EYKra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SFIALVSQEPTLyqGT-----VRENIILGANND--------VTDEQIKFACQEANIYDfiMSLPDGMNTLVGskgaLLSG 1236
Cdd:COG1101 80 KYIGRVFQDPMM--GTapsmtIEENLALAYRRGkrrglrrgLTKKRRELFRELLATLG--LGLENRLDTKVG----LLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1237 GQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDK--AAKGRTTIAVAHRLS--------TIqkadiiyVFDQ 1306
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqaldygnrLI-------MMHE 224
|
....
gi 164423939 1307 GRIV 1310
Cdd:COG1101 225 GRII 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1094-1321 |
9.77e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 108.30 E-value: 9.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTrPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEP--TLYQGTVRENIILGANN-----DVTDEQIKFACQEANIYDFIMSLPDGmntlvgskgalLSGGQKQRIAIAR 1246
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENhavpyDEMHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1247 ALIRDPKILLLDEATSALDSESEHVVQAALD--KAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKK 1321
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
127-395 |
9.83e-26 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 108.88 E-value: 9.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 127 YFAG-----VTTYDDFTDELAR---------LVLYFVYLAIGEFVTMYIttvgFIYSGEHISGKIREHYLESCMRQNIGF 192
Cdd:cd18780 17 YFFGqvidaVTNHSGSGGEEALralnqavliLLGVVLIGSIATFLRSWL----FTLAGERVVARLRKRLFSAIIAQEIAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 193 FDKLGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQ 272
Cdd:cd18780 93 FDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 273 NIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQGSRFLL 352
Cdd:cd18780 173 FQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVI 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 164423939 353 SGDT---ELRKILTVMMSVmigAFNLGNIAPNLQAFVTALGAAAKI 395
Cdd:cd18780 253 DGELttgLLTSFLLYTLTV---AMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
437-656 |
1.12e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 107.82 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 437 VVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWL-RQQIALVSQEPTLFA-CTI 514
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPeLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 515 YDNIR---HGLIGTKWESESEEQQRERIYEAARKANAHDFI--TSLPEGYETNVGErgflLSGGQKQRIAIARAIVSDPK 589
Cdd:COG0411 97 LENVLvaaHARLGRGLLAALLRLPRARREEREARERAEELLerVGLADRADEPAGN----LSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 590 ILLLDEATSALDTK-SEGVVQAALEVAAE-GRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAELLA 656
Cdd:COG0411 173 LLLLDEPAAGLNPEeTEELAELIRRLRDErGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
440-650 |
1.50e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.53 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 440 MEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEP-TLFACTI--YD 516
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPdNQFVGSIvkYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 517 nIRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIAIARAIVSDPKILLLDEA 596
Cdd:PRK13648 105 -VAFGL---ENHAVPYDEMHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 597 TSALDTKS-EGVVQAALEVAAEGRTT-ITIAHRLSTIKDAHNIVVMAQGRIVEQGT 650
Cdd:PRK13648 170 TSMLDPDArQNLLDLVRKVKSEHNITiISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
421-657 |
1.76e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.94 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIY-PSRP-DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN----VR 494
Cdd:PRK13646 2 TIRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 495 WLRQQIALVSQ--EPTLFActiyDNI-RHGLIGTKweseseeQQRERIYEAarKANAHDFITSLpeGYETNVGERG-FLL 570
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFE----DTVeREIIFGPK-------NFKMNLDEV--KNYAHRLLMDL--GFSRDVMSQSpFQM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 571 SGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEV--AAEGRTTITIAHRLSTI-KDAHNIVVMAQGRIVE 647
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVS 226
|
250
....*....|
gi 164423939 648 QGTHAELLAK 657
Cdd:PRK13646 227 QTSPKELFKD 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1094-1328 |
1.81e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.87 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEP--TLYQGTVRENIILGANND-VTDEQIKFACQEA----NIYDFIMSLPdgmntlvgskgALLSGGQKQRIAIAR 1246
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1247 ALIRDPKILLLDEATSALD----SESEHVVQAALDKAAkgRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKN 1322
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
....*.
gi 164423939 1323 GRYAEL 1328
Cdd:PRK13642 232 EDMVEI 237
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1107-1307 |
1.95e-25 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 105.88 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1107 PEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSF----IALVSQEPTLY 1182
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1183 QGTVRENIILGAnnDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATS 1262
Cdd:cd03290 92 NATVEENITFGS--PFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 164423939 1263 ALDSE-SEHVVQAALDKAAKG--RTTIAVAHRLSTIQKADIIYVFDQG 1307
Cdd:cd03290 170 ALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
422-644 |
2.55e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 105.18 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVR---WLRQ 498
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 499 QIALVSQEPTLFA-CTIYDNIRHGLIGTkweSESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQR 577
Cdd:cd03292 79 KIGVVFQDFRLLPdRNVYENVAFALEVT---GVPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 578 IAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGR 644
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1091-1321 |
2.58e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 107.24 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1091 DGTIEFRDVHFRYPTRPEqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREI--SSLNVNEY 1168
Cdd:PRK13636 3 DYILKVEELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1169 RSFIALVSQEP--TLYQGTVRENIILGANN-----DVTDEQIKFACQEAniydfimslpdGMNTLVGSKGALLSGGQKQR 1241
Cdd:PRK13636 81 RESVGMVFQDPdnQLFSASVYQDVSFGAVNlklpeDEVRKRVDNALKRT-----------GIEHLKDKPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1242 IAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQ-KADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
...
gi 164423939 1319 MKK 1321
Cdd:PRK13636 230 FAE 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
436-656 |
2.77e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 105.83 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 DVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLNVRWL-RQQIALVSQE---- 506
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTllkaISGLL----PPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGrrif 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 PTLfacTIYDNIRHGligtkweseseeqqreriyeAARKANAHDFITSLPEGYET--NVGER----GFLLSGGQKQRIAI 580
Cdd:COG0410 91 PSL---TVEENLLLG--------------------AYARRDRAEVRADLERVYELfpRLKERrrqrAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 581 ARAIVSDPKILLLDEAtsaldtkSEG----VVQ---AAL-EVAAEGrttITI------AHRLSTIkdAHNIVVMAQGRIV 646
Cdd:COG0410 148 GRALMSRPKLLLLDEP-------SLGlaplIVEeifEIIrRLNREG---VTIllveqnARFALEI--ADRAYVLERGRIV 215
|
250
....*....|
gi 164423939 647 EQGTHAELLA 656
Cdd:COG0410 216 LEGTAAELLA 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1079-1320 |
2.86e-25 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 112.83 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1079 TWSNEgDLIKQVDGTIEFRDVHFRYP-----TRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLErFYDP----L 1149
Cdd:TIGR00955 4 SWRNS-DVFGRVAQDGSWKQLVSRLRgcfcrERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1150 SGGIFIDGREIsslNVNEYRSFIALVSQE----PTLyqgTVRENIILGAN----NDVTDEQIKFACQEAnIYDfiMSLPD 1221
Cdd:TIGR00955 82 SGSVLLNGMPI---DAKEMRAISAYVQQDdlfiPTL---TVREHLMFQAHlrmpRRVTKKEKRERVDEV-LQA--LGLRK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1222 GMNTLVGSKGAL--LSGGQKQRIAIARALIRDPKILLLDEATSALDSESEH-VVQAALDKAAKGRTTIAVAHRLST--IQ 1296
Cdd:TIGR00955 153 CANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYsVVQVLKGLAQKGKTIICTIHQPSSelFE 232
|
250 260
....*....|....*....|....
gi 164423939 1297 KADIIYVFDQGRIVEQGTHSELMK 1320
Cdd:TIGR00955 233 LFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1094-1332 |
3.07e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.41 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRY-PTRP-EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISS----LNVNE 1167
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1168 YRSFIALVSQ--EPTLYQGTVRENIILGANN-DVTDEQIKFACQEaniydfimslpdgMNTLVGSKGAL-------LSGG 1237
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfGVSEEDAKQKARE-------------MIELVGLPEELlarspfeLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1238 QKQRIAIARALIRDPKILLLDEATSALDSESEHVVQ---AALDKaAKGRTTIAVAHRLSTI-QKADIIYVFDQGRIVEQG 1313
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQG 228
|
250
....*....|....*....
gi 164423939 1314 THSELMKKNgryAELVNLQ 1332
Cdd:PRK13634 229 TPREIFADP---DELEAIG 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
422-654 |
3.20e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.26 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSrpdVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVR-WLRQQI 500
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEPTLFAC-TIYDNI-------RHGLIGTKweseseeqqreRIYEAARKAnahdfITSLpeGYETNVGERGFLLSG 572
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIflgreprRGGLIDWR-----------AMRRRAREL-----LARL--GLDIDPDTPVGDLSV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 573 GQKQRIAIARAIVSDPKILLLDEATSALdTKSEgvVQAALEV----AAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVE 647
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASL-TERE--VERLFRIirrlKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
....*..
gi 164423939 648 QGTHAEL 654
Cdd:COG1129 221 TGPVAEL 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1111-1318 |
3.42e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYD-----PLSGGIFIDGREISSLNVNEYRSFIALVSQEPT-LYQG 1184
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 TVRENIILG-------ANNDVTDEQIKFACQEANIYDfimSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKILLL 1257
Cdd:PRK14247 98 SIFENVALGlklnrlvKSKKELQERVRWALEKAQLWD---EVKDRLDAPAGK----LSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1258 DEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREV 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
442-657 |
4.83e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 107.74 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDI---STLNVRWLRQQIALVSQEPtlFACTiydNI 518
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNP--YGSL---NP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 519 RHG---------LIGTKweseseeqqrerIYEAARKANAHDFITSL---PEGYetnvGERGFLLSGGQKQRIAIARAIVS 586
Cdd:PRK11308 108 RKKvgqileeplLINTS------------LSAAERREKALAMMAKVglrPEHY----DRYPHMFSGGQRQRIAIARALML 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 587 DPKILLLDEATSALDTKsegvVQA-ALEVAAE-----GRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAELLAK 657
Cdd:PRK11308 172 DPDVVVADEPVSALDVS----VQAqVLNLMMDlqqelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
422-654 |
5.26e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 104.51 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVVVmEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTlNVRWLRQQIA 501
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLF-ACTIYDNIR-HGLI-GtkweseseeqqrerIYEAARKANAHDFI--TSLPEGYETNVGErgflLSGGQKQ 576
Cdd:cd03263 79 YCPQFDALFdELTVREHLRfYARLkG--------------LPKSEIKEEVELLLrvLGLTDKANKRART----LSGGMKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 577 RIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHrlsTIKDA----HNIVVMAQGRIVEQGTHA 652
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH---SMDEAealcDRIAIMSDGKLRCIGSPQ 217
|
..
gi 164423939 653 EL 654
Cdd:cd03263 218 EL 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
138-395 |
5.29e-25 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 106.80 E-value: 5.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 138 TDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGIS 217
Cdd:cd18576 32 TASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 218 EKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAF 297
Cdd:cd18576 112 TTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 298 GTQDRLARRYDAHLTRAehFGFRLKGSI--GVMVAGMMTVLYLNYGLAFWQGSRFLLSGDTELRKILT-VMMSVMIGA-- 372
Cdd:cd18576 192 TREDYEIERYRKALERV--VKLALKRARirALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAGsi 269
|
250 260
....*....|....*....|...
gi 164423939 373 FNLGNIAPNLQAfvtALGAAAKI 395
Cdd:cd18576 270 GSLADLYGQLQK---ALGASERV 289
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1109-1318 |
5.71e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.60 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1109 QPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGREIS---SLN-----VNEYRSFIALVSQ 1177
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ---PEAGTIRVGDITIDtarSLSqqkglIRQLRQHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1178 EPTLY-QGTVRENIILG---ANNDVTDEQIKFACQE-ANIydfimslpdgmnTLVGSKGAL---LSGGQKQRIAIARALI 1249
Cdd:PRK11264 93 NFNLFpHRTVLENIIEGpviVKGEPKEEATARARELlAKV------------GLAGKETSYprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1250 RDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
427-673 |
5.76e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.62 E-value: 5.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQE 506
Cdd:PRK13548 5 ARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 PTL-FACTIYDNIRHGLIGtkwESESEEQQRERIYEAARKANAHDFitslpegyetnvGERGFL-LSGGQKQRIAIARAI 584
Cdd:PRK13548 85 SSLsFPFTVEEVVAMGRAP---HGLSRAEDDALVAAALAQVDLAHL------------AGRDYPqLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 585 V------SDPKILLLDEATSALDTK-SEGVVQAALEVAAE-GRTTITIAHRLS-TIKDAHNIVVMAQGRIVEQGTHAELL 655
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAhQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
250
....*....|....*...
gi 164423939 656 akrgayyklvTAQAIAAV 673
Cdd:PRK13548 230 ----------TPETLRRV 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1116-1333 |
7.00e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 104.66 E-value: 7.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1116 NLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDG----------REISSLnvneyrsFialvsQEPTLYQG- 1184
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttppsrRPVSML-------F-----QENNLFSHl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 TVRENIILGAN-----NDVTDEQIKFACQEANIYDFIMSLPdgmntlvgskgALLSGGQKQRIAIARALIRDPKILLLDE 1259
Cdd:PRK10771 87 TVAQNIGLGLNpglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1260 ATSALDSESEHVVQAALDKAAKGR--TTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELMKKNGRYAELVNLQS 1333
Cdd:PRK10771 156 PFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSGKASASALLGIKS 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1110-1318 |
7.48e-25 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 106.09 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1110 PVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGReisslnvneyrsfIALVSQEPTLYQGTVREN 1189
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1190 IILGanndVTDEQIKF-----ACQeanIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSAL 1264
Cdd:cd03291 118 IIFG----VSYDEYRYksvvkACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1265 DSESE-HVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSEL 1318
Cdd:cd03291 191 DVFTEkEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
436-655 |
9.70e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.40 E-value: 9.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDI--STLNVRWLRQQIALVSQEPTLFA-C 512
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFYLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 513 TIYDNIRHGLIGTKweseseeqqreriyeAARKANAHDFITSLpegyETNVG--ERGF----LLSGGQKQRIAIARAIVS 586
Cdd:PRK09493 93 TALENVMFGPLRVR---------------GASKEEAEKQAREL----LAKVGlaERAHhypsELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 587 DPKILLLDEATSALDTK-SEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAELL 655
Cdd:PRK09493 154 KPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1112-1301 |
1.69e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.09 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYD-----PLSGGIFIDGREISSLNVN--EYRSFIALVSQEPTLYQG 1184
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDtvDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 TVRENIILG------ANNDVTDEQIKFACQEANIYDfimSLPDGMNtlvgsKGAL-LSGGQKQRIAIARALIRDPKILLL 1257
Cdd:PRK14239 101 SIYENVVYGlrlkgiKDKQVLDEAVEKSLKGASIWD---EVKDRLH-----DSALgLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 164423939 1258 DEATSALDSESEHVVQAALDKAAKGRTTIAVAHrlsTIQKADII 1301
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1093-1337 |
1.81e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.91 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRY-PTRP-EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREI----SSLNVN 1166
Cdd:PRK13641 2 SIKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1167 EYRSFIALVSQ--EPTLYQGTVRENIILGANNdvtdeqIKFACQEANIYDFIMSLPDGMNTLVGSKGAL-LSGGQKQRIA 1243
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKN------FGFSEDEAKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1244 IARALIRDPKILLLDEATSALDSESEH-VVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELMKk 1321
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS- 234
|
250
....*....|....*.
gi 164423939 1322 ngryaelvNLQSLEKH 1337
Cdd:PRK13641 235 --------DKEWLKKH 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1094-1319 |
1.93e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 109.39 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTR--------PEQPVLRGLNLSIQPGQYVALVGASGCGKSTT-IALLeRFyDPLSGGIFIDGREISSLN 1164
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RL-IPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1165 VNE---YRSFIALVSQEPtlYqG------TVREnII--------LGANNDVTDEQIKFACQEaniydfimslpdgmntlV 1227
Cdd:COG4172 354 RRAlrpLRRRMQVVFQDP--F-GslsprmTVGQ-IIaeglrvhgPGLSAAERRARVAEALEE-----------------V 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1228 GSKGALL-------SGGQKQRIAIARALIRDPKILLLDEATSALDseseHVVQAA-LD-----KAAKGRTTIAVAHRLST 1294
Cdd:COG4172 413 GLDPAARhryphefSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAV 488
|
250 260
....*....|....*....|....*.
gi 164423939 1295 IQK-ADIIYVFDQGRIVEQGTHSELM 1319
Cdd:COG4172 489 VRAlAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1109-1329 |
1.98e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.84 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1109 QPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISslNVNEYRSFIALVSQEPTLY-QGTVR 1187
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1188 ENIILGANND-VTDEQIKFACQEaniydfIMSLPDgMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDS 1266
Cdd:PRK11607 110 QNIAFGLKQDkLPKAEIASRVNE------MLGLVH-MQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1267 E----SEHVVQAALDKAakGRTTIAVAH-RLSTIQKADIIYVFDQGRIVEQGTHSELMKK-NGRY-AELV 1329
Cdd:PRK11607 183 KlrdrMQLEVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHpTTRYsAEFI 250
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
422-658 |
3.09e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 3.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVvvMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDD--VDISTLNVRWLRQQ 499
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEP--TLFACTIYDNIRHGLIGTKweseseeQQRERIYEAARKANAHDFITSLPEgyetnvgERGFLLSGGQKQR 577
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLK-------LPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 578 IAIARAIVSDPKILLLDEATSALDTK--SEgVVQAALEVAAEGRTTITIA-HRLSTIK-DAHNIVVMAQGRIVEQGTHAE 653
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMgvSE-IMKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228
|
....*
gi 164423939 654 LLAKR 658
Cdd:PRK13636 229 VFAEK 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1094-1318 |
3.21e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.11 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:PRK13652 4 IETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEP--TLYQGTVRENIILGANNDVTDEQ-IKFACQEAniydfIMSLpdGMNTLVGSKGALLSGGQKQRIAIARALIR 1250
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEEtVAHRVSSA-----LHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1251 DPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTI-QKADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1056-1320 |
4.34e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 110.64 E-value: 4.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1056 DMGKATEAARDLKElfDRKPTVDTwsnEGDLIKQVDGTIEFRDVHFrYPTRPEQpVLRGLNLSIQPGQYVALVGASGCGK 1135
Cdd:PTZ00243 627 DYGSPSSASRHIVE--GGTGGGHE---ATPTSERSAKTPKMKTDDF-FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGK 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1136 STTI-ALLERFydplsggifidgrEISSLNVNEYRSfIALVSQEPTLYQGTVRENIILGANNDVTDEQ--IKFACQEANI 1212
Cdd:PTZ00243 700 STLLqSLLSQF-------------EISEGRVWAERS-IAYVPQQAWIMNATVRGNILFFDEEDAARLAdaVRVSQLEADL 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1213 ydfiMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSE-SEHVVQAALDKAAKGRTTIAVAHR 1291
Cdd:PTZ00243 766 ----AQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQ 841
|
250 260
....*....|....*....|....*....
gi 164423939 1292 LSTIQKADIIYVFDQGRIVEQGTHSELMK 1320
Cdd:PTZ00243 842 VHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1112-1290 |
5.23e-24 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 102.16 E-value: 5.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEyrsfiALVSQEPTLYQG-TVRENI 1190
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR-----MVVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1191 ILGANNDVTDeqIKFACQEANIYDFIMSLpdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEH 1270
Cdd:TIGR01184 76 ALAVDRVLPD--LSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|..
gi 164423939 1271 VVQAALDKAAK--GRTTIAVAH 1290
Cdd:TIGR01184 152 NLQEELMQIWEehRVTVLMVTH 173
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1105-1265 |
6.56e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.02 E-value: 6.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1105 TRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDP---LSGGIFIDGREISSLNVNEYRsfIALVSQEPTL 1181
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRR--IGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1182 Y-QGTVRENIILGANNDVT----DEQIKFACQEANIYDFIMSLPdgmntlvgskgALLSGGQKQRIAIARALIRDPKILL 1256
Cdd:COG4136 88 FpHLSVGENLAFALPPTIGraqrRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALL 156
|
....*....
gi 164423939 1257 LDEATSALD 1265
Cdd:COG4136 157 LDEPFSKLD 165
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
422-658 |
8.07e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.89 E-value: 8.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIA 501
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEP--TLFACTIYDNIRHGLIGtkwESESEEQQRERIYEAARKANAHDFITSLPegyetnvgergFLLSGGQKQRIA 579
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVN---MGLDKDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 580 IARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGThAELLAK 657
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTD 227
|
.
gi 164423939 658 R 658
Cdd:PRK13647 228 E 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
422-656 |
8.38e-24 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 101.47 E-value: 8.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLNV-RWL 496
Cdd:cd03218 1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTtfymIVGLV----KPDSGKILLDGQDITKLPMhKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 497 RQQIALVSQEPTLF-ACTIYDNIRHGLIGTKWESEseeqqreriyEAARKANA--HDF-ITSLpegyETNVGERgflLSG 572
Cdd:cd03218 74 RLGIGYLPQEASIFrKLTVEENILAVLEIRGLSKK----------EREEKLEEllEEFhITHL----RKSKASS---LSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 573 GQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEG----------RTTITIAHRlstikdahnIVVMA 641
Cdd:cd03218 137 GERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIkILKDRGigvlitdhnvRETLSITDR---------AYIIY 207
|
250
....*....|....*
gi 164423939 642 QGRIVEQGTHAELLA 656
Cdd:cd03218 208 EGKVLAEGTPEEIAA 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
752-1311 |
8.52e-24 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 107.58 E-value: 8.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 752 IKLIASFNKKEWHMMLVGIFFSAICGAGNptqavffAKLISslsrpIVNEEIRASIKSDASFwCLMYLMLALVQCLAFSV 831
Cdd:COG4615 1 MNLLRLLLRESRWLLLLALLLGLLSGLAN-------AGLIA-----LINQALNATGAALARL-LLLFAGLLVLLLLSRLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 832 QGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLiaACTVALA 911
Cdd:COG4615 68 SQLLLTRLGQHAVARLRLRLSRRILAAPLERLER--IGAARLLAALTEDVRTISQAFVRLPELLQSVALVL--GCLAYLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 912 -LGWKLALVCIATIPILLGCgfyrfwmiahYQRRAKSAYAGSASyASEAITAM-RTVASLT-----------REQDVLQ- 977
Cdd:COG4615 144 wLSPPLFLLTLVLLGLGVAG----------YRLLVRRARRHLRR-AREAEDRLfKHFRALLegfkelklnrrRRRAFFDe 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 978 HYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALgfwyggtliakheydmftffIVFSSVIFGAQSAGSVFSFA--- 1054
Cdd:COG4615 213 DLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGL--------------------ILFLLPALGWADPAVLSGFVlvl 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1055 --------------PDMGKATEAARDLKELFDRKPTVDTWSNEGDLIKQVDG--TIEFRDVHFRYPTRPEQPVLR-G-LN 1116
Cdd:COG4615 273 lflrgplsqlvgalPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDEGFTlGpID 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1117 LSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGtvreniILGANN 1196
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDG 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1197 DVTDEQIKfacqeaniyDFIMSLpdGMNTLVGSK-GAL----LSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHV 1271
Cdd:COG4615 427 EADPARAR---------ELLERL--ELDHKVSVEdGRFsttdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRV 495
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 164423939 1272 VQAAL--DKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVE 1311
Cdd:COG4615 496 FYTELlpELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1093-1316 |
9.47e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 9.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYPTrpeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDG------REISSLNVN 1166
Cdd:PRK11124 2 SIQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1167 EYRSFIALVSQEPTLY-QGTVRENII------LGANNDVTDEQIKFACQEANIYDFIMSLPdgmntlvgskgALLSGGQK 1239
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWpHLTVQQNLIeapcrvLGLSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1240 QRIAIARALIRDPKILLLDEATSALDSE-SEHVVQAALDKAAKGRTTIAVAHRLSTIQKA--DIIYVfDQGRIVEQGTHS 1316
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKTasRVVYM-ENGHIVEQGDAS 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1092-1309 |
9.81e-24 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 102.63 E-value: 9.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1092 GTIEFRDVHFRYpTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDpLSGGIFIDGREISSLNVNEYRSF 1171
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1172 IALVSQEPTLYQGTVRENiiLGANNDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRD 1251
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKN--LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1252 PKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRI 1309
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
422-658 |
1.15e-23 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 102.19 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPS------RPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN--- 492
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 493 VRWLRQQIALVSQE-PTLFactiydNIRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLpeGYETNVGER-GFLL 570
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAV------NPRMTV---RQIIGEPLRHLTSLDESEQKARIAELLDMV--GLRSEDADKlPRQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 571 SGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEV--AAEGRTTITIAHRLSTI-KDAHNIVVMAQGRIVE 647
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
250
....*....|.
gi 164423939 648 QGTHAELLAKR 658
Cdd:TIGR02769 232 ECDVAQLLSFK 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1094-1329 |
1.28e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 108.91 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLsggifidgrEISSLNVneyRSFIA 1173
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA---------ETSSVVI---RGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQGTVRENIILGAnnDVTDEQIKFACQEANIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPK 1253
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFGS--DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1254 ILLLDEATSALDSESEH-VVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELV 1329
Cdd:PLN03232 761 IYIFDDPLSALDAHVAHqVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
433-639 |
1.32e-23 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 100.25 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 433 SRPDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLNVRWlRQQIALVSQEPT 508
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLL----PPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 509 LF-ACTIYDNIR-----HGLIGTkweseseeqqRERIYEAARKANahdfitslPEGYEtnvGERGFLLSGGQKQRIAIAR 582
Cdd:COG4133 86 LKpELTVRENLRfwaalYGLRAD----------REAIDEALEAVG--------LAGLA---DLPVRQLSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 583 AIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITIAHRLSTIKDAHNIVV 639
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1094-1314 |
1.36e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.99 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLN-VNEYRSFI 1172
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQEP-TLYQG-TVRENIILGANNDV-----TDEQIKFACQEANIYDFIMSLPDGmntlvgskgalLSGGQKQRIAIA 1245
Cdd:PRK13644 80 GIVFQNPeTQFVGrTVEEDLAFGPENLClppieIRKRVDRALAEIGLEKYRHRSPKT-----------LSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1246 RALIRDPKILLLDEATSALDSESEHVVQAALDKA-AKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGT 1314
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
422-646 |
1.71e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.70 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENI-KHIYPSRPD-VVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVrWLR-Q 498
Cdd:COG1101 2 LELKNLsKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRaK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 499 QIALVSQEPTLFAC---TIYDNI--------RHGL-IGTKweseseeqqreriyeAARKANAHDFITSLPEGYE----TN 562
Cdd:COG1101 81 YIGRVFQDPMMGTApsmTIEENLalayrrgkRRGLrRGLT---------------KKRRELFRELLATLGLGLEnrldTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 563 VGergfLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAEGR-TTITIAHRLstiKDAHN---- 636
Cdd:COG1101 146 VG----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKtAALVLELTEKIVEENNlTTLMVTHNM---EQALDygnr 218
|
250
....*....|
gi 164423939 637 IVVMAQGRIV 646
Cdd:COG1101 219 LIMMHEGRII 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
427-601 |
1.91e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.17 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQE 506
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 PTLFACTIYDN------IRHgligtkweseseeqqrERIYEAARKANAHDFitSLPEG-YETNVGErgflLSGGQKQRIA 579
Cdd:PRK10247 90 PTLFGDTVYDNlifpwqIRN----------------QQPDPAIFLDDLERF--ALPDTiLTKNIAE----LSGGEKQRIS 147
|
170 180
....*....|....*....|..
gi 164423939 580 IARAIVSDPKILLLDEATSALD 601
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALD 169
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
421-655 |
1.94e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.24 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQI 500
Cdd:PRK11231 2 TLRTENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQE-PTLFACTIYDNIRHG----------LIGTKWESESEEQQRERIYEAARKAnahdfITSlpegyetnvgergfl 569
Cdd:PRK11231 79 ALLPQHhLTPEGITVRELVAYGrspwlslwgrLSAEDNARVNQAMEQTRINHLADRR-----LTD--------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSegvvQAAL-----EVAAEGRTTITIAHRLS-TIKDAHNIVVMAQG 643
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH----QVELmrlmrELNTQGKTVVTVLHDLNqASRYCDHLVVLANG 214
|
250
....*....|..
gi 164423939 644 RIVEQGTHAELL 655
Cdd:PRK11231 215 HVMAQGTPEEVM 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1094-1319 |
2.14e-23 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 100.31 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEY-RSFI 1172
Cdd:cd03218 1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRaRLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQEPTLYQG-TVRENI--ILGANNDVTDEQIKFAcqEANIYDF-IMSLPDgmntlvgSKGALLSGGQKQRIAIARAL 1248
Cdd:cd03218 78 GYLPQEASIFRKlTVEENIlaVLEIRGLSKKEREEKL--EELLEEFhITHLRK-------SKASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1249 IRDPKILLLDEATSALDSESEHVVQaALDKAAKGR------TTIAVAHRLSTIQKADIIYvfdQGRIVEQGTHSELM 1319
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQ-KIIKILKDRgigvliTDHNVRETLSITDRAYIIY---EGKVLAEGTPEEIA 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1108-1313 |
2.15e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 99.60 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlNVNEYRSFIALVSqEPTLYQG-TV 1186
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALIE-APGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 RENIILGANNDVTDEQIkfacqeaniydfIMSLPD--GMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSAL 1264
Cdd:cd03268 90 RENLRLLARLLGIRKKR------------IDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1265 DSESEHVVQAAL-DKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:cd03268 158 DPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
422-650 |
2.42e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.87 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDIStlNVRWLRQQIA 501
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFA-CTIYDNIRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIAI 580
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGL---RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 581 ARAIVSDPKILLLDEATSALDTKSEGVVQaaLEVAAEGR----TTITIAHRLS---TIKDahNIVVMAQGRIVEQGT 650
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQ--NELKALQRklgiTFVFVTHDQEealTMSD--RIVVMRDGRIEQDGT 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
435-643 |
2.57e-23 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 99.71 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 435 PDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWL----RQQIALVSQEPTLF 510
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 511 ACTIYDNIRHGLIGTKWEseseeqqreriYEAARKA-NAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPK 589
Cdd:cd03290 92 NATVEENITFGSPFNKQR-----------YKAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 590 ILLLDEATSALDTK-SEGVVQAALE--VAAEGRTTITIAHRLSTIKDAHNIVVMAQG 643
Cdd:cd03290 161 IVFLDDPFSALDIHlSDHLMQEGILkfLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
442-649 |
2.75e-23 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 99.29 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGkTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDV--DISTLNVRWLRQQ--IALVSQEPTLFA-CTIYD 516
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINLPPQQrkIGLVFQQYALFPhLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 517 NIRHGLIGTKWESESEEQQRERIYEAarkanahdfITSLPEGYetnVGErgflLSGGQKQRIAIARAIVSDPKILLLDEA 596
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLLG---------LDHLLNRY---PAQ----LSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 597 TSALDTKSEGVVQAAL-EVAAE-GRTTITIAHRLSTI-KDAHNIVVMAQGRIVEQG 649
Cdd:cd03297 159 FSALDRALRLQLLPELkQIKKNlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
442-680 |
2.99e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 102.88 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWL----RQQIALVSQEPTLFA-CTIYD 516
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLFPhLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 517 NIRHGLIGTKweseseeqqreriyEAARKANAHDFITSLpeGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEA 596
Cdd:TIGR02142 95 NLRYGMKRAR--------------PSERRISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 597 TSALDTKSEGVVQAALE-VAAEGRTTIT-IAHRLSTIKD-AHNIVVMAQGRIVEQGTHAELLAkRGAYYKLVTAQAiAAV 673
Cdd:TIGR02142 159 LAALDDPRKYEILPYLErLHAEFGIPILyVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA-SPDLPWLAREDQ-GSL 236
|
....*..
gi 164423939 674 NEMTAEE 680
Cdd:TIGR02142 237 IEGVVAE 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1094-1323 |
3.56e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.93 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQ---PVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSL-NVNEYR 1169
Cdd:PRK13633 5 IKCKNVSYKYESNEEStekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SFIALVSQEP--TLYQGTVRENIILGANN-DVTDEQIKFACQEA----NIYDFIMSLPDgmntlvgskgaLLSGGQKQRI 1242
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlGIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1243 AIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSE--- 1317
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEifk 233
|
....*....
gi 164423939 1318 ---LMKKNG 1323
Cdd:PRK13633 234 eveMMKKIG 242
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1094-1321 |
3.70e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.97 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYP--TRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE---- 1167
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1168 YRSFIALVSQ--EPTLYQGTVRENIILGANN-DVTDEQIKFACQEaniydfimSLpdgmnTLVGSKGAL-------LSGG 1237
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfGVSQEEAEALARE--------KL-----ALVGISESLfeknpfeLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1238 QKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK-GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTH 1315
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKP 229
|
....*.
gi 164423939 1316 SELMKK 1321
Cdd:PRK13649 230 KDIFQD 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
422-675 |
4.06e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.96 E-value: 4.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIA 501
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEP--TLFACTIYDNIRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLPEgyetnvgergfLLSGGQKQRIA 579
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGL---ENKGIPHEEMKERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 580 IARAIVSDPKILLLDEATSALDTKSE-GVVQAALEVAAE-GRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAK 657
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRlELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
250 260
....*....|....*....|...
gi 164423939 658 RGAYYKL-----VTAQAIAAVNE 675
Cdd:PRK13650 231 GNDLLQLgldipFTTSLVQSLRQ 253
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
422-656 |
4.68e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.55 E-value: 4.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIA 501
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEP--TLFACTIYDNIRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLPEgyetnvgergfLLSGGQKQRIA 579
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGM---ENQGIPREEMIKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 580 IARAIVSDPKILLLDEATSALD-TKSEGVVQAALEVAAEGR-TTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLA 656
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDpTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1094-1311 |
5.03e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 99.43 E-value: 5.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTrPEQPV--LRGLNLSIQPGQYVALVGASGCGKSTTIAL---LERfydPLSGGIFIDGREISSLNVNE- 1167
Cdd:COG4181 9 IELRGLTKTVGT-GAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDEDAr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1168 -----------YRSFIALvsqePTLyqgTVRENIIL-----GANNdvtdeqikfACQEAniydfimslpDGMNTLVGSKG 1231
Cdd:COG4181 85 arlrarhvgfvFQSFQLL----PTL---TALENVMLplelaGRRD---------ARARA----------RALLERVGLGH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1232 AL------LSGGQKQRIAIARALIRDPKILLLDEATSALDSE-SEHVVQA--ALDKAAkGRTTIAVAHRLSTIQKADIIY 1302
Cdd:COG4181 139 RLdhypaqLSGGEQQRVALARAFATEPAILFADEPTGNLDAAtGEQIIDLlfELNRER-GTTLVLVTHDPALAARCDRVL 217
|
....*....
gi 164423939 1303 VFDQGRIVE 1311
Cdd:COG4181 218 RLRAGRLVE 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
415-631 |
5.07e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.11 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 415 LENVVGTIRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYK-----PIEGKVYLDDVDI- 488
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 489 -STLNVRWLRQQIALVSQEPTLFACTIYDNIRHGLIGTKWESESEEQQrerIYEAARKAnahdfiTSLPEGYETNVGERG 567
Cdd:PRK14258 78 eRRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDD---IVESALKD------ADLWDEIKHKIHKSA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 568 FLLSGGQKQRIAIARAIVSDPKILLLDEATSALD----TKSEGVVQaALEVAAEgRTTITIAHRLSTI 631
Cdd:PRK14258 149 LDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQ-SLRLRSE-LTMVIVSHNLHQV 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
422-647 |
6.32e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 99.05 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRP-DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLV---ERfykPIEGKVYLDDVDISTLN----V 493
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDLFALDedarA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 494 RWLRQQIALVSQE----PTLfacTIYDNIRHGLigtkweseseeqqreriyEAARKANAHDFITSLPEgyETNVGERgfL 569
Cdd:COG4181 86 RLRARHVGFVFQSfqllPTL---TALENVMLPL------------------ELAGRRDARARARALLE--RVGLGHR--L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 ------LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTT-ITIAHRLSTIKDAHNIVVMA 641
Cdd:COG4181 141 dhypaqLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTlVLVTHDPALAARCDRVLRLR 220
|
....*.
gi 164423939 642 QGRIVE 647
Cdd:COG4181 221 AGRLVE 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1098-1318 |
6.59e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.08 E-value: 6.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1098 DVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGReisSLNVNEyRSFIALVSQ 1177
Cdd:PRK13638 6 DLWFRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSK-RGLLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1178 EPTLYQGTVRENIILGANNDVTDEQIKFACQEANIYDFImslpDGMNTLVGSKG------ALLSGGQKQRIAIARALIRD 1251
Cdd:PRK13638 79 VATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRV----DEALTLVDAQHfrhqpiQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1252 PKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTI-QKADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEV 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
422-657 |
6.99e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 100.26 E-value: 6.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVVVmEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVR--W-LRQ 498
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPAL-NDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKtvWdIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 499 QIALVSQEP--TLFACTIYDNIRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQ 576
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGL---ENRAVPRPEMIKIVRDVLADVGMLDYIDSEPAN-----------LSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 577 RIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAE-GRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAEL 654
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGkEQILKLIRKLKKKnNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
...
gi 164423939 655 LAK 657
Cdd:PRK13640 231 FSK 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1111-1313 |
8.88e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 98.50 E-value: 8.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKST---TIALLERFYDPLSGGIFIDGREissLNVNEYRSFIALVSQEPTLYQG-TV 1186
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQP---RKPDQFQKCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 RENIILGANNDVTDEQIKFACQEAniyDFIMSLPDGMNTLVGS---KGalLSGGQKQRIAIARALIRDPKILLLDEATSA 1263
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKR---VEDVLLRDLALTRIGGnlvKG--ISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1264 LDSESEH-VVQAALDKAAKGRTTIAVAHRlstiQKADIIYVFDQ------GRIVEQG 1313
Cdd:cd03234 174 LDSFTALnLVSTLSQLARRNRIVILTIHQ----PRSDLFRLFDRilllssGEIVYSG 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1111-1313 |
1.00e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 97.74 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlnvnEYRSFIALVSQEPTLYQG-TVREN 1189
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLPEERGLYPKmKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1190 II-LGANNDVTDEQIKfacqeANIYDFIMSLpdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSES 1268
Cdd:cd03269 91 LVyLAQLKGLKKEEAR-----RRIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 164423939 1269 -EHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:cd03269 164 vELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
814-1023 |
1.16e-22 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 99.77 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 814 WCLMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLG 893
Cdd:cd18544 43 LALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDR--TPVGRLVTRVTNDTEALNELFTSGLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 894 TIIMVLTTLIAACTVALALGWKLALVCIATIPILlgcgfyrFWMIAHYQRRAKSAY-------AGSASYASEAITAMRTV 966
Cdd:cd18544 121 TLIGDLLLLIGILIAMFLLNWRLALISLLVLPLL-------LLATYLFRKKSRKAYrevreklSRLNAFLQESISGMSVI 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 967 ASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLI 1023
Cdd:cd18544 194 QLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQV 250
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1085-1320 |
1.25e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 99.09 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1085 DLIKQVDGTIEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLN 1164
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1165 VNEYRSFIALVSQEPTLYQG-TVRENIILG-------------ANNDVTDEQIKfacqeaniydfIMSLPDGMNTLVGSk 1230
Cdd:PRK10575 80 SKAFARKVAYLPQQLPAAEGmTVRELVAIGrypwhgalgrfgaADREKVEEAIS-----------LVGLKPLAHRLVDS- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1231 galLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAA--KGRTTIAVAHRLSTIQK-ADIIYVFDQG 1307
Cdd:PRK10575 148 ---LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqeRGLTVIAVLHDINMAARyCDYLVALRGG 224
|
250
....*....|...
gi 164423939 1308 RIVEQGTHSELMK 1320
Cdd:PRK10575 225 EMIAQGTPAELMR 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
421-652 |
1.27e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDD------VDISTLNVR 494
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 495 WLRQQIALVSQEPTLFA-CTIYDNIRHG---LIG-TKweseseeqqreriyEAAR-KANAH-------DFITSLPegyet 561
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPhLTVMENLIEApckVLGlSK--------------EQAReKAMKLlarlrltDKADRFP----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 562 nvgergFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAEGRTTITIAHRLSTI-KDAHNIVV 639
Cdd:COG4161 140 ------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVY 213
|
250
....*....|...
gi 164423939 640 MAQGRIVEQGTHA 652
Cdd:COG4161 214 MEKGRIIEQGDAS 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
421-651 |
1.38e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYL--DDVDISTLN----VR 494
Cdd:PRK11124 2 SIQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTPsdkaIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 495 WLRQQIALVSQEPTLFA-CTIYDNirhgLIgtkweseSEEQQRERIYEAARKANAHDFITSLpegYETNVGERGFL-LSG 572
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPhLTVQQN----LI-------EAPCRVLGLSKDQALARAEKLLERL---RLKPYADRFPLhLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 573 GQKQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAEGRTTITIAHRLSTI-KDAHNIVVMAQGRIVEQGT 650
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHIVEQGD 224
|
.
gi 164423939 651 H 651
Cdd:PRK11124 225 A 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
431-640 |
1.40e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.53 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 431 YPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVylddvdistlnVRWLRQQIALVSQ---EP 507
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 508 TLFACTIYDNIRHGLigtkWESESEEqqreriyeaaRKANAHDfiTSLPEGYETNVGERGFL------LSGGQKQRIAIA 581
Cdd:NF040873 68 DSLPLTVRDLVAMGR----WARRGLW----------RRLTRDD--RAAVDDALERVGLADLAgrqlgeLSGGQRQRALLA 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 582 RAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITIAHRLSTIKDAHNIVVM 640
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1110-1329 |
1.64e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 105.38 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1110 PVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGReisslnvneyrsfIALVSQEPTLYQGTVREN 1189
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1190 IILGanndVTDEQIKF-----ACQeanIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSAL 1264
Cdd:TIGR01271 507 IIFG----LSYDEYRYtsvikACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1265 DSESE-HVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGTHSELMKKNGRYAELV 1329
Cdd:TIGR01271 580 DVVTEkEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1112-1318 |
1.89e-22 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 97.44 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlNVNEYRSFIALVSQEPTLYQG-TVRENI 1190
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1191 -----ILGANNDVTDEQIkfacqeANIYDFiMSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKILLLDEATSALD 1265
Cdd:cd03265 95 yiharLYGVPGAERRERI------DELLDF-VGLLEAADRLVKT----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1266 SES-----EHVVQAaldKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:cd03265 164 PQTrahvwEYIEKL---KEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
442-680 |
2.11e-22 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 100.56 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGKTTALVGASGSGKSTIVGLV---ERfykPIEGKVYLDD---VDiSTLNVrWL---RQQIALVSQEPTLFA- 511
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGevlQD-SARGI-FLpphRRRIGYVFQEARLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 512 CTIYDNIRHGligtkweseseeqqreriYEAARKANAH-DF--------ITSL----PEGyetnvgergflLSGGQKQRI 578
Cdd:COG4148 92 LSVRGNLLYG------------------RKRAPRAERRiSFdevvellgIGHLldrrPAT-----------LSGGERQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 579 AIARAIVSDPKILLLDEATSALDTKSEGVVQAALE-VAAEGRTTIT-IAH------RLSTikdahNIVVMAQGRIVEQGT 650
Cdd:COG4148 143 AIGRALLSSPRLLLMDEPLAALDLARKAEILPYLErLRDELDIPILyVSHsldevaRLAD-----HVVLLEQGRVVASGP 217
|
250 260 270
....*....|....*....|....*....|
gi 164423939 651 HAELLAkRGAYYKLVTAQAIAAVNEMTAEE 680
Cdd:COG4148 218 LAEVLS-RPDLLPLAGGEEAGSVLEATVAA 246
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
422-654 |
2.16e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.92 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRP--DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDIS---------- 489
Cdd:PRK13631 22 LRVKNLYCVFDEKQenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGdkknnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 490 ------TLNVRWLRQQIALVSQEP--TLFACTIYDNIRHGLIGTKweseseeqqrERIYEAARKANAHDFITSLPEGYEt 561
Cdd:PRK13631 102 npyskkIKNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALG----------VKKSEAKKLAKFYLNKMGLDDSYL- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 562 nvgERG-FLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEG-VVQAALEVAAEGRTTITIAHRLSTIKD-AHNIV 638
Cdd:PRK13631 171 ---ERSpFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVI 247
|
250
....*....|....*.
gi 164423939 639 VMAQGRIVEQGTHAEL 654
Cdd:PRK13631 248 VMDKGKILKTGTPYEI 263
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1093-1318 |
2.32e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 100.30 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYPTRpeQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERFydpLSGGIFIDGREISSLNVNEyR 1169
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTllrMVAGLERI---TSGEIWIGGRVVNELEPAD-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SfIALVSQEPTLY-QGTVRENIILG-ANNDVTDEQIKFACQEANIydfIMSLpdgmNTLVGSKGALLSGGQKQRIAIARA 1247
Cdd:PRK11650 77 D-IAMVFQNYALYpHMSVRENMAYGlKIRGMPKAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1248 LIRDPKILLLDEATSALDsesehvvqaaldkaAKGR----------------TTIAVAH-RLSTIQKADIIYVFDQGRIv 1310
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLD--------------AKLRvqmrleiqrlhrrlktTSLYVTHdQVEAMTLADRVVVMNGGVA- 213
|
....*....
gi 164423939 1311 EQ-GTHSEL 1318
Cdd:PRK11650 214 EQiGTPVEV 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1093-1324 |
2.35e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.03 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlnvnEYRSFI 1172
Cdd:COG4152 1 MLELKGLTKRFGDKT---AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQEPTLYQG-TVRENII-LGANNDVTDEQIKfacqeANIYDFI--MSLPDGMNTLVGSkgalLSGGQKQRIAIARAL 1248
Cdd:COG4152 74 GYLPEERGLYPKmKVGEQLVyLARLKGLSKAEAK-----RRADEWLerLGLGDRANKKVEE----LSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1249 IRDPKILLLDEATSALDSES-EHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELMKKNGR 1324
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
425-656 |
3.17e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 97.84 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 425 ENIKHIYPS------RPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN---VRW 495
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 LRQQIALVSQE------PTLFACTIYDN-IRHGLigtkweseseeqqreRIYEAARKANAHDFI--TSLPEGYetnVGER 566
Cdd:PRK10419 87 FRRDIQMVFQDsisavnPRKTVREIIREpLRHLL---------------SLDKAERLARASEMLraVDLDDSV---LDKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 567 GFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTksegVVQA-ALEVAAE-----GRTTITIAHRLSTI-KDAHNIVV 639
Cdd:PRK10419 149 PPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL----VLQAgVIRLLKKlqqqfGTACLFITHDLRLVeRFCQRVMV 224
|
250
....*....|....*..
gi 164423939 640 MAQGRIVEQGTHAELLA 656
Cdd:PRK10419 225 MDNGQIVETQPVGDKLT 241
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1094-1305 |
3.40e-22 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 94.91 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYdPLSGGifidgrEISSLNVNEyrsfIA 1173
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-PWGSG------RIGMPEGED----LL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQGTVRENIILganndvtdeqikfacqeaniydfimslPDGMNtlvgskgalLSGGQKQRIAIARALIRDPK 1253
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY---------------------------PWDDV---------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1254 ILLLDEATSALDSESEHVVQAALDKAakGRTTIAVAHRLSTIQKADIIYVFD 1305
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHRPSLWKFHDRVLDLD 161
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
439-654 |
3.43e-22 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 96.83 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLNVRWL-RQQIALVSQEPTLFA-C 512
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTllktLMGLL----PVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPrL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 513 TIYDNIRHGLigtkweseseeqqreriyeAARKANAH---DFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPK 589
Cdd:TIGR03410 91 TVEENLLTGL-------------------AALPRRSRkipDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 590 ILLLDEATsaldtksEGV-------VQAAL-EVAAEGRTTIT-IAHRLSTIKD-AHNIVVMAQGRIVEQGTHAEL 654
Cdd:TIGR03410 152 LLLLDEPT-------EGIqpsiikdIGRVIrRLRAEGGMAILlVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
422-658 |
3.48e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.55 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIY-PSRP-DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDIST----LNVRW 495
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 LRQQIALVSQ--EPTLFACTIYDNIRHGLI--GTKWEseseeqqreriyEAARKANAHDFITSLPEgyetNVGERG-FLL 570
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMnfGVSEE------------DAKQKAREMIELVGLPE----ELLARSpFEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 571 SGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEgvvQAALEVAAE-----GRTTITIAHRLSTIKD-AHNIVVMAQGR 644
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR---KEMMEMFYKlhkekGLTTVLVTHSMEDAARyADQIVVMHKGT 223
|
250
....*....|....
gi 164423939 645 IVEQGTHAELLAKR 658
Cdd:PRK13634 224 VFLQGTPREIFADP 237
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1094-1318 |
3.76e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.41 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTrpeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDpLSGGIFIDGR-EI-------SSLNV 1165
Cdd:PRK14258 8 IKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRvEFfnqniyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1166 NEYRSFIALVSQEPTLYQGTVRENI-----ILGANNDVT-DEQIKFACQEANIYDFIMslpdgmNTLvgSKGAL-LSGGQ 1238
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVaygvkIVGWRPKLEiDDIVESALKDADLWDEIK------HKI--HKSALdLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1239 KQRIAIARALIRDPKILLLDEATSALDSES----EHVVQAALDKAAkgRTTIAVAHRLSTIQK-ADIIYVFDQ-----GR 1308
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSLRLRSE--LTMVIVSHNLHQVSRlSDFTAFFKGnenriGQ 233
|
250
....*....|
gi 164423939 1309 IVEQGTHSEL 1318
Cdd:PRK14258 234 LVEFGLTKKI 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
438-657 |
4.05e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.85 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 438 VVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRW-LRQQIALVSQEP--TLFACTI 514
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNPdnQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 515 YDNIRHGL--IGTKwesesEEQQRERIYEAARKANAHDFITSLPEgyetnvgergfLLSGGQKQRIAIARAIVSDPKILL 592
Cdd:PRK13633 104 EEDVAFGPenLGIP-----PEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 593 LDEATSALDTKS-EGVVQAALEVAAE-GRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAK 657
Cdd:PRK13633 168 FDEPTAMLDPSGrREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1096-1268 |
4.50e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1096 FRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGReisslnvneYRsfIALV 1175
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1176 SQEPTLYQG-TVRENIILG----------------ANNDVTDEQIKFA-----CQEANIYDF------IMS---LPDGM- 1223
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGdaelraleaeleeleaKLAEPDEDLERLAelqeeFEALGGWEAearaeeILSglgFPEEDl 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 164423939 1224 NTLVGSkgalLSGGQKQRIAIARALIRDPKILLLDEATSALDSES 1268
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
436-655 |
8.21e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.14 E-value: 8.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVG----LVERFYKP-IEGKVYLDDVDISTLNVRWLRQQIALVSQEPT-L 509
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEArVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 510 FACTIYDNIRHGLIGTKwESESEEQQRERIYEAARKANahdfitsLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPK 589
Cdd:PRK14247 95 PNLSIFENVALGLKLNR-LVKSKKELQERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 590 ILLLDEATSALDTKSEGVVQAA-LEVAAEgRTTITIAH---RLSTIKDAhnIVVMAQGRIVEQGTHAELL 655
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLfLELKKD-MTIVLVTHfpqQAARISDY--VAFLYKGQIVEWGPTREVF 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1094-1313 |
8.25e-22 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 95.51 E-value: 8.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRY-PTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlNVNEYRSFI 1172
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQEPTLYQG-TVRENIILGANNdvtdEQIKFACQEANIYDFIMSLpdGMNTLVGSKGALLSGGQKQRIAIARALIRD 1251
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGL----YGLKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 1252 PKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
422-655 |
9.62e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 95.92 E-value: 9.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGK-VYLDDVDISTLNVRWLRQQI 500
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEPTLF---ACTIYDNIRHGL---IGTkWESeseeqqreriYEAARKANAHDFITSLpeGYEtNVGERGFL-LSGG 573
Cdd:COG1119 81 GLVSPALQLRfprDETVLDVVLSGFfdsIGL-YRE----------PTDEQRERARELLELL--GLA-HLADRPFGtLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 574 QKQRIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEGRTT-ITIAHRLSTIKDA-HNIVVMAQGRIVEQGT 650
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGArELLLALLDKLAAEGAPTlVLVTHHVEEIPPGiTHVLLLKDGRVVAAGP 226
|
....*
gi 164423939 651 HAELL 655
Cdd:COG1119 227 KEEVL 231
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
766-1041 |
9.67e-22 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 97.11 E-value: 9.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 766 MLVGIFFSAICGAGNPtqavFFAKLIsslsRPIVNEEIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKCSERLIH 845
Cdd:cd18552 1 LALAILGMILVAATTA----ALAWLL----KPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 846 RVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIP 925
Cdd:cd18552 73 DLRNDLFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 926 ILlgcgfyrFWMIAHYQRRAKS-------AYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSS 998
Cdd:cd18552 151 LA-------ALPIRRIGKRLRKisrrsqeSMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 164423939 999 LLFAASNSLMFLAFALGFWYGGTLIAKHEY---DMFTFFIVFSSVI 1041
Cdd:cd18552 224 LSSPLMELLGAIAIALVLWYGGYQVISGELtpgEFISFITALLLLY 269
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
786-1053 |
1.07e-21 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 96.94 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 786 FFAKLISSLSRPIvnEEIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFdr 865
Cdd:cd18780 18 FFGQVIDAVTNHS--GSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFF-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 866 DENSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIPILLGCGFYRFWMIAHYQRRA 945
Cdd:cd18780 94 DVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 946 KSAYAGSASYASEAITAMRTVASLTREQDVLQHYkdslAKQQHASLISVLKSSLLFAASNSLMF----LAFALGFWYGGT 1021
Cdd:cd18780 174 QDALAAASTVAEESISNIRTVRSFAKETKEVSRY----SEKINESYLLGKKLARASGGFNGFMGaaaqLAIVLVLWYGGR 249
|
250 260 270
....*....|....*....|....*....|..
gi 164423939 1022 LiakheydmftffivfssVIFGAQSAGSVFSF 1053
Cdd:cd18780 250 L-----------------VIDGELTTGLLTSF 264
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
439-656 |
1.07e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.19 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTL-------------NVRWLRQQIALVSQ 505
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 506 EPTLFA-CTIYDNIRHGLIgtkwesESEEQQRERIYEAARKANAHDFITslpegyETNVGERGFLLSGGQKQRIAIARAI 584
Cdd:PRK10619 100 HFNLWShMTVLENVMEAPI------QVLGLSKQEARERAVKYLAKVGID------ERAQGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 585 VSDPKILLLDEATSALDTKSEG-VVQAALEVAAEGRTTITIAHRLSTIKDAHN-IVVMAQGRIVEQGTHAELLA 656
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGeVLRIMQQLAEEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFG 241
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1110-1308 |
1.26e-21 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 95.19 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1110 PVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFI--DGREISSLNVNEY------RSFIALVSQ---- 1177
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPReilalrRRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1178 -----------EPTLYQGTVRENiilganndvtdeqikfACQEA-------NIYDFIMSLPDgmntlvgskgALLSGGQK 1239
Cdd:COG4778 105 iprvsaldvvaEPLLERGVDREE----------------ARARArellarlNLPERLWDLPP----------ATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1240 QRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKA-AKGRTTIAVAHRLSTIQK-ADIIYVFDQGR 1308
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
437-626 |
1.30e-21 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 95.19 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 437 VVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDD----VDIST------LNVRwlRQQIALVSQ- 505
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQaspreiLALR--RRTIGYVSQf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 506 ------EPTLfactiyDNIRHGLI--GTKweseseeqqreriyEAARKANAHDFITSLpegyetNVGERGFLL-----SG 572
Cdd:COG4778 102 lrviprVSAL------DVVAEPLLerGVD--------------REEARARARELLARL------NLPERLWDLppatfSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 573 GQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVA-AEGRTTITIAH 626
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFH 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
424-646 |
1.33e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.34 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 424 LENIKHIYPS-RPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNvrwlRQQIAL 502
Cdd:PRK10535 7 LKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLD----ADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 503 VSQEPTLFACTIYDNIRHgligtkwESESEEQQRERIY----EAARKANAHDFITSLpeGYETNVGERGFLLSGGQKQRI 578
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSH-------LTAAQNVEVPAVYagleRKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 579 AIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIV 646
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILhQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
433-656 |
1.34e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 96.06 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 433 SRPDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVErfykPIEGKVYLDDVDISTLNVRWLRQQIALVSQEP- 507
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTlakmLAGIIE----PTSGEILINGHKLEYGDYKYRCKHIRMIFQDPn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 508 TLFactiydNIRHGlIGTkweseseeqqrerIYEAARKANahdfiTSLpegyetNVGER-----------GFL------- 569
Cdd:COG4167 98 TSL------NPRLN-IGQ-------------ILEEPLRLN-----TDL------TAEEReerifatlrlvGLLpehanfy 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 ---LSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgVVQAALEVAAE-GRTTITIAHRLSTIKD-AHNIVVMAQ 642
Cdd:COG4167 147 phmLSSGQKQRVALARALILQPKIIIADEALAALDmsVRSQ-IINLMLELQEKlGISYIYVSQHLGIVKHiSDKVLVMHQ 225
|
250
....*....|....
gi 164423939 643 GRIVEQGTHAELLA 656
Cdd:COG4167 226 GEVVEYGKTAEVFA 239
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1097-1309 |
1.63e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.51 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1097 RDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPlSGGIFIDGreisSLNVNEYRSFIALVS 1176
Cdd:PRK11247 16 NAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETP-SAGELLAG----TAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1177 QEPTLYQ-GTVRENIILGANNDVTDEQIKfACQEANIYDFIMSLPdgmntlvgskgALLSGGQKQRIAIARALIRDPKIL 1255
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGLKGQWRDAALQ-ALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1256 LLDEATSALDSESEHVVQAALDK--AAKGRTTIAVAHRLS-TIQKADIIYVFDQGRI 1309
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
439-693 |
1.75e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.37 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDIStlNVRWLRQQIALVSQEPTLFA-CTIYDN 517
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPhMTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 518 IRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIAIARAIVSDPKILLLDEAT 597
Cdd:PRK11607 112 IAFGL---KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 598 SALDTKSEGVVQaaLEVA----AEGRTTITIAH-RLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYklvTAQAIAA 672
Cdd:PRK11607 178 GALDKKLRDRMQ--LEVVdileRVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY---SAEFIGS 252
|
250 260
....*....|....*....|.
gi 164423939 673 VNEMtaeeEAALDQQEEAALI 693
Cdd:PRK11607 253 VNVF----EGVLKERQEDGLV 269
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
806-1054 |
2.01e-21 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 96.01 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 806 SIKSDASFWCLMYLMLALVQCLA----FS-VQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDrdENSAGALTSFLSTE 880
Cdd:cd18576 25 AALGGGDTASLNQIALLLLGLFLlqavFSfFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFH--ERRVGELTSRLSND 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 881 TTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIP--ILLGCGFYRFwmIAHYQRRAKSAYAGSASYASE 958
Cdd:cd18576 103 VTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPvvVLVAVLFGRR--IRKLSKKVQDELAEANTIVEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 959 AITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHEY---DMFTFfi 1035
Cdd:cd18576 181 TLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELtagDLVAF-- 258
|
250
....*....|....*....
gi 164423939 1036 vfssVIFGAQSAGSVFSFA 1054
Cdd:cd18576 259 ----LLYTLFIAGSIGSLA 273
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
422-655 |
2.01e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.15 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIA 501
Cdd:COG4604 2 IEIKNVSKRYG---GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFA-CTIYDnirhgLIG-----------TKweseseeQQRERIYEAARKANAHDFitslpegyetnvgERGFL 569
Cdd:COG4604 79 ILRQENHINSrLTVRE-----LVAfgrfpyskgrlTA-------EDREIIDEAIAYLDLEDL-------------ADRYL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 --LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSegVVQ--AALEVAAE--GRTTITIAHrlstikD-------AHN 636
Cdd:COG4604 134 deLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKH--SVQmmKLLRRLADelGKTVVIVLH------DinfascyADH 205
|
250
....*....|....*....
gi 164423939 637 IVVMAQGRIVEQGTHAELL 655
Cdd:COG4604 206 IVAMKDGRVVAQGTPEEII 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1111-1321 |
2.24e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.48 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEyRSfIALVSQEPTLY-QGTVREN 1189
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-ICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1190 I-----ILGANNDVTDEQIKFACQEANIYDFIMSLPDGmntlvgskgalLSGGQKQRIAIARALIRDPKILLLDEATSAL 1264
Cdd:PRK11432 99 VgyglkMLGVPKEERKQRVKEALELVDLAGFEDRYVDQ-----------ISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1265 DS-------ESEHVVQAALdkaakGRTTIAVAHRLS-TIQKADIIYVFDQGRIVEQGTHSELMKK 1321
Cdd:PRK11432 168 DAnlrrsmrEKIRELQQQF-----NITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1112-1336 |
2.33e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 95.23 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPL-----SGGIFIDGREISSLNVN--EYRSFIALVSQEPTLYQG 1184
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 TVRENI-----ILGANNDVtDEQIKFACQEANIYDfimSLPDGMNTlvgsKGALLSGGQKQRIAIARALIRDPKILLLDE 1259
Cdd:PRK14243 106 SIYDNIaygarINGYKGDM-DELVERSLRQAALWD---EVKDKLKQ----SGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1260 ATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVFDQGRIVEQGthselmkknGRYAELVNLQSLEK 1336
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG---------GRYGYLVEFDRTEK 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1099-1318 |
2.46e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 99.76 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1099 VHFRYPTRpEQPVLRGLNLSIQPGQYVALVGASGCGKSTT----IALLERFYDPLSGGIFIDGREISSLNVNEYRSF--- 1171
Cdd:COG4172 14 VAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1172 -IALVSQEPT-----LYqgTVRENI--ILGANNDVTDEQIKFACQEaniydfimslpdgMNTLVGSKGAL---------L 1234
Cdd:COG4172 93 rIAMIFQEPMtslnpLH--TIGKQIaeVLRLHRGLSGAAARARALE-------------LLERVGIPDPErrldayphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1235 SGGQKQRIAIARALIRDPKILLLDEATSALDsesehV-VQA---ALDKAAKGRTTIAVA---HRLSTIQK-ADIIYVFDQ 1306
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALD-----VtVQAqilDLLKDLQRELGMALLlitHDLGVVRRfADRVAVMRQ 232
|
250
....*....|..
gi 164423939 1307 GRIVEQGTHSEL 1318
Cdd:COG4172 233 GEIVEQGPTAEL 244
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1094-1319 |
2.56e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.41 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlNVNEYRSFIA 1173
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQ----EPTLyqgTVRENI-ILGANNDVTDEQIKFACQeaNIYDFiMSLPDGMNTLVGSkgalLSGGQKQRIAIARAL 1248
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLlVFGRYFGLSAAAARALVP--PLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1249 IRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELM 1319
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
421-658 |
4.59e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.90 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIY-PSRP-DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDI----STLNVR 494
Cdd:PRK13641 2 SIKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 495 WLRQQIALVSQ--EPTLFACTIYDNIRHGligtkweseseeQQRERIYEAARKANAHDFITSLpeGYETNVGERG-FLLS 571
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFG------------PKNFGFSEDEAKEKALKWLKKV--GLSEDLISKSpFELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 572 GGQKQRIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQG 649
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHA 227
|
....*....
gi 164423939 650 THAELLAKR 658
Cdd:PRK13641 228 SPKEIFSDK 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1094-1319 |
5.01e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.99 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTrpeQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIA 1173
Cdd:COG4604 2 IEIKNVSKRYGG---KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPT----LyqgTVRENIILG-----------ANNDVTDEQIKFacqeaniydfiMSLPDgmntlvgskgaL----- 1233
Cdd:COG4604 79 ILRQENHinsrL---TVRELVAFGrfpyskgrltaEDREIIDEAIAY-----------LDLED-----------Ladryl 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1234 --LSGGQKQRIAIARALIRDPKILLLDEATSALDseSEHVVQ--AALDKAA--KGRTTIAVAHRLS-TIQKADIIYVFDQ 1306
Cdd:COG4604 134 deLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD--MKHSVQmmKLLRRLAdeLGKTVVIVLHDINfASCYADHIVAMKD 211
|
250
....*....|...
gi 164423939 1307 GRIVEQGTHSELM 1319
Cdd:COG4604 212 GRVVAQGTPEEII 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1094-1313 |
5.49e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.14 E-value: 5.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYD-----PLSGGIFIDGREISSLNVN-- 1166
Cdd:PRK14267 5 IETVNLRVYYG---SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1167 EYRSFIALVSQEPTLY-QGTVRENIILG-------ANNDVTDEQIKFACQEANIYDfimSLPDGMNTLVGSkgalLSGGQ 1238
Cdd:PRK14267 82 EVRREVGMVFQYPNPFpHLTIYDNVAIGvklnglvKSKKELDERVEWALKKAALWD---EVKDRLNDYPSN----LSGGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1239 KQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1107-1299 |
5.59e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 5.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1107 PEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGReisslnvneyrSFIALVSQ---EPTLYQ 1183
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQrseVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1184 GTVRENIILGANNDVTDEQIKFACQEANIYDFIMSLpdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSA 1263
Cdd:NF040873 72 LTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 164423939 1264 LDSESEHVVQAAL-DKAAKGRTTIAVAHRLSTIQKAD 1299
Cdd:NF040873 150 LDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
422-628 |
5.89e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.08 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRpdvVVMEDVSLVIPAGKTTALVGASGSGKSTIV-------GLVERFYkpIEGKVYLDDVDI--STLN 492
Cdd:PRK14243 11 LRTENLNVYYGSF---LAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR--VEGKVTFHGKNLyaPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 493 VRWLRQQIALVSQEPTLFACTIYDNIRHG--LIGTKweseseEQQRERIYEAARKANAHDFItslpegyETNVGERGFLL 570
Cdd:PRK14243 86 PVEVRRRIGMVFQKPNPFPKSIYDNIAYGarINGYK------GDMDELVERSLRQAALWDEV-------KDKLKQSGLSL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 571 SGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRL 628
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
427-654 |
8.05e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.56 E-value: 8.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVrwlrQQ--IALVS 504
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI----QQrdICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 505 QEPTLFA-CTIYDNIRHGLigtKWESESEEQQRERIYEAARkanahdfITSLpEGYETNVGERgflLSGGQKQRIAIARA 583
Cdd:PRK11432 85 QSYALFPhMSLGENVGYGL---KMLGVPKEERKQRVKEALE-------LVDL-AGFEDRYVDQ---ISGGQQQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 584 IVSDPKILLLDEATSALD-----TKSEGV--VQAALEVaaegrTTITIAHRLS---TIKDAhnIVVMAQGRIVEQGTHAE 653
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDanlrrSMREKIreLQQQFNI-----TSLYVTHDQSeafAVSDT--VIVMNKGKIMQIGSPQE 223
|
.
gi 164423939 654 L 654
Cdd:PRK11432 224 L 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1098-1319 |
9.75e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.49 E-value: 9.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1098 DVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREIS-------SLNVNE--- 1167
Cdd:PRK10619 10 DLHKRYG---EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVADknq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1168 ---YRSFIALVSQEPTLYQG-TVRENI------ILGANNDVTDEQIKFACQEANIYDfimslpdgmnTLVGSKGALLSGG 1237
Cdd:PRK10619 87 lrlLRTRLTMVFQHFNLWSHmTVLENVmeapiqVLGLSKQEARERAVKYLAKVGIDE----------RAQGKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1238 QKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQKADIIYVF-DQGRIVEQGTH 1315
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAP 236
|
....
gi 164423939 1316 SELM 1319
Cdd:PRK10619 237 EQLF 240
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1121-1319 |
1.02e-20 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 95.56 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1121 PGQYV-ALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISS----LNVNEYRSFIALVSQEPTLY-QGTVRENIILGA 1194
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFpHLSVRGNLRYGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1195 NN-DVTDEQIKFAcqeaNIYDFImslpdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQ 1273
Cdd:TIGR02142 101 KRaRPSERRISFE----RVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 164423939 1274 AALDKAAK--GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELM 1319
Cdd:TIGR02142 172 PYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
421-648 |
1.31e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.00 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIYP-SRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRwlRqq 499
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 iALVSQEPTLFA-CTIYDNIRHGLigtkweseseeqQRERIYEAARKANAHDFITSlpegyetnVGERGFL------LSG 572
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNVAFGL------------RLRGVPKAERRARAEELLAL--------VGLADFArrriwqLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 573 GQKQRIAIARAIVSDPKILLLDEATSALD--TKsEGVVQAALEVAAEGRTTI-TIAHR------LSTikdahNIVVMA-- 641
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDalTR-EQMQELLLDVWQRTGKGVfLITHSveealfLAT-----RLVVMSpg 211
|
....*..
gi 164423939 642 QGRIVEQ 648
Cdd:COG4525 212 PGRIVER 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1094-1321 |
1.38e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 91.05 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRyptRPEQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfYDPLSGGIFIDGREISSLNVNE-YR 1169
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTlakTIMGHPK-YEVTEGEILFKGEDITDLPPEErAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1170 SFIALVSQEPTLYQGtvreniilganndvtdeqIKFAcqeaniyDFIMSLPDGmntlvgskgalLSGGQKQRIAIARALI 1249
Cdd:cd03217 77 LGIFLAFQYPPEIPG------------------VKNA-------DFLRYVNEG-----------FSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1250 RDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAH--RLSTIQKADIIYVFDQGRIVEQGTHS---ELMKK 1321
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElalEIEKK 198
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1108-1318 |
1.54e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.10 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLErfyDPLSGGIFIDGREISSLNVNEyRSfIALVSQEPTLY-Q 1183
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTllrMIAGLE---DITSGDLFIGEKRMNDVPPAE-RG-VGMVFQSYALYpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1184 GTVRENI-----ILGANNDVTDEQIKfacQEANIYDfimslpdgMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLD 1258
Cdd:PRK11000 90 LSVAENMsfglkLAGAKKEEINQRVN---QVAEVLQ--------LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1259 EATSALDSESEHVVQAALDKAAK--GRTTIAVAH-RLSTIQKADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
440-655 |
1.59e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.87 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 440 MEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQ----QIALVSQEPTLFA-CTI 514
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 515 YDNIRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIAIARAIVSDPKILLLD 594
Cdd:PRK10070 124 LDNTAFGM---ELAGINAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 595 EATSALDTKSEGVVQAALE--VAAEGRTTITIAHRL-STIKDAHNIVVMAQGRIVEQGTHAELL 655
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
420-656 |
1.66e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.53 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 420 GTIRLENIKHIYPSRP--DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDIST-----LN 492
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 493 VRWLRQQIALVSQEP--TLFACTIYDNIRHGLIGTKWESEseeqqreriyEAARKANAHDFITSLPEGYetnVGERGFLL 570
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQ----------EAYKKVPELLKLVQLPEDY---VKRSPFEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 571 SGGQKQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAE-GRTTITIAHRLSTI-KDAHNIVVMAQGRIVE 647
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKgEEDFINLFERLNKEyKKRIIMVTHNMDQVlRIADEVIVMHEGKVIS 231
|
....*....
gi 164423939 648 QGTHAELLA 656
Cdd:PRK13645 232 IGSPFEIFS 240
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
421-655 |
1.71e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.93 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIYPSRpdvVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQI 500
Cdd:PRK10575 11 TFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQE-PTLFACTIYDNIR------HGLIGtKWESESEEQQRERIYEAARKANAHDFITSlpegyetnvgergflLSGG 573
Cdd:PRK10575 88 AYLPQQlPAAEGMTVRELVAigrypwHGALG-RFGAADREKVEEAISLVGLKPLAHRLVDS---------------LSGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 574 QKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGR--TTITIAHRLS-TIKDAHNIVVMAQGRIVEQGT 650
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGT 231
|
....*
gi 164423939 651 HAELL 655
Cdd:PRK10575 232 PAELM 236
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1108-1321 |
1.80e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.05 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERfYDPLSGGIFIDGREISSLNVNEyRS----FIALvsQEPT 1180
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDILELSPDE-RAragiFLAF--QYPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1181 LYQG-TVReNIILGANNDVTDEQI------KFACQEANIYDFIMSLPD-GMNtlVGskgalLSGGQKQRIAIARALIRDP 1252
Cdd:COG0396 88 EIPGvSVS-NFLRTALNARRGEELsareflKLLKEKMKELGLDEDFLDrYVN--EG-----FSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1253 KILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAH--RLSTIQKADIIYVFDQGRIVEQGThSELMKK 1321
Cdd:COG0396 160 KLAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KELALE 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
420-656 |
2.29e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 420 GTIRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLNVrW 495
Cdd:COG1137 2 MTLEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLV----KPDSGRIFLDGEDITHLPM-H 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 LRQQ--IALVSQEPTLFA-CTIYDNIR-----HGLigTKweseseeqqreriYEAARKANA--HDF-ITSLpegyetnVG 564
Cdd:COG1137 74 KRARlgIGYLPQEASIFRkLTVEDNILavlelRKL--SK-------------KEREERLEEllEEFgITHL-------RK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 565 ERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAalevaaegrttitIAHRLST------IKDaHN-- 636
Cdd:COG1137 132 SKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQK-------------IIRHLKErgigvlITD-HNvr 197
|
250 260
....*....|....*....|....*...
gi 164423939 637 ----IV----VMAQGRIVEQGTHAELLA 656
Cdd:COG1137 198 etlgICdrayIISEGKVLAEGTPEEILN 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
422-656 |
2.59e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.57 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvvMEdVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRwlRQQIA 501
Cdd:PRK10771 2 LKLTDITWLYHHLP----MR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFA-CTIYDNIRHGL-IGTKweseSEEQQRERIYEAARKANAHDFITSLPegyetnvGErgflLSGGQKQRIA 579
Cdd:PRK10771 75 MLFQENNLFShLTVAQNIGLGLnPGLK----LNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 580 IARAIVSDPKILLLDEATSALDT--KSEgVVQAALEVAAEGRTT-ITIAHRLStikDAHNI----VVMAQGRIVEQGTHA 652
Cdd:PRK10771 140 LARCLVREQPILLLDEPFSALDPalRQE-MLTLVSQVCQERQLTlLMVSHSLE---DAARIaprsLVVADGRIAWDGPTD 215
|
....
gi 164423939 653 ELLA 656
Cdd:PRK10771 216 ELLS 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
422-649 |
3.86e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 90.50 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENI-KHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTlNVRWLRQQI 500
Cdd:cd03266 2 ITADALtKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEPTLFA-CTIYDNIR-----HGLIGTKweseseeqQRERIYEAARKANAHDFItslpegyETNVGErgflLSGGQ 574
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEyfaglYGLKGDE--------LTARLEELADRLGMEELL-------DRRVGG----FSTGM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALD-TKSEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQG 649
Cdd:cd03266 142 RQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
141-395 |
4.23e-20 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 92.23 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 141 LARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKV 220
Cdd:cd07346 38 LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 221 GLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQ 300
Cdd:cd07346 118 LQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 301 DRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQGSRFLLSGDTELRKILTVMMSVMIGAFNLGNIAP 380
Cdd:cd07346 198 EREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLAN 277
|
250
....*....|....*
gi 164423939 381 NLQAFVTALGAAAKI 395
Cdd:cd07346 278 LYNQLQQALASLERI 292
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
786-1064 |
4.71e-20 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 92.19 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 786 FFAKLISSLSRPIVNEEIRASiksdASFWCLMYLM-LALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFD 864
Cdd:cd18573 18 AIGKLIDVASKESGDIEIFGL----SLKTFALALLgVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 865 RdeNSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIPILLGCG--FYRFwmIAHYQ 942
Cdd:cd18573 94 K--NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAvfYGRY--VRKLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 943 RRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASlISVLKSSLLFAASNSLM-FLAFALGFWYGGT 1021
Cdd:cd18573 170 KQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLA-KKEALASGLFFGSTGFSgNLSLLSVLYYGGS 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 164423939 1022 LIAKHEY---DMFTFFI--VFSSVifgaqSAGSVFSFAPDMGKATEAA 1064
Cdd:cd18573 249 LVASGELtvgDLTSFLMyaVYVGS-----SVSGLSSFYSELMKGLGAS 291
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1097-1314 |
5.16e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 92.72 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1097 RDVHFRYPTR-----PEQPV--LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREI---SSLNVN 1166
Cdd:PRK11308 9 IDLKKHYPVKrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1167 EYRSFIALVSQEPtlYqGTV--RENI--ILGA----NNDVTDEQIKFACQEaniydfimslpdgMNTLVGSKGA------ 1232
Cdd:PRK11308 89 LLRQKIQIVFQNP--Y-GSLnpRKKVgqILEEplliNTSLSAAERREKALA-------------MMAKVGLRPEhydryp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1233 -LLSGGQKQRIAIARALIRDPKILLLDEATSALD-SESEHVVQAALD-KAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGR 1308
Cdd:PRK11308 153 hMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQAQVLNLMMDlQQELGLSYVFISHDLSVVEHiADEVMVMYLGR 232
|
....*.
gi 164423939 1309 IVEQGT 1314
Cdd:PRK11308 233 CVEKGT 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
439-650 |
5.70e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.22 E-value: 5.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRwlRQQIALVSQEPTLFA-CTIYDN 517
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRhMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 518 IRHGLigtkweseseeqqreRIYEAARKANAHDF---ITSLPEGYE-TNVGER-GFLLSGGQKQRIAIARAIVSDPKILL 592
Cdd:PRK10851 95 IAFGL---------------TVLPRRERPNAAAIkakVTQLLEMVQlAHLADRyPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 593 LDEATSALDTKsegvvqaaleVAAEGR------------TTITIAH-RLSTIKDAHNIVVMAQGRIVEQGT 650
Cdd:PRK10851 160 LDEPFGALDAQ----------VRKELRrwlrqlheelkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
440-633 |
6.51e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.61 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 440 MEDVSLVIPAGKTTALVGASGSGKSTIVGLVERF--YKP---IEGKVYLDDVDI---STLNVRwLRQQIALVSQEPTLFA 511
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIyspRTDTVD-LRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 512 CTIYDNIRHGL--IGTKWESESEEQQRERIYEAARKANAHDFItslpegYETNVGergflLSGGQKQRIAIARAIVSDPK 589
Cdd:PRK14239 100 MSIYENVVYGLrlKGIKDKQVLDEAVEKSLKGASIWDEVKDRL------HDSALG-----LSGGQQQRVCIARVLATSPK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 164423939 590 ILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRL---STIKD 633
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRISD 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
364-660 |
7.97e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.26 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 364 VMMSVmiGAFnlGNIAPNLQAFVTALGAAAKIYNTIDR--------ESPIDSSSEEGGKLENVVGTIRLENIKhIYpsRP 435
Cdd:COG4178 301 LMQAA--SAF--GQVQGALSWFVDNYQSLAEWRATVDRlagfeealEAADALPEAASRIETSEDGALALEDLT-LR--TP 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 D-VVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLverfYKPIEGKVYLDDvdistlnvrwlRQQIALVSQEP--- 507
Cdd:COG4178 374 DgRPLLEDLSLSLKPGERLLITGPSGSGKSTllraIAGL----WPYGSGRIARPA-----------GARVLFLPQRPylp 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 508 --TLFACTIYDNIRHgligtkweseseEQQRERIYEAARKANAHDFITSLPEgyETNVGERgflLSGGQKQRIAIARAIV 585
Cdd:COG4178 439 lgTLREALLYPATAE------------AFSDAELREALEAVGLGHLAERLDE--EADWDQV---LSLGEQQRLAFARLLL 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 586 SDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRlSTIKDAHNIVVmaqgRIVEQGTHAELLAKRGA 660
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-STLAAFHDRVL----ELTGDGSWQLLPAEAPA 571
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
422-649 |
8.69e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 89.26 E-value: 8.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNvrwlRQQIA 501
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLF-ACTIYDNIRH--GLIGTKweseseeqqrerIYEAARkaNAHDFITSLP-EGYETNVGERgflLSGGQKQR 577
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlaQLKGLK------------KEEARR--RIDEWLERLElSEYANKRVEE---LSKGNQQK 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 578 IAIARAIVSDPKILLLDEATSALDTKSEGVV-QAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQG 649
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNVELLkDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-656 |
8.78e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.93 E-value: 8.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDI---STLNVR---WLRQQIALVSQEPTLFAC 512
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggrSIFNYRdvlEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 513 TIYDNIRHGLIGTKWESESeeqqreriyEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILL 592
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRK---------EFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 593 LDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLS-TIKDAHNIVVMAQGRIVEQGTHAELLA 656
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1092-1259 |
9.09e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.09 E-value: 9.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1092 GTIEFRDVHFRYPTRPeqpVLRGLNLSIQPGQYVALVGASGCGKSTTiallerFY------DPLSGGIFIDGREISSLNV 1165
Cdd:COG1137 2 MTLEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1166 NEY-RSFIALVSQEPTLYQG-TVRENI--ILGANNdVTDEQIKfACQEANIYDFimslpdGMNTLVGSKGALLSGGQKQR 1241
Cdd:COG1137 73 HKRaRLGIGYLPQEASIFRKlTVEDNIlaVLELRK-LSKKERE-ERLEELLEEF------GITHLRKSKAYSLSGGERRR 144
|
170
....*....|....*...
gi 164423939 1242 IAIARALIRDPKILLLDE 1259
Cdd:COG1137 145 VEIARALATNPKFILLDE 162
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1094-1319 |
9.64e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 90.67 E-value: 9.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTR------PEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNvNE 1167
Cdd:COG4167 5 LEVRNLSKTFKYRtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD-YK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1168 YRS-FIALVSQEP--TLyqgTVRENI--ILGA----NNDVTDEQikfacQEANIYDFIMS---LPDGMNTlvgsKGALLS 1235
Cdd:COG4167 84 YRCkHIRMIFQDPntSL---NPRLNIgqILEEplrlNTDLTAEE-----REERIFATLRLvglLPEHANF----YPHMLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1236 GGQKQRIAIARALIRDPKILLLDEATSALD-SESEHVVQAALDKAAK-GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQ 1312
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDmSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEY 231
|
....*..
gi 164423939 1313 GTHSELM 1319
Cdd:COG4167 232 GKTAEVF 238
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1116-1319 |
9.84e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 92.47 E-value: 9.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1116 NLSIQPGQYVALVGASGCGKST---TIALLERfydPLSGGIFIDGR----EISSLNVNEYRSFIALVSQEPTL---YqgT 1185
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTllrAIAGLER---PDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLfphL--S 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1186 VRENIILGAnndvtdeqiKFACQEANIYDF--IMSLPdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSA 1263
Cdd:COG4148 94 VRGNLLYGR---------KRAPRAERRISFdeVVELL-GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1264 LDSESEHVVQAALDKAAKgRTTIA---VAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELM 1319
Cdd:COG4148 164 LDLARKAEILPYLERLRD-ELDIPilyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1094-1310 |
1.07e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.18 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQ-PVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVN------ 1166
Cdd:PRK10535 5 LELKDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADalaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1167 -EYRSFI-----------ALVSQE-PTLYQGTVRENiilganndvtdeqikfacQEANIYDFIMSLpdGMNTLVGSKGAL 1233
Cdd:PRK10535 85 rEHFGFIfqryhllshltAAQNVEvPAVYAGLERKQ------------------RLLRAQELLQRL--GLEDRVEYQPSQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1234 LSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQKADIIYVFDQGRIV 1310
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
380-658 |
1.08e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 96.00 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 380 PNLQAFVTAL----GAAAKIYNTIdresPIDSSSEEGGKLENVV-GTIRLENIKHIYpsRPDV-VVMEDVSLVIPAGKTT 453
Cdd:PTZ00243 1266 PELDEEVDALerrtGMAADVTGTV----VIEPASPTSAAPHPVQaGSLVFEGVQMRY--REGLpLVLRGVSFRIAPREKV 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 454 ALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNIRHGLIGTKwesesee 533
Cdd:PTZ00243 1340 GIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASS------- 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 534 qqrERIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVS-DPKILLLDEATSALDTKSEGVVQAAL 612
Cdd:PTZ00243 1413 ---AEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATV 1489
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 164423939 613 EVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKR 658
Cdd:PTZ00243 1490 MSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
426-655 |
1.25e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.11 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 426 NIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYK------PIEGKVYLDDVDISTLNVRWLRQQ 499
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEPTLFA-CTIYDNIRHGLI--GTKWESESEEQQRERIYEAARKANAHDFITSlPEGYetnvgergflLSGGQKQ 576
Cdd:PRK14246 92 VGMVFQQPNPFPhLSIYDNIAYPLKshGIKEKREIKKIVEECLRKVGLWKEVYDRLNS-PASQ----------LSGGQQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 577 RIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTI-KDAHNIVVMAQGRIVEQGTHAELL 655
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
423-602 |
1.74e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 88.31 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 423 RLENIKHIYPSRPDVvvmEDVSLVIPAGKTTALVGASGSGKST----IVG-LVERFykPIEGKVYLDDVDISTLNVRwlR 497
Cdd:COG4136 3 SLENLTITLGGRPLL---APLSLTVAPGEILTLMGPSGSGKSTllaaIAGtLSPAF--SASGEVLLNGRRLTALPAE--Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 QQIALVSQEPTLFA-CTIYDNIRHGLIGTkweseseeqqrerIYEAARKANAHDFITS--LPEGYETNVGErgflLSGGQ 574
Cdd:COG4136 76 RRIGILFQDDLLFPhLSVGENLAFALPPT-------------IGRAQRRARVEQALEEagLAGFADRDPAT----LSGGQ 138
|
170 180
....*....|....*....|....*...
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALDT 602
Cdd:COG4136 139 RARVALLRALLAEPRALLLDEPFSKLDA 166
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1094-1314 |
2.38e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.99 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPEQP-------------------VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIF 1154
Cdd:COG1134 5 IEVENVSKSYRLYHEPSrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1155 IDGReISSLnvneyrsfIAL-VSQEPTLyqgTVRENI-----ILGANNDVTDEQIKFACQEANIYDFImslpdgmNTLVG 1228
Cdd:COG1134 85 VNGR-VSAL--------LELgAGFHPEL---TGRENIylngrLLGLSRKEIDEKFDEIVEFAELGDFI-------DQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1229 SkgalLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAAL-DKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQ 1306
Cdd:COG1134 146 T----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIrELRESGRTVIFVSHSMGAVRRlCDRAIWLEK 221
|
....*...
gi 164423939 1307 GRIVEQGT 1314
Cdd:COG1134 222 GRLVMDGD 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
422-656 |
2.98e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVV--VMEDVSLVIPAGKTTALVGASGSGKSTIV-----------GLVERFY-------KPIEGKV 481
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnalllpdtGTIEWIFkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 482 YLDDVDISTL------NVRWLRQQIALVSQ--EPTLFACTIYDNIRHGLI--GTKWEseseeqqreriyEAARKANAHDF 551
Cdd:PRK13651 83 VLEKLVIQKTrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVsmGVSKE------------EAKKRAAKYIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 552 ITSLPEGYetnVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDtkSEGVVQAAL---EVAAEGRTTITIAHRL 628
Cdd:PRK13651 151 LVGLDESY---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD--PQGVKEILEifdNLNKQGKTIILVTHDL 225
|
250 260
....*....|....*....|....*....
gi 164423939 629 -STIKDAHNIVVMAQGRIVEQGTHAELLA 656
Cdd:PRK13651 226 dNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1105-1313 |
3.02e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.83 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1105 TRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTL-YQ 1183
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1184 GTVRENIILG--------ANNDVTDEQ-IKFACQEANIYDFImslpdgmNTLVGSkgalLSGGQKQRIAIARALIRDPKI 1254
Cdd:PRK09536 92 FDVRQVVEMGrtphrsrfDTWTETDRAaVERAMERTGVAQFA-------DRPVTS----LSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1255 LLLDEATSALDseSEHVVQA---ALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:PRK09536 161 LLLDEPTASLD--INHQVRTlelVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
442-649 |
3.96e-19 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 86.84 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGKTTALVGASGSGKSTIVGLV--ERFYKPIEGKVYLDDVDISTlnvRWLRQQIALVSQEPTLFAC-TIYDNI 518
Cdd:cd03213 27 NVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHPTlTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 519 RHgligtkweseseeqqreriyeAARKanahdfitslpegyetnvgeRGflLSGGQKQRIAIARAIVSDPKILLLDEATS 598
Cdd:cd03213 104 MF---------------------AAKL--------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 164423939 599 ALDTKSE-GVVQAALEVAAEGRTTITIAHRLST--IKDAHNIVVMAQGRIVEQG 649
Cdd:cd03213 141 GLDSSSAlQVMSLLRRLADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1100-1313 |
6.52e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 87.39 E-value: 6.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1100 HFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGrEISSLNVNEYRSFIALV-SQE 1178
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVfGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1179 PTL-YQGTVRENIILgaNNDVTD-EQIKFACQEANIYDfIMSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKILL 1256
Cdd:cd03267 104 TQLwWDLPVIDSFYL--LAAIYDlPPARFKKRLDELSE-LLDLEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1257 LDEATSALDSESEHVVQAALDKAAKGR--TTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
422-650 |
6.82e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.65 E-value: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPS-RP-DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTL----NVRW 495
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 LRQQIALVSQ--EPTLFACTIYDNIRHGligtkwesesEEQQRERIYEAARKANAHDFITSLPEgyetNVGERG-FLLSG 572
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG----------PQNFGVSQEEAEALAREKLALVGISE----SLFEKNpFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 573 GQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITIAHRLSTIKDAHNIV-VMAQGRIVEQGT 650
Cdd:PRK13649 149 GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFkKLHQSGMTIVLVTHLMDDVANYADFVyVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
422-656 |
9.35e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.12 E-value: 9.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN-VRWLRQQI 500
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEP-TLFAC-TIYDNIRHGligtkweSESEEQQRERIYEAARKANAhdfitslpegyETNVGERGF----LLSGGQ 574
Cdd:PRK13644 80 GIVFQNPeTQFVGrTVEEDLAFG-------PENLCLPPIEIRKRVDRALA-----------EIGLEKYRHrspkTLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAE 653
Cdd:PRK13644 142 GQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPEN 221
|
...
gi 164423939 654 LLA 656
Cdd:PRK13644 222 VLS 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1094-1321 |
9.97e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.25 E-value: 9.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYptRPEQP----VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLN----V 1165
Cdd:PRK13643 2 IKFEKVNYTY--QPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1166 NEYRSFIALVSQEP--TLYQGTVRENIILGANN-DVTDEQI-KFACQEANIYdfimslpdGMNTLVGSKGAL-LSGGQKQ 1240
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfGIPKEKAeKIAAEKLEMV--------GLADEFWEKSPFeLSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1241 RIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK-GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV 231
|
...
gi 164423939 1319 MKK 1321
Cdd:PRK13643 232 FQE 234
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1094-1321 |
1.08e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.12 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlNVNEYRSFIA 1173
Cdd:PRK13536 42 IDLAGVSKSYG---DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTL-YQGTVRENIILGANndvtdeqiKFACQEANIYDFIMSLPD--GMNTLVGSKGALLSGGQKQRIAIARALIR 1250
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLVFGR--------YFGMSTREIEAVIPSLLEfaRLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1251 DPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELMKK 1321
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1101-1332 |
1.48e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 88.37 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1101 FRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTI----ALLERFYDPLSGGIFIDGREISSL------------N 1164
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVthfnGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkikN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1165 VNEYRSFIALVSQEP--TLYQGTVRENIILGAnndVTDEQIKF-ACQEANIYDFIMSLPDgmnTLVGSKGALLSGGQKQR 1241
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFGP---VALGVKKSeAKKLAKFYLNKMGLDD---SYLERSPFGLSGGQKRR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1242 IAIARALIRDPKILLLDEATSALDSESEH-VVQAALDKAAKGRTTIAVAHRLSTI-QKADIIYVFDQGRIVEQGTHSE-- 1317
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEif 264
|
250 260 270
....*....|....*....|....*....|....*..
gi 164423939 1318 ----------------------LMKKNGRYAELVNLQ 1332
Cdd:PRK13631 265 tdqhiinstsiqvprviqvindLIKKDPKYKKLYQKQ 301
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1110-1318 |
1.54e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.88 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1110 PVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSF-IALVSQEPTLYQG-TVR 1187
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1188 ENIILG-ANNDVTDEQIKFACQEANIydfimSL-PDgmntlvgSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALD 1265
Cdd:PRK15439 105 ENILFGlPKRQASMQKMKQLLAALGC-----QLdLD-------SSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1266 -SESEHVVQAALDKAAKGRTTIAVAHRLSTI-QKADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK15439 173 pAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1094-1310 |
1.62e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.47 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpeqPV--LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSF 1171
Cdd:COG3845 6 LELRGITKRFG-----GVvaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1172 -IALVSQEPTLYQG-TVRENIILGA--------NNDVTDEQIKFACQEaniYDFIMSLpdgmNTLVGSkgalLSGGQKQR 1241
Cdd:COG3845 81 gIGMVHQHFMLVPNlTVAENIVLGLeptkggrlDRKAARARIRELSER---YGLDVDP----DAKVED----LSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1242 IAIARALIRDPKILLLDEATSAL-DSESEHVVqAALDK-AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIV 1310
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1116-1319 |
2.11e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 89.32 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1116 NLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSF----IALVSQEPTLY-QGTVRENI 1190
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMpHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1191 ILG---ANNDVTDEQIKF--ACQEANIYDFIMSLPDGmntlvgskgalLSGGQKQRIAIARALIRDPKILLLDEATSALD 1265
Cdd:PRK10070 128 AFGmelAGINAEERREKAldALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1266 SESEHVVQAALDK--AAKGRTTIAVAHRL-STIQKADIIYVFDQGRIVEQGTHSELM 1319
Cdd:PRK10070 197 PLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
141-395 |
2.24e-18 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 87.15 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 141 LARLVLYFVYLAIGEFVTMYITTVGfiysGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKV 220
Cdd:cd18575 39 FLLLLAVALVLALASALRFYLVSWL----GERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 221 GLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQ 300
Cdd:cd18575 115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTRE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 301 DRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQGSRFLLSGDTELRKILTVMMSVMIGAFNLGNIAP 380
Cdd:cd18575 195 DAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSE 274
|
250
....*....|....*
gi 164423939 381 NLQAFVTALGAAAKI 395
Cdd:cd18575 275 VWGDLQRAAGAAERL 289
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1111-1313 |
2.73e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.15 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTT-IALLERFydPLSGGIFIDGREISSLNVNE---YRSFIALVSQEP--TLyqg 1184
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPnsSL--- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 TVRENI--ILGANNDVTDEQIKFACQEANIYDFIMSLpdGMNTLVGSK-GALLSGGQKQRIAIARALIRDPKILLLDEAT 1261
Cdd:PRK15134 376 NPRLNVlqIIEEGLRVHQPTLSAAQREQQVIAVMEEV--GLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1262 SALDseseHVVQA---ALDKAAKGRTTIA---VAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:PRK15134 454 SSLD----KTVQAqilALLKSLQQKHQLAylfISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1112-1308 |
2.86e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYdP---LSGGIFIDGREISSLNVNEY-RSFIALVSQEPTLYQG-TV 1186
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 RENIILGA---NNDVTD-EQIKFACQEaniydFIMSLPDGMNtlVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATS 1262
Cdd:PRK13549 100 LENIFLGNeitPGGIMDyDAMYLRAQK-----LLAQLKLDIN--PATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 164423939 1263 AL-DSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGR 1308
Cdd:PRK13549 173 SLtESETAVLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
422-646 |
3.11e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.70 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSrpdVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDD--VDISTLNVRwLRQQ 499
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDA-IALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEPTLF-ACTIYDNIRHGLIGTKWESESeeqqreriYEAARKAnahdfITSLPEGY------ETNVGErgflLSG 572
Cdd:COG3845 82 IGMVHQHFMLVpNLTVAENIVLGLEPTKGGRLD--------RKAARAR-----IRELSERYgldvdpDAKVED----LSV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 573 GQKQRIAIARAIVSDPKILLLDEATSALdTKSEgvVQAALEV----AAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIV 646
Cdd:COG3845 145 GEQQRVEILKALYRGARILILDEPTAVL-TPQE--ADELFEIlrrlAAEGKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1111-1319 |
3.68e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.19 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQG-TVREN 1189
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1190 IILGAnndvTDEQIKFACQEANIYDFIMSL--PDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSE 1267
Cdd:PRK10253 102 VARGR----YPHQPLFTRWRKEDEEAVTKAmqATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1268 SEHVVQAALDK--AAKGRTTIAVAHRLS-TIQKADIIYVFDQGRIVEQGTHSELM 1319
Cdd:PRK10253 178 HQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1112-1318 |
4.20e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.20 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE-YRSFIALVSQE----PTLyqgTV 1186
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 RENIILG---ANNDVTDEQ--IKFACQE-ANIydfimslpdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEA 1260
Cdd:PRK11288 97 AENLYLGqlpHKGGIVNRRllNYEAREQlEHL---------GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1261 TSALDS-ESEHVVQAALDKAAKGRTTIAVAHRLSTI-QKADIIYVFDQGRIVEqgTHSEL 1318
Cdd:PRK11288 168 TSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
424-659 |
4.59e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.12 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 424 LEnIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVErfYKPIEGKVYLDDVDISTLNV--RwLR 497
Cdd:COG0396 1 LE-IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakvLMGHPK--YEVTSGSILLDGEDILELSPdeR-AR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 QQIALVSQEPTLFA-CTIYDNIRHGLIGTKWESESEEQQRERIYEAARKAN-AHDFITSlpegyETNVGergflLSGGQK 575
Cdd:COG0396 77 AGIFLAFQYPVEIPgVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGlDEDFLDR-----YVNEG-----FSGGEK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 576 QRIAIARAIVSDPKILLLDEATSALD-----TKSEGVvqaaLEVAAEGRTTITIAH--RLSTIKDAHNIVVMAQGRIVEQ 648
Cdd:COG0396 147 KRNEILQMLLLEPKLAILDETDSGLDidalrIVAEGV----NKLRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKS 222
|
250
....*....|...
gi 164423939 649 GTH--AELLAKRG 659
Cdd:COG0396 223 GGKelALELEEEG 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1109-1333 |
5.09e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 90.84 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1109 QPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlNVNEYRSFIALVSQEPTLYQG-TVR 1187
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1188 ENIILGAnndvtdeQIKFACQEANIYDFIMSLPD-GMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDS 1266
Cdd:TIGR01257 1022 EHILFYA-------QLKGRSWEEAQLEMEAMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1267 ESEHVVQAALDKAAKGRTTIAVAHRLStiqKADI----IYVFDQGRIVEQGThsELMKKN----GRYAELV----NLQS 1333
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT--PLFLKNcfgtGFYLTLVrkmkNIQS 1168
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
807-1023 |
5.13e-18 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 86.21 E-value: 5.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 807 IKSDASFWCLMYLM--LALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFdrDENSAGALTSFLSTETTHV 884
Cdd:cd18784 29 EKSQDKFSRAIIIMglLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFF--DTVKTGDITSRLTSDTTTM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 885 AGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIPILLGCG-FYRFWmiahYQRRAKS---AYAGSASYASEAI 960
Cdd:cd18784 107 SDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSkVYGDY----YKKLSKAvqdSLAKANEVAEETI 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 961 TAMRTVASLTREQDVLQHYKDSLakQQHASLisVLKSSLLFA---ASNSLMFLA-FALGFWYGGTLI 1023
Cdd:cd18784 183 SSIRTVRSFANEDGEANRYSEKL--KDTYKL--KIKEALAYGgyvWSNELTELAlTVSTLYYGGHLV 245
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
144-395 |
6.63e-18 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 86.03 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 144 LVLYFVYLAIGEFVTMYIttvgFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLT 223
Cdd:cd18573 47 LLGVFVVGAAANFGRVYL----LRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 224 LQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRL 303
Cdd:cd18573 123 LRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 304 ARRYDAHLTRAEHFGFRLK-------GSIGVMV-AGMMTVLYLnyglafwqGSRFLLSGDtelrkiLTV--MMSVMIGAF 373
Cdd:cd18573 203 VERYAKKVDEVFDLAKKEAlasglffGSTGFSGnLSLLSVLYY--------GGSLVASGE------LTVgdLTSFLMYAV 268
|
250 260
....*....|....*....|....*.
gi 164423939 374 NLGNIAPNLQAFVT----ALGAAAKI 395
Cdd:cd18573 269 YVGSSVSGLSSFYSelmkGLGASSRL 294
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1107-1266 |
6.85e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.75 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1107 PEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFialvSQEPTLYQGTV 1186
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVF----QNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 RENIILGAN-NDVTDEQIKFACQEaniydfimslpdgMNTLVGSKGA------LLSGGQKQRIAIARALIRDPKILLLDE 1259
Cdd:PRK11248 88 QDNVAFGLQlAGVEKMQRLEIAHQ-------------MLKKVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLDE 154
|
....*..
gi 164423939 1260 ATSALDS 1266
Cdd:PRK11248 155 PFGALDA 161
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
813-1039 |
7.82e-18 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 85.60 E-value: 7.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 813 FWCLMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRDE---------NSAGALTSFLStetth 883
Cdd:cd18545 41 IIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPvgkilsrviNDVNSLSDLLS----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 884 vaglSGVTlgTIIMVLTTLIAACTVALALGWKLALVCIATIPILLgcGFYRFWmiahyQRRAKSAY-----AGSA--SYA 956
Cdd:cd18545 116 ----NGLI--NLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLV--LVVFLL-----RRRARKAWqrvrkKISNlnAYL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 957 SEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHEYDMFTfFIV 1036
Cdd:cd18545 183 HESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGV-LVA 261
|
...
gi 164423939 1037 FSS 1039
Cdd:cd18545 262 FIG 264
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
433-694 |
8.03e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 8.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 433 SRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTL-FA 511
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 512 CTIYDNIRHGLI-GTKWESESEEQQRERIYEAARKANAHDF----ITSlpegyetnvgergflLSGGQKQRIAIARAIVS 586
Cdd:PRK09536 92 FDVRQVVEMGRTpHRSRFDTWTETDRAAVERAMERTGVAQFadrpVTS---------------LSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 587 DPKILLLDEATSALDTKSE-GVVQAALEVAAEGRTTITIAHRLS-TIKDAHNIVVMAQGRIVEQGTHAELLAK---RGAY 661
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTAdtlRAAF 236
|
250 260 270
....*....|....*....|....*....|....*
gi 164423939 662 --YKLVTAQAIAAVNEMTAEEEAalDQQEEAALIR 694
Cdd:PRK09536 237 daRTAVGTDPATGAPTVTPLPDP--DRTEAAADTR 269
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
816-1053 |
8.33e-18 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 85.61 E-value: 8.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 816 LMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTI 895
Cdd:cd18575 40 LLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFET--TRTGEVLSRLTTDTTLIQTVVGSSLSIA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 896 IMVLTTLIAACTVALALGWKLALVCIATIPILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDV 975
Cdd:cd18575 118 LRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAE 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 976 LQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGtliakheydmftffivfSSVIFGAQSAGSVFSF 1053
Cdd:cd18575 198 RQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGA-----------------HDVLAGRMSAGELSQF 258
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
141-338 |
9.56e-18 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 85.18 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 141 LARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKV 220
Cdd:cd18551 35 SGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 221 GLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQ 300
Cdd:cd18551 115 PQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAE 194
|
170 180 190
....*....|....*....|....*....|....*...
gi 164423939 301 DRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYL 338
Cdd:cd18551 195 ERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQL 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
422-657 |
9.83e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.85 E-value: 9.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYpsRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIA 501
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEP--TLFACTIYDNIRHGLIGtkwESESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIA 579
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPIN---LGLDEETVAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 580 IARAIVSDPKILLLDEATSALDtkSEGVVQAALEVAA----EGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAEL 654
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLD--PQGVKELIDFLNDlpetYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
...
gi 164423939 655 LAK 657
Cdd:PRK13652 226 FLQ 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1109-1318 |
1.03e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.76 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1109 QPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSG-----GIFIDGREISSL-NVNEYRSFIALVSQEPTLY 1182
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1183 QGTVRENIILG--ANNDVTDEQIKFACQeANIYDfiMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEA 1260
Cdd:PRK14271 114 PMSIMDNVLAGvrAHKLVPRKEFRGVAQ-ARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1261 TSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
821-1065 |
1.09e-17 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 85.18 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 821 LALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTIIMVLT 900
Cdd:cd18551 45 LFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDR--RRSGDLVSRVTNDTTLLRELITSGLPQLVTGVL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 901 TLIAACTVALALGWKLALVCIATIPILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYK 980
Cdd:cd18551 123 TVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 981 DSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHEYDMFTF--FIVFSSVIFGAqsAGSVFSFAPDMG 1058
Cdd:cd18551 203 EAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLvaFLLYLFQLITP--LSQLSSFFTQLQ 280
|
....*..
gi 164423939 1059 KATEAAR 1065
Cdd:cd18551 281 KALGALE 287
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
405-1306 |
1.28e-17 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 89.40 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 405 IDSSSEEGGKLENVVGTIRLENIKHIYPSR--PDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVERFYKPIE 478
Cdd:TIGR00956 40 VAADSDYQPTFPNALLKILTRGFRKLKKFRdtKTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 479 GKVYLDDVDISTLnVRWLRQQIALVSQEPTLFA-CTIYDNIRHGlIGTKWESESEEQQRERIYeAARKANAHDFITSLPE 557
Cdd:TIGR00956 120 GVITYDGITPEEI-KKHYRGDVVYNAETDVHFPhLTVGETLDFA-ARCKTPQNRPDGVSREEY-AKHIADVYMATYGLSH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 558 GYETNVGE---RGflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSegvvqaALEVAAEGRTTITIAHRLSTI--- 631
Cdd:TIGR00956 197 TRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiy 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 632 ---KDAHN----IVVMAQGRIVEQG--THA-ELLAKRGayYKLVTAQAIAA-VNEMTAEEEAALDQQEEAALIRKAT--- 697
Cdd:TIGR00956 269 qcsQDAYElfdkVIVLYEGYQIYFGpaDKAkQYFEKMG--FKCPDRQTTADfLTSLTSPAERQIKPGYEKKVPRTPQefe 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 698 ---RNSQKEGGAAGYVEDPEDNIAEKLDRSKSQQSVSSVAIAARKKEEPKEYGLWTLIKLIAsfnKKEWHMMLVGIFFSA 774
Cdd:TIGR00956 347 tywRNSPEYAQLMKEIDEYLDRCSESDTKEAYRESHVAKQSKRTRPSSPYTVSFSMQVKYCL---ARNFLRMKGNPSFTL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 775 ICGAGNPTQAVffakLISSLSRPIVNEEIRASIKSDASFWCLMYLMLALVQCLAFSVQGW-LFAKCSERLIHRVRDMAFR 853
Cdd:TIGR00956 424 FMVFGNIIMAL----ILSSVFYNLPKNTSDFYSRGGALFFAILFNAFSSLLEIASMYEARpIVEKHRKYALYHPSADAIA 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 854 SFLrqdVEF-------------------FDRDensAGA-----LTSFLSTETthvagLSGVtLGTIIMVLTTLIAACTVA 909
Cdd:TIGR00956 500 SII---SEIpfkiiesvvfniilyfmvnFRRT---AGRfffylLILFICTLA-----MSHL-FRSIGAVTKTLSEAMTPA 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 910 LALGWKLALVCIATIPILLGCGFYRfWMiahyqrraksAYAGSASYASEAITAMRTVAsltREQDVLQHYK-----DSLA 984
Cdd:TIGR00956 568 AILLLALSIYTGFAIPRPSMLGWSK-WI----------YYVNPLAYAFESLMVNEFHG---RRFECSQYVPsgggyDNLG 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 985 KQQHASLISVLKSSLLFAASNSLMFLAFALGF---WYG-GTLIAkheydmFTFFIVFSSVIF-----GAQSAGSVFSF-- 1053
Cdd:TIGR00956 634 VTNKVCTVVGAEPGQDYVDGDDYLKLSFQYYNshkWRNfGIIIG------FTVFFFFVYILLtefnkGAKQKGEILVFrr 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1054 --APDMGKATEAARDLKELFDRK---PTVDTWSNEGDLIKQVD-------GTIEFRDVHFRYPTRPEQPV-LRGLNLSIQ 1120
Cdd:TIGR00956 708 gsLKRAKKAGETSASNKNDIEAGevlGSTDLTDESDDVNDEKDmekesgeDIFHWRNLTYEVKIKKEKRViLNNVDGWVK 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1121 PGQYVALVGASGCGKSTTI-ALLERfydpLSGGIFIDGREISS---LNVNEYRSfIALVSQEPT-LYQGTVRENIILGA- 1194
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLnVLAER----VTTGVITGGDRLVNgrpLDSSFQRS-IGYVQQQDLhLPTSTVRESLRFSAy 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1195 ---NNDVTDEqikfacqEANIY-DFIMSLPdGMNT----LVGSKGALLSGGQKQRIAIARALIRDPKILL-LDEATSALD 1265
Cdd:TIGR00956 863 lrqPKSVSKS-------EKMEYvEEVIKLL-EMESyadaVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
970 980 990 1000
....*....|....*....|....*....|....*....|..
gi 164423939 1266 SESEHVVQAALDKAAK-GRTTIAVAHRLStiqkADIIYVFDQ 1306
Cdd:TIGR00956 935 SQTAWSICKLMRKLADhGQAILCTIHQPS----AILFEEFDR 972
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1112-1317 |
1.29e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.39 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE---YRSFIALVSQEP-TLYQGTVR 1187
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1188 EN-----IILGANNDVTDEQIKFACQEANIYDFIMSLPdgmntlvgskgALLSGGQKQRIAIARALIRDPKILLLDEATS 1262
Cdd:PRK10908 98 DNvaiplIIAGASGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1263 ALDSE-SEHVVQAALDKAAKGRTTIAVAHRLSTIQKADI-IYVFDQGRIVEqGTHSE 1317
Cdd:PRK10908 167 NLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHLHG-GVGGE 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
422-664 |
1.35e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.36 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDI-----STLNVRwl 496
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkkSLLEVR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 497 rQQIALVSQEP--TLFACTIYDNIRHGLIGTKwesESEEQQRERIYEAARKANAhdfitslpEGYETNVGERgflLSGGQ 574
Cdd:PRK13639 78 -KTVGIVFQNPddQLFAPTVEEDVAFGPLNLG---LSKEEVEKRVKEALKAVGM--------EGFENKPPHH---LSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITIAHRLSTI-KDAHNIVVMAQGRIVEQGTHA 652
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPK 222
|
250
....*....|....*.
gi 164423939 653 ELLAK----RGAYYKL 664
Cdd:PRK13639 223 EVFSDietiRKANLRL 238
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1100-1313 |
1.44e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 83.35 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1100 HFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGReISSLnvneyrsfIAL-VSQE 1178
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSL--------LGLgGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1179 PTLyqgTVRENI-----ILGANNDVTDEQIKFacqeanIYDFiMSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPK 1253
Cdd:cd03220 97 PEL---TGRENIylngrLLGLSRKEIDEKIDE------IIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1254 ILLLDEATSALDSE-SEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:cd03220 163 ILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
422-653 |
1.56e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.00 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVvvMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVR---WLRQ 498
Cdd:PRK10908 2 IRFEHVSKAYLGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 499 QIALVSQEPTLFA-CTIYDNIRHGLIgtkWESESEEQQRERIYEAARKANAHDFITSLPegyetnvgergFLLSGGQKQR 577
Cdd:PRK10908 80 QIGMIFQDHHLLMdRTVYDNVAIPLI---IAGASGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 578 IAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAEGRTTITIAHRLSTI-KDAHNIVVMAQGRIVEqGTHAE 653
Cdd:PRK10908 146 VGIARAVVNKPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLIsRRSYRMLTLSDGHLHG-GVGGE 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
422-655 |
1.78e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.40 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIY-PSRPDVV-VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN----VRW 495
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 LRQQIALVSQEP--TLFACTIYDNIRHGligtkweseseEQQRERIYEAARKANAH--DFITSLPEGYEtnvgERGFLLS 571
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFG-----------PQNFGIPKEKAEKIAAEklEMVGLADEFWE----KSPFELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 572 GGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALE-VAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQG 649
Cdd:PRK13643 147 GGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFEsIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
....*.
gi 164423939 650 THAELL 655
Cdd:PRK13643 227 TPSDVF 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1111-1309 |
1.87e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 81.71 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE-YRSFIALVSQEPtLYQG----- 1184
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDR-KREGlvldl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 TVRENIILGAnndvtdeqikfacqeaniydfimslpdgmntlvgskgaLLSGGQKQRIAIARALIRDPKILLLDEATSAL 1264
Cdd:cd03215 94 SVAENIALSS--------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1265 DSES-EHVVQAALDKAAKGRTTIAVahrlST-----IQKADIIYVFDQGRI 1309
Cdd:cd03215 136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
440-649 |
2.39e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.78 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 440 MEDVSLVIPAGKTTALVGASGSGKSTIvglverfYKPIEGKVYLDDVDISTLNV---RWLRQQ-IALVSQEPTL---FAC 512
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTL-------FKALMGFVRLASGKISILGQptrQALQKNlVAYVPQSEEVdwsFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 513 TIYDNI---RHGLIGtkWESESEEQQRERIYEAARKANAHDFitslpegYETNVGErgflLSGGQKQRIAIARAIVSDPK 589
Cdd:PRK15056 96 LVEDVVmmgRYGHMG--WLRRAKKRDRQIVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 590 ILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQG 649
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLrELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1093-1311 |
2.56e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 86.95 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYPTRPEQpvLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFI 1172
Cdd:PRK10522 322 TLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1173 ALVSQEPTLYQGTvreniiLGANNDVTDEQIkfacqeanIYDFIMSLpdGMN---TLVGSKGAL--LSGGQKQRIAIARA 1247
Cdd:PRK10522 400 SAVFTDFHLFDQL------LGPEGKPANPAL--------VEKWLERL--KMAhklELEDGRISNlkLSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1248 LIRDPKILLLDEATSALDSESEHVVQAALDKA--AKGRTTIAVAHRLSTIQKADIIYVFDQGRIVE 1311
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYQVLLPLlqEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
138-503 |
3.05e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 86.78 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 138 TDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGIS 217
Cdd:COG4615 44 GAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 218 EKVGLtLQALATFIAAFV-IGFVSFwkltLILLSTVVALTLVMGGGSQFIIKFSKQ-NIAAYAEggsvaDEVISSVRnAI 295
Cdd:COG4615 124 RLPEL-LQSVALVLGCLAyLAWLSP----PLFLLTLVLLGLGVAGYRLLVRRARRHlRRAREAE-----DRLFKHFR-AL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 296 AFGT------QDR----LARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQGSRFLLSGDTELRKILTVM 365
Cdd:COG4615 193 LEGFkelklnRRRrrafFDEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFVLVL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 366 MsVMIGAfnLGNIAPNLQAFVTALGAAAKIyNTIDREspIDSSSEEGGKLENVV-----GTIRLENIKHIYPSRPDvvvm 440
Cdd:COG4615 273 L-FLRGP--LSQLVGALPTLSRANVALRKI-EELELA--LAAAEPAAADAAAPPapadfQTLELRGVTYRYPGEDG---- 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 441 eD-------VSLVIPAGKTTALVGASGSGKST----IVGLverfYKPIEGKVYLDDVDISTLNVRWLRQQIALV 503
Cdd:COG4615 343 -DegftlgpIDLTIRRGELVFIVGGNGSGKSTlaklLTGL----YRPESGEILLDGQPVTADNREAYRQLFSAV 411
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
433-645 |
3.39e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 80.94 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 433 SRPDVVvmEDVSLVIPAGKTTALVGASGSGKS----TIVGLverfYKPIEGKVYLDDVDISTLNVR-WLRQQIALVSQep 507
Cdd:cd03215 11 SVKGAV--RDVSFEVRAGEIVGIAGLVGNGQTelaeALFGL----RPPASGEITLDGKPVTRRSPRdAIRAGIAYVPE-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 508 tlfactiyDNIRHGLIGTkweseseeqqrERIYEaarkaNAhdfitSLPegyetnvgergFLLSGGQKQRIAIARAIVSD 587
Cdd:cd03215 83 --------DRKREGLVLD-----------LSVAE-----NI-----ALS-----------SLLSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 588 PKILLLDEATSALD--TKSEgVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRI 645
Cdd:cd03215 123 PRVLILDEPTRGVDvgAKAE-IYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
439-649 |
3.69e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 81.49 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWlrQQIALVSQEPTLF-ACTIYDN 517
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYpNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 518 IR-HGLIGTKweseseeqqreriyeaaRKANAHDFITSLPEGYETNVGERGFllSGGQKQRIAIARAIVSDPKILLLDEA 596
Cdd:cd03268 93 LRlLARLLGI-----------------RKKRIDEVLDVVGLKDSAKKKVKGF--SLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 597 TSALDTksEGVV---QAALEVAAEGRTTITIAHRLSTI-KDAHNIVVMAQGRIVEQG 649
Cdd:cd03268 154 TNGLDP--DGIKelrELILSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
135-311 |
4.29e-17 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 83.29 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 135 DDFTDELARLVLYFVYLAIGEFV--TMYITTVGFIYSgeHISGKIrehyLESCMRQNIGFFDKLGAGEVTTRITADTNLI 212
Cdd:cd18589 33 EAFTAAITVMSLLTIASAVSEFVcdLIYNITMSRIHS--RLQGLV----FAAVLRQEIAFFDSNQTGDIVSRVTTDTEDM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 213 QEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLIllsTVVALTLVMgggsqFIIKFS---KQNIA-----AYAEGGSVA 284
Cdd:cd18589 107 SESLSENLSLLMWYLARGLFLFIFMLWLSPKLALL---TALGLPLLL-----LVPKFVgkfQQSLAvqvqkSLARANQVA 178
|
170 180
....*....|....*....|....*..
gi 164423939 285 DEVISSVRNAIAFGTQDRLARRYDAHL 311
Cdd:cd18589 179 VETFSAMKTVRSFANEEGEAQRYRQRL 205
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
424-601 |
4.55e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.42 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 424 LENIKHIYPSRpdvVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLnvrwlRQQIALV 503
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 504 SQEPTLFAC-TIYDNIRHGLIGtKWeseseeqqreriyeaarKANAHDFITSLpeGYETNVGERGFLLSGGQKQRIAIAR 582
Cdd:PRK11247 87 FQDARLLPWkKVIDNVGLGLKG-QW-----------------RDAALQALAAV--GLADRANEWPAALSGGQKQRVALAR 146
|
170
....*....|....*....
gi 164423939 583 AIVSDPKILLLDEATSALD 601
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALD 165
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
419-656 |
4.95e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 419 VGTIRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVERfykpIEGKVYLDDVDISTLNVR 494
Cdd:PRK10895 1 MATLTAKNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 495 W-LRQQIALVSQEPTLFA-CTIYDNIRHGLigtkweseseeQQRERIYEAARKANAHDFITSLP-EGYETNVGERgflLS 571
Cdd:PRK10895 74 ArARRGIGYLPQEASIFRrLSVYDNLMAVL-----------QIRDDLSAEQREDRANELMEEFHiEHLRDSMGQS---LS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 572 GGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALE-VAAEGRTTITIAHRL-STIKDAHNIVVMAQGRIVEQG 649
Cdd:PRK10895 140 GGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEhLRDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHG 219
|
....*..
gi 164423939 650 THAELLA 656
Cdd:PRK10895 220 TPTEILQ 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1101-1319 |
5.65e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.53 E-value: 5.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1101 FRYPT----RPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNeYRS-FIALV 1175
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS-YRSqRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1176 SQEPTLYQGTvRENI--ILGA----NNDVTDEQikfacQEANIYDFIMS---LPDGMNTLvgskGALLSGGQKQRIAIAR 1246
Cdd:PRK15112 93 FQDPSTSLNP-RQRIsqILDFplrlNTDLEPEQ-----REKQIIETLRQvglLPDHASYY----PHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1247 ALIRDPKILLLDEATSALD-SESEHVVQAALDKAAK-GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELM 1319
Cdd:PRK15112 163 ALILRPKVIIADEALASLDmSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
439-676 |
7.08e-17 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 82.59 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKpIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIYDNI 518
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 519 R-HGligtKWESESeeqqrerIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEAT 597
Cdd:cd03289 98 DpYG----KWSDEE-------IWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 598 SALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYyklvtAQAIAAVNEM 676
Cdd:cd03289 167 AHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF-----KQAISPSDRL 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
438-649 |
8.23e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 8.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 438 VVMEDVSLVIPAGKTTALVGASGSGKSTiVGLVERFYKPIEGKVYLDDVDISTLNVRWL---RQQIALVSQEPT------ 508
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKST-TGLALLRLINSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNsslnpr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 509 LFACTIydnIRHGLigtkweseseEQQRERIYEAARKANAHDFITSL---PEGYETNVGErgflLSGGQKQRIAIARAIV 585
Cdd:PRK15134 379 LNVLQI---IEEGL----------RVHQPTLSAAQREQQVIAVMEEVgldPETRHRYPAE----FSGGQRQRIAIARALI 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 586 SDPKILLLDEATSALDTKSEGVVQAALEVAAEGR--TTITIAHRLSTIKD-AHNIVVMAQGRIVEQG 649
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1094-1311 |
1.07e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIfidgrEISSlNVNeyrsfIA 1173
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-----KLGE-TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQE-----PTLyqgTVRENIILGANNDvtdeqikfacQEANIYDFIMSL---PDGMNTLVGSkgalLSGGQKQRIAIA 1245
Cdd:COG0488 382 YFDQHqeeldPDK---TVLDELRDGAPGG----------TEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALA 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1246 RALIRDPKILLLDEATSALDSESEHVVQAALDkAAKGrTTIAVAH-R--LSTIqkADIIYVFDQGRIVE 1311
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
438-655 |
1.81e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.19 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 438 VVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPT--------- 508
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATtpgditvqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 509 LFACTIYDnirHGLIGTKWESESEeqqreriyEAARKANAHDFITSLP-EGYETnvgergflLSGGQKQRIAIARAIVSD 587
Cdd:PRK10253 101 LVARGRYP---HQPLFTRWRKEDE--------EAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 588 PKILLLDEATSALDTKSEgvvQAALEVAAE-----GRTTITIAHRLS-TIKDAHNIVVMAQGRIVEQGTHAELL 655
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQ---IDLLELLSElnrekGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1111-1318 |
2.21e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.44 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKST---TIALLERFYdplSGGIFIDGREISSLNVNEYRsfIALVSQEPTLYQG-TV 1186
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTllrIIAGLEHQT---SGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRHmTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 RENIILGANNDVTDEQIkfacQEANIYDFIMSLPD--GMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSAL 1264
Cdd:PRK10851 92 FDNIAFGLTVLPRRERP----NAAAIKAKVTQLLEmvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1265 DSESEHVVQAALDKAAK--GRTTIAVAH-RLSTIQKADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
427-649 |
2.37e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 79.11 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVErfYKPIEGKVYLDDVDISTLNV--RwLRQQI 500
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTlaktIMGHPK--YEVTEGEILFKGEDITDLPPeeR-ARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEPTLFActiydnirhgliGTKweseseeqqreriyeaarkaNAhDFITSLPEGyetnvgergflLSGGQKQRIAI 580
Cdd:cd03217 80 FLAFQYPPEIP------------GVK--------------------NA-DFLRYVNEG-----------FSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 581 ARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEGRTTITIAH--RLSTIKDAHNIVVMAQGRIVEQG 649
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDAlRLVAEVINKLREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1108-1319 |
2.79e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.16 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKSTTI-ALLERFY-DPLSGGIFIDGREISSLNVNEyrsfIALVSQEPTLY-QG 1184
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLnALAGRIQgNNFTGTILANNRKPTKQILKR----TGFVTQDDILYpHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 TVRENII----LGANNDVTdEQIKFACQEANIYDfiMSLPDGMNTLVGS---KGalLSGGQKQRIAIARALIRDPKILLL 1257
Cdd:PLN03211 156 TVRETLVfcslLRLPKSLT-KQEKILVAESVISE--LGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1258 DEATSALDSESEH-VVQAALDKAAKGRTTIAVAHRLST--IQKADIIYVFDQGRIVEQGTHSELM 1319
Cdd:PLN03211 231 DEPTSGLDATAAYrLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1108-1318 |
3.38e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.09 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERF---YDP---LSGGIFIDGREISSLNVNEYRSFIALVSQEPTL 1181
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1182 Y-QGTVRENII--LGANNDVTDEQIKFACQEA-NIYDFIMSLPDGMNtlvgSKGALLSGGQKQRIAIARALIRDPKILLL 1257
Cdd:PRK14246 102 FpHLSIYDNIAypLKSHGIKEKREIKKIVEEClRKVGLWKEVYDRLN----SPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1258 DEATSALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
146-327 |
4.11e-16 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 80.67 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 146 LYFVYLAIGEFVTMYITTVGFIysGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADtnlIQE-------GISE 218
Cdd:cd18574 48 LLGLYLLQSLLTFAYISLLSVV--GERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEfkssfkqCVSQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 219 KVGLTLQALATFIAAFVIGFvsfwKLTLILLstvVALTLVMGGGSQ---FIIKFSKQNIAAYAEGGSVADEVISSVRNAI 295
Cdd:cd18574 123 GLRSVTQTVGCVVSLYLISP----KLTLLLL---VIVPVVVLVGTLygsFLRKLSRRAQAQVAKATGVADEALGNIRTVR 195
|
170 180 190
....*....|....*....|....*....|..
gi 164423939 296 AFGTQDRLARRYDAHLTRAEHFGFRLKGSIGV 327
Cdd:cd18574 196 AFAMEDRELELYEEEVEKAAKLNEKLGLGIGI 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
439-656 |
4.68e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYkPIEGKVYLDDvDI-----STLNV--RWLRQ----QIALVSQEP 507
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSPPVVYPSG-DIrfhgeSLLHAseQTLRGvrgnKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 508 TlfactIYDNIRHGLigtkwesESEEQQRERIYEAARKANAHDFITSLPEgyetNVGERG---------FLLSGGQKQRI 578
Cdd:PRK15134 102 M-----VSLNPLHTL-------EKQLYEVLSLHRGMRREAARGEILNCLD----RVGIRQaakrltdypHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 579 AIARAIVSDPKILLLDEATSALDTKsegvVQAAL-----EVAAE-GRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTH 651
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVS----VQAQIlqllrELQQElNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRA 241
|
....*
gi 164423939 652 AELLA 656
Cdd:PRK15134 242 ATLFS 246
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1094-1322 |
4.69e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.52 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRY----PTrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGI---FID---------- 1156
Cdd:PRK13651 3 IKVKNIVKIFnkklPT--ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDeknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1157 -------------GREISslNVNEYRSFIALVSQ--EPTLYQGTVRENIILGANN-DVTDEQIKfacQEANIYDFIMSLP 1220
Cdd:PRK13651 81 ekvleklviqktrFKKIK--KIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSmGVSKEEAK---KRAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1221 DgmNTLVGSKGALlSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK-GRTTIAVAHRL-STIQKA 1298
Cdd:PRK13651 156 E--SYLQRSPFEL-SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLdNVLEWT 232
|
250 260
....*....|....*....|....
gi 164423939 1299 DIIYVFDQGRIVEQGTHSELMKKN 1322
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDTYDILSDN 256
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
424-601 |
4.71e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 424 LENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDvdistlNVRwlrqqIALV 503
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 504 SQEPTLFA-CTIYDNIRHGLIGT----KWESESEEQQRERIYEAARKANAHDFITSL-------------------PEGY 559
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELraleAELEELEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsglgfpEEDL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 164423939 560 ETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALD 601
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
436-694 |
4.87e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.54 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 DVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVErfykPIEGKVYLDDVDIStlnvRWLRQQIALVSQEPTLFA 511
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTtiriILGILA----PDSGEVLWDGEPLD----PEDRRRIGYLPEERGLYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 512 -CTIYDNIR-----HGLigTKweseseeqqreriYEAARKANA----HDfitsLPEGYETNVGErgflLSGGQKQRIAIA 581
Cdd:COG4152 85 kMKVGEQLVylarlKGL--SK-------------AEAKRRADEwlerLG----LGDRANKKVEE----LSKGNQQKVQLI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 582 RAIVSDPKILLLDEATSALD-TKSEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAELLAKRG 659
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDpVNVELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 164423939 660 A-YYKLVTAQAIAAVNEMTAEEEAalDQQEEAALIR 694
Cdd:COG4152 222 RnTLRLEADGDAGWLRALPGVTVV--EEDGDGAELK 255
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
441-654 |
5.71e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.91 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 441 EDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKV-YL--DDVDISTLNVRWLRQQIALVSQEPtlFAC- 512
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTfaraIIGLV----KATDGEVaWLgkDLLGMKDDEWRAVRSDIQMIFQDP--LASl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 513 ----TIYDNIrhgligtkweseseeqqreriyeaarkanAHDFITSLPEGYETNVGER--------GFL----------L 570
Cdd:PRK15079 112 nprmTIGEII-----------------------------AEPLRTYHPKLSRQEVKDRvkammlkvGLLpnlinrypheF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 571 SGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEG-VVQAALEVAAE-GRTTITIAHRLSTIKD-AHNIVVMAQGRIVE 647
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAqVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 242
|
....*..
gi 164423939 648 QGTHAEL 654
Cdd:PRK15079 243 LGTYDEV 249
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
424-654 |
6.22e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.42 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 424 LENIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWL---RQQI 500
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEPTLFA-CTIYDNIRHGLigtkweseseeqqreriyeaarkaNAHdfiTSLPEGYETN--------VGERGFL-- 569
Cdd:PRK11831 87 SMLFQSGALFTdMNVFDNVAYPL------------------------REH---TQLPAPLLHStvmmkleaVGLRGAAkl 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 ----LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGV-VQAALEV-AAEGRTTITIAHRLS---TIKDAHNIVvm 640
Cdd:PRK11831 140 mpseLSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVlVKLISELnSALGVTCVVVSHDVPevlSIADHAYIV-- 217
|
250
....*....|....
gi 164423939 641 AQGRIVEQGTHAEL 654
Cdd:PRK11831 218 ADKKIVAHGSAQAL 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1112-1310 |
6.42e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 82.57 E-value: 6.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFY--DPLSGGIFIDGREISSLNVNEY-RSFIALVSQEPTLYQG-TVR 1187
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1188 ENIILGanNDVT-------DEQIKFACQEANIYdfiMSLPDGMNTL-VGSKGallsGGQKQRIAIARALIRDPKILLLDE 1259
Cdd:TIGR02633 97 ENIFLG--NEITlpggrmaYNAMYLRAKNLLRE---LQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1260 ATSAL-DSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIV 1310
Cdd:TIGR02633 168 PSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-649 |
6.68e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.12 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYK-----PIEGKVYLDDVDISTLNVRWL--RQQIALVSQEPTLFA 511
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 512 -CTIYDNIRHGLIGTKwESESEEQQRERIYEAARKANAHDFITSLPEGYETNvgergflLSGGQKQRIAIARAIVSDPKI 590
Cdd:PRK14267 99 hLTIYDNVAIGVKLNG-LVKSKKELDERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 591 LLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAH---RLSTIKDAHNIVVMaqGRIVEQG 649
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaQAARVSDYVAFLYL--GKLIEVG 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
434-656 |
7.61e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.06 E-value: 7.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 434 RPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPtlfACT 513
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 514 IYDNIRHGLI-------GTKwesESEEQQRERIYEAARKanahdfITSLPEgyetNVGERGFLLSGGQKQRIAIARAIVS 586
Cdd:PRK15112 100 LNPRQRISQIldfplrlNTD---LEPEQREKQIIETLRQ------VGLLPD----HASYYPHMLAPGQKQRLGLARALIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 587 DPKILLLDEATSALD-TKSEGVVQAALEV-AAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAELLA 656
Cdd:PRK15112 167 RPKVIIADEALASLDmSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
422-654 |
7.84e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 78.18 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTlNVRWLRQQIA 501
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTL-FACTIYDN--IRHGLIGTKWESEseeqqreriyeAARKANAHDFItSLPEGYETNVGErgflLSGGQKQRI 578
Cdd:cd03265 77 IVFQDLSVdDELTGWENlyIHARLYGVPGAER-----------RERIDELLDFV-GLLEAADRLVKT----YSGGMRRRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 579 AIARAIVSDPKILLLDEATSALDTKSEGVVQAALE--VAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAEL 654
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEklKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
421-656 |
8.49e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.59 E-value: 8.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKhIYPSRPDVvvmEDVSLVIPAGKTTALVGASGSGKS-TIVGL-------VERfykpIEGKVYLDDVDISTLN 492
Cdd:PRK10418 4 QIELRNIA-LQAAQPLV---HGVSLTLQRGRVLALVGGSGSGKSlTCAAAlgilpagVRQ----TAGRVLLDGKPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 493 VRwlRQQIALVSQEP-TLF--ACTIYDNIRHGLIGTkwESESEEQQRERIYEAARKANAHDFITSLPegyetnvgergFL 569
Cdd:PRK10418 76 LR--GRKIATIMQNPrSAFnpLHTMHTHARETCLAL--GKPADDATLTAALEAVGLENAARVLKLYP-----------FE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALE--VAAEGRTTITIAHRLSTI-KDAHNIVVMAQGRIV 646
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLEsiVQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIV 220
|
250
....*....|
gi 164423939 647 EQGTHAELLA 656
Cdd:PRK10418 221 EQGDVETLFN 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1111-1319 |
9.28e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 9.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEY-RSFIALVSQEPTLYQG-TVRE 1188
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARaRRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1189 NI--ILGANNDVTDEQIKFACQEANIYDFIMSLPDGMntlvgskGALLSGGQKQRIAIARALIRDPKILLLDEATSALDS 1266
Cdd:PRK10895 98 NLmaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 1267 ES--------EHVVQAALDKAAKG---RTTIAVAHRlstiqkadiIYVFDQGRIVEQGTHSELM 1319
Cdd:PRK10895 171 ISvidikriiEHLRDSGLGVLITDhnvRETLAVCER---------AYIVSQGHLIAHGTPTEIL 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
416-654 |
1.69e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 416 ENVVGTIRLEnIKHIypSRPDVVvmEDVSLVIPAGKTTALVGASGSGKS----TIVGLverfYKPIEGKVYLDDVDISTL 491
Cdd:COG1129 249 AAAPGEVVLE-VEGL--SVGGVV--RDVSFSVRAGEILGIAGLVGAGRTelarALFGA----DPADSGEIRLDGKPVRIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 492 NVR-WLRQQIALVSQE-------PTLfacTIYDNI---------RHGLIGtkweseseeqqreriyEAARKANAHDFITS 554
Cdd:COG1129 320 SPRdAIRAGIAYVPEDrkgeglvLDL---SIRENItlasldrlsRGGLLD----------------RRRERALAEEYIKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 555 L---PEGYETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgvVQAAL-EVAAEGRTTI------ 622
Cdd:COG1129 381 LrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAE--IYRLIrELAAEGKAVIvissel 454
|
250 260 270
....*....|....*....|....*....|....*.
gi 164423939 623 ----TIAHRlstikdahnIVVMAQGRIVEQGTHAEL 654
Cdd:COG1129 455 pellGLSDR---------ILVMREGRIVGELDREEA 481
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
440-626 |
1.76e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 77.12 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 440 MEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDvdistlnvrwlrQQIA-------LVSQEPTLFA- 511
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG------------KQITepgpdrmVVFQNYSLLPw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 512 CTIYDNIrhgligtkweSESEEQQRERIYEAARKANAHDFI--TSLPEGYETNVGErgflLSGGQKQRIAIARAIVSDPK 589
Cdd:TIGR01184 69 LTVRENI----------ALAVDRVLPDLSKSERRAIVEEHIalVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPK 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 164423939 590 ILLLDEATSALDTKSEGVVQAAL-EVAAEGR-TTITIAH 626
Cdd:TIGR01184 135 VLLLDEPFGALDALTRGNLQEELmQIWEEHRvTVLMVTH 173
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
439-658 |
1.92e-15 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 78.36 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDvdistlnvrwlrqQIALVSQEPTLFACTIYDNI 518
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 519 RHGLIGTKWEseseeqqreriYEAARKA-NAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEAT 597
Cdd:cd03291 119 IFGVSYDEYR-----------YKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 598 SALDTKSEG-VVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKR 658
Cdd:cd03291 188 GYLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
436-657 |
1.98e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYL--DDVDISTLNVRWLRQQIALVSQEP--TLFA 511
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqgKPLDYSKRGLLALRQQVATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 512 CTIYDNIRHGL--IGTkweseseeqqreriyeaarkanAHDFITSLPEGYETNVGERGF------LLSGGQKQRIAIARA 583
Cdd:PRK13638 93 TDIDSDIAFSLrnLGV----------------------PEAEITRRVDEALTLVDAQHFrhqpiqCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 584 IVSDPKILLLDEATSALDTKSEGVVQAALE-VAAEGRTTITIAHRLSTIKDAHNIV-VMAQGRIVEQGTHAELLAK 657
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRrIVAQGNHVIISSHDIDLIYEISDAVyVLRQGQILTHGAPGEVFAC 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
146-667 |
2.17e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 81.88 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 146 LYFVYLAIGE-FVTM-YITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLT 223
Cdd:TIGR01271 927 IFYIYVGTADsVLALgFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDF 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 224 LQALATFIAAfvIGFVSFWKLTLILLSTVVALTLVMGggSQFIIKFSKQNIAAYAEGGS-VADEVISSVR---NAIAFGT 299
Cdd:TIGR01271 1007 IQLTLIVLGA--IFVVSVLQPYIFIAAIPVAVIFIML--RAYFLRTSQQLKQLESEARSpIFSHLITSLKglwTIRAFGR 1082
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 300 QDRLARRYDAHLTRAEHFGFRLKGSIG--VMVAGMMTVLylnyglaFWQGSRFLL-----SGDTELRKILTVMMSVMiGA 372
Cdd:TIGR01271 1083 QSYFETLFHKALNLHTANWFLYLSTLRwfQMRIDIIFVF-------FFIAVTFIAigtnqDGEGEVGIILTLAMNIL-ST 1154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 373 FNLgniAPNLQAFVTAL-GAAAKIYNTIDReSPIDSSSEEGGKLENVVGTIRLEN--IKHIYPSRPDVVV---------- 439
Cdd:TIGR01271 1155 LQW---AVNSSIDVDGLmRSVSRVFKFIDL-PQEEPRPSGGGGKYQLSTVLVIENphAQKCWPSGGQMDVqgltakytea 1230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 440 ----MEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKpIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFACTIY 515
Cdd:TIGR01271 1231 gravLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFR 1309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 516 DNIRHGligTKWESESeeqqrerIYEAARKANAHDFITSLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDE 595
Cdd:TIGR01271 1310 KNLDPY---EQWSDEE-------IWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 596 ATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELLAKRGAYYKLVTA 667
Cdd:TIGR01271 1380 PSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSA 1451
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
421-657 |
2.34e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.12 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIYPSrpDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLvERfykpI-EGKVYLDDVDISTLNVRw 495
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTllrmVAGL-ER----ItSGEIWIGGRVVNELEPA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 lRQQIALVSQEPTLFA-CTIYDNIRHGLigtKWESESEEQQRERIYEAARkanahdfITSLPEgyetnvgergFL----- 569
Cdd:PRK11650 75 -DRDIAMVFQNYALYPhMSVRENMAYGL---KIRGMPKAEIEERVAEAAR-------ILELEP----------LLdrkpr 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 -LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEgvVQAALEVAAEGR---TT-----------ITIAHRLstikda 634
Cdd:PRK11650 134 eLSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR--VQMRLEIQRLHRrlkTTslyvthdqveaMTLADRV------ 205
|
250 260
....*....|....*....|....
gi 164423939 635 hniVVMAQGRIvEQ-GTHAELLAK 657
Cdd:PRK11650 206 ---VVMNGGVA-EQiGTPVEVYEK 225
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
141-395 |
4.79e-15 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 77.46 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 141 LARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKV 220
Cdd:cd18552 38 LLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 221 GLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQ 300
Cdd:cd18552 118 TVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 301 DRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQGSRFLLSGDT---ELRKILTVMMSVMIGAFNLGN 377
Cdd:cd18552 198 DYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELtpgEFISFITALLLLYQPIKRLSN 277
|
250
....*....|....*...
gi 164423939 378 IAPNLQafvTALGAAAKI 395
Cdd:cd18552 278 VNANLQ---RGLAAAERI 292
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
442-649 |
4.94e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.38 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDD---VDI-STLNVRWLRQQIALVSQEPTLFA-CTIYD 516
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAeKGICLPPEKRRIGYVFQDARLFPhYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 517 NIRHGLigtkweseseeqqreriyeaARKANAH-DFITSLPeGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDE 595
Cdd:PRK11144 96 NLRYGM--------------------AKSMVAQfDKIVALL-GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 596 ATSALDT--KSEgvVQAALE-VAAEGRTTIT-IAHRLSTI-KDAHNIVVMAQGRIVEQG 649
Cdd:PRK11144 155 PLASLDLprKRE--LLPYLErLAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
434-649 |
6.56e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 75.39 E-value: 6.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 434 RPDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVERFYKpIEGKVYLDDVDIS----TLNVRWLRQQIALVSQ 505
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPRKpdqfQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 506 ---EPTLFACTIYDNIRHgligTKWESESEEQQRERIYEAARKANAHDFITSLpegyetnvgergfllSGGQKQRIAIAR 582
Cdd:cd03234 96 ltvRETLTYTAILRLPRK----SSDAIRKKRVEDVLLRDLALTRIGGNLVKGI---------------SGGERRRVSIAV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 583 AIVSDPKILLLDEATSALDTKSE-GVVQAALEVAAEGRTTITIAH--RLSTIKDAHNIVVMAQGRIVEQG 649
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
422-647 |
6.83e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.28 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVrwlrqQIA 501
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-----ERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQEPTLFAC-TIYDNIRHGLigtkweseseeqQRERIYEAARKANAHDFITSLP-EGYETnvgERGFLLSGGQKQRIA 579
Cdd:PRK11248 74 VVFQNEGLLPWrNVQDNVAFGL------------QLAGVEKMQRLEIAHQMLKKVGlEGAEK---RYIWQLSGGQRQRVG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 580 IARAIVSDPKILLLDEATSALDTKSEGVVQA-ALEVAAE-GRTTITIAHrlstikDAHNIVVMAQ---------GRIVE 647
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALDAFTREQMQTlLLKLWQEtGKQVLLITH------DIEEAVFMATelvllspgpGRVVE 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
570-639 |
7.89e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 73.73 E-value: 7.89e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEvaAEGRTTITIAHRlSTIKDAHNIVV 639
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK--ELGITVISVGHR-PSLWKFHDRVL 158
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
766-1039 |
8.54e-15 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 76.70 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 766 MLVGIFFSAIcgagnptqAVFFAKLISSLSRPIVNEEIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKCSERLIH 845
Cdd:cd18542 1 YLLAILALLL--------ATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 846 RVRDMAFRSFLRQDVEFFDRdeNSAGAL----TS-------FLSTETTHVaglsgvtLGTIIMVLTTLIaactVALALGW 914
Cdd:cd18542 73 DLRNDLYDHLQRLSFSFHDK--ARTGDLmsrcTSdvdtirrFLAFGLVEL-------VRAVLLFIGALI----IMFSINW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 915 KLALVCIATIPILlgcgfyrFWMIAHYQRRAKSAYAGS-------ASYASEAITAMRTVASLTRE----QDVLQHYKDSL 983
Cdd:cd18542 140 KLTLISLAIIPFI-------ALFSYVFFKKVRPAFEEIreqegelNTVLQENLTGVRVVKAFAREdyeiEKFDKENEEYR 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 984 AKQQHASLIsvlkSSLLFAASNSLMFLAFALGFWYGGTLIAKHEydmFTF--FIVFSS 1039
Cdd:cd18542 213 DLNIKLAKL----LAKYWPLMDFLSGLQIVLVLWVGGYLVINGE---ITLgeLVAFIS 263
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
760-1023 |
9.03e-15 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 76.36 E-value: 9.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 760 KKEWHMMLVGIFFSAICGAGNPTqavffaklissLSRPIVNEEIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKC 839
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPL-----------LTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 840 SERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLsgVTLGTIIMV--LTTLIAACTVALALGWKLA 917
Cdd:cd18540 70 EMGVSYDLRKKAFEHLQTLSFSYFDK--TPVGWIMARVTSDTQRLGEI--ISWGLVDLVwgITYMIGILIVMLILNWKLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 918 LVCIATIPILLGCGFYRFWMIAHYQRRAK---SAYagSASYaSEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISV 994
Cdd:cd18540 146 LIVLAVVPVLAVVSIYFQKKILKAYRKVRkinSRI--TGAF-NEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAA 222
|
250 260
....*....|....*....|....*....
gi 164423939 995 LKSSLLFAASNSLMFLAFALGFWYGGTLI 1023
Cdd:cd18540 223 RLSALFLPIVLFLGSIATALVLWYGGILV 251
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1111-1265 |
9.46e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.24 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVneyrsfialvsqeptlyqgtvreni 1190
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSS------------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1191 ilGANNDVTDEQIKFacqeanIYDFIMSLPD-------GMNTLVGSKG-------------------------ALLSGGQ 1238
Cdd:PRK11629 79 --AAKAELRNQKLGF------IYQFHHLLPDftalenvAMPLLIGKKKpaeinsralemlaavglehranhrpSELSGGE 150
|
170 180
....*....|....*....|....*..
gi 164423939 1239 KQRIAIARALIRDPKILLLDEATSALD 1265
Cdd:PRK11629 151 RQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
815-1027 |
1.13e-14 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 76.37 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 815 CLMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAG-----------ALTSFLSTetth 883
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHER--ETSGrimtrmtsdidALSELLQT---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 884 vaGLSG--VTLGTIIMVLTTLiaactvaLALGWKLALVCIATIPILlgcgfyrFWMIAHYQRRAKSAY-------AGSAS 954
Cdd:cd18546 116 --GLVQlvVSLLTLVGIAVVL-------LVLDPRLALVALAALPPL-------ALATRWFRRRSSRAYrrareriAAVNA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 955 YASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHE 1027
Cdd:cd18546 180 DLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGT 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
436-649 |
1.15e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN---VRWLRQQIALVSQEP----- 507
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPyasld 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 508 --TLFACTIYDNIR-HGLIGTKweseseeqqreriYEAARKANAHDFITSLPEGYETNVGErgflLSGGQKQRIAIARAI 584
Cdd:PRK10261 416 prQTVGDSIMEPLRvHGLLPGK-------------AAAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARAL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 585 VSDPKILLLDEATSALDTKSEG-VVQAALEVAAE-GRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQG 649
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGqIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
427-654 |
1.30e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.38 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLD-----DVDISTLNVRWLRQQIA 501
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGekrmnDVPPAERGVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVsqePTLfacTIYDNIRHGLigtKWESESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIAIA 581
Cdd:PRK11000 86 LY---PHL---SVAENMSFGL---KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 582 RAIVSDPKILLLDEATSALDtksegvvqAALEVAAE----------GRTTITIAH-RLSTIKDAHNIVVMAQGRIVEQGT 650
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLD--------AALRVQMRieisrlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK 217
|
....
gi 164423939 651 HAEL 654
Cdd:PRK11000 218 PLEL 221
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
794-1023 |
1.34e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 76.01 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 794 LSRPIVNEEIRASIKsDASFWCLMYLMLALV-----QCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeN 868
Cdd:cd18563 21 LTKILIDDVLIQLGP-GGNTSLLLLLVLGLAgayvlSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDK--R 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 869 SAGALTSFLSTETTHVAG-LSGVTLGTIIMVLTtLIAACTVALALGWKLALVCIATIPILLgCGFYRFW--MIAHYQRRA 945
Cdd:cd18563 98 QTGSLMSRVTSDTDRLQDfLSDGLPDFLTNILM-IIGIGVVLFSLNWKLALLVLIPVPLVV-WGSYFFWkkIRRLFHRQW 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 946 KSAyAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLI 1023
Cdd:cd18563 176 RRW-SRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQV 252
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
815-1027 |
1.38e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 76.01 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 815 CLMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLsteTTHVAGLSGVTLGT 894
Cdd:cd18564 57 AAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDR--RRTGDLLSRL---TGDVGAIQDLLVSG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 895 IIMVLT---TLIAACTVALALGWKLALVCIATIPILlgcgfyrFWMIAHYQRRAKSA------YAGS-ASYASEAITAMR 964
Cdd:cd18564 132 VLPLLTnllTLVGMLGVMFWLDWQLALIALAVAPLL-------LLAARRFSRRIKEAsreqrrREGAlASVAQESLSAIR 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 965 TVASLTREqdvlQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALG----FWYGGTLIAKHE 1027
Cdd:cd18564 205 VVQAFGRE----EHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGtalvLWFGAWLVLAGR 267
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1108-1321 |
1.69e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 74.83 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALL--ERFYDPLSGGIFIDGREISSLNVNEYRS---FIALvsQEPTLY 1182
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGegiFMAF--QYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1183 QGTVRENIILGANNDVTDEQIKFACQEANIYDFI------MSLPDgmNTLVGSKGALLSGGQKQRIAIARALIRDPKILL 1256
Cdd:PRK09580 91 PGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMeekialLKMPE--DLLTRSVNVGFSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1257 LDEATSALDSESEHVVQAALDKAAKG-RTTIAVAH--RLSTIQKADIIYVFDQGRIVEQGTHSeLMKK 1321
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFT-LVKQ 235
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1106-1320 |
1.92e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.25 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1106 RPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTI-ALLERFYDP-------LSGGIFIDGREISSLNVNEYRSFIALVSQ 1177
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1178 --EPTlYQGTVRENIILG-------------ANNDVTDEQIKFAcqeaniydfimslpdGMNTLVGSKGALLSGGQKQRI 1242
Cdd:PRK13547 91 aaQPA-FAFSAREIVLLGrypharragalthRDGEIAWQALALA---------------GATALVGRDVTTLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1243 AIARAL---------IRDPKILLLDEATSALDSESEHVVQAALDKAAK----GRTTIAVAHRLSTiQKADIIYVFDQGRI 1309
Cdd:PRK13547 155 QFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwnlGVLAIVHDPNLAA-RHADRIAMLADGAI 233
|
250
....*....|.
gi 164423939 1310 VEQGTHSELMK 1320
Cdd:PRK13547 234 VAHGAPADVLT 244
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1115-1323 |
2.18e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.58 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1115 LNLSIQPGQYVALVGASGCGKSTTIA----LLerfydPLSGGIFIDGREISSLNVNE---YRS---------FIALVSQE 1178
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAElarHRAylsqqqtppFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1179 PTLYQGTvreniilGANNDVTDEQIKFACQEANIYDFimsLPDGMNTlvgskgalLSGGQKQRIAIARALIR-------D 1251
Cdd:PRK03695 90 LTLHQPD-------KTRTEAVASALNEVAEALGLDDK---LGRSVNQ--------LSGGEWQRVRLAAVVLQvwpdinpA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1252 PKILLLDEATSALDsesehVVQ-AALDK-----AAKGRTTIAVAHRLS-TIQKADIIYVFDQGRIVEQGTHSELMKKNG 1323
Cdd:PRK03695 152 GQLLLLDEPMNSLD-----VAQqAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1112-1318 |
2.43e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.52 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVN-EYRSFIALVSQEPTLY-QGTVREN 1189
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIdELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1190 IILG-------ANNDVTDeqIKFACQEANIYDFIMSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKILLLDEATS 1262
Cdd:PRK09700 101 LYIGrhltkkvCGVNIID--WREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1263 AL-DSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK09700 175 SLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
436-644 |
2.52e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTlNVRWLRQQIALVSQEPTL-FACTI 514
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLdLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 515 YDNIrhgLIGTKWESEseeqqreriyeAARKANAhdFITSLPE--GYETNVGERGFLLSGGQKQRIAIARAIVSDPKILL 592
Cdd:PRK13536 132 RENL---LVFGRYFGM-----------STREIEA--VIPSLLEfaRLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 593 LDEATSALDTKSEGVVQAALE-VAAEGRTTITIAH----------RLSTIKDAHNIvvmAQGR 644
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRsLLARGKTILLTTHfmeeaerlcdRLCVLEAGRKI---AEGR 255
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
420-649 |
2.61e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 73.72 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 420 GTIRLENIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVylddvdISTLNVRWLrqq 499
Cdd:cd03220 18 SSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV------TVRGRVSSL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IAL-VSQEPTLfacTIYDNIR-----HGLIGTkweseseeqqreriYEAARKANAHDFiTSLPEGYETNVGErgflLSGG 573
Cdd:cd03220 89 LGLgGGFNPEL---TGRENIYlngrlLGLSRK--------------EIDEKIDEIIEF-SELGDFIDLPVKT----YSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 574 QKQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQG 649
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
139-341 |
2.71e-14 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 139 DELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISE 218
Cdd:cd18784 33 DKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 219 KVGLTLQALATFIAAFVIGFVSFWKLTLIllsTVVALTLVMGGGS---QFIIKFSKQNIAAYAEGGSVADEVISSVRNAI 295
Cdd:cd18784 113 NLNIFLRSLVKAIGVIVFMFKLSWQLSLV---TLIGLPLIAIVSKvygDYYKKLSKAVQDSLAKANEVAEETISSIRTVR 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 296 AFGTQDRLARRYDAHLTRAehfgFRLKGSIGVMVAG----------MMTVLYLNYG 341
Cdd:cd18784 190 SFANEDGEANRYSEKLKDT----YKLKIKEALAYGGyvwsneltelALTVSTLYYG 241
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
443-654 |
2.74e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.55 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 443 VSLVIPAGKTTALVGASGSGKS----TIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQ----QIALVSQEP--TLFAC 512
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPmtSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 513 -----TIYDNIRHGLIGTKweseseeqqreriyeAARKANAHDFIT--SLPEGyETNVGERGFLLSGGQKQRIAIARAIV 585
Cdd:PRK11022 106 ytvgfQIMEAIKVHQGGNK---------------KTRRQRAIDLLNqvGIPDP-ASRLDVYPHQLSGGMSQRVMIAMAIA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 586 SDPKILLLDEATSALD-TKSEGVVQAALEVA-AEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAEL 654
Cdd:PRK11022 170 CRPKLLIADEPTTALDvTIQAQIIELLLELQqKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
439-650 |
3.14e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 73.70 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRW---LR-QQIALVSQEPTLFA-CT 513
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKLGFIYQFHHLLPdFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 514 IYDNIRHGL-IGTKWESeseeqqreriyEAARKAnaHDFITSLpeGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILL 592
Cdd:PRK11629 104 ALENVAMPLlIGKKKPA-----------EINSRA--LEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 593 LDEATSALDTK-SEGVVQAALEV-AAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGT 650
Cdd:PRK11629 169 ADEPTGNLDARnADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
434-655 |
3.43e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 434 RPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVErFYKP----IEGKVYLDDVDIstlNVRWLRQQIALVSQE--- 506
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDdlf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 -PTLfacTIYDNIrhgligtkwESESEEQQRERIYEAARKANAHDFIT--SLPEGYETNVGERGFL--LSGGQKQRIAIA 581
Cdd:TIGR00955 111 iPTL---TVREHL---------MFQAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 582 RAIVSDPKILLLDEATSALDTKSEG-VVQAALEVAAEGRTTITIAHRLST--IKDAHNIVVMAQGRIVEQGTHAELL 655
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYsVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1111-1319 |
3.65e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE-YRSFIALVSQEPTLY-QGTVRE 1188
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFsRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1189 NIILG---ANNDVTDEQIKfacqeaNIYDFIMSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKILLLDEATSALd 1265
Cdd:PRK11614 100 NLAMGgffAERDQFQERIK------WVYELFPRLHERRIQRAGT----MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1266 seSEHVVQAALDKAAK----GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELM 1319
Cdd:PRK11614 169 --APIIIQQIFDTIEQlreqGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALL 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1094-1324 |
3.80e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 72.28 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPT-RPEQPVLRGLNLSIQPGQYVALVGASGCGKSTtiaLLerfyDPLS---------GGIFIDGREISSl 1163
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LL----DVLAgrktagvitGEILINGRPLDK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1164 nvnEYRSFIALVSQEPTLYQG-TVRENIILGANndvtdeqikfacqeaniydfimslpdgmntLVGskgalLSGGQKQRI 1242
Cdd:cd03232 76 ---NFQRSTGYVEQQDVHSPNlTVREALRFSAL------------------------------LRG-----LSVEQRKRL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1243 AIARALIRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLStiqkADIIYVFDqgRIVeqgthseLMKK 1321
Cdd:cd03232 118 TIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPS----ASIFEKFD--RLL-------LLKR 184
|
...
gi 164423939 1322 NGR 1324
Cdd:cd03232 185 GGK 187
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1107-1313 |
5.05e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.58 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1107 PEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDP----LSGGIFIDGREISSlnvNEYRS-FIALVSQEP-- 1179
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAP---CALRGrKIATIMQNPrs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1180 ------TLyQGTVRENiiLGANNDVTDEQIKFACQEAniydfiMSLPDgMNTLVGSKGALLSGGQKQRIAIARALIRDPK 1253
Cdd:PRK10418 91 afnplhTM-HTHARET--CLALGKPADDATLTAALEA------VGLEN-AARVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1254 ILLLDEATSALDSesehVVQA-ALD-----KAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQG 1313
Cdd:PRK10418 161 FIIADEPTTDLDV----VAQArILDllesiVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1108-1321 |
6.67e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.14 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERF--YDPLSGGIFIDGREISSLNVNEyRSF--IALVSQEPTLYQ 1183
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEE-RAHlgIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1184 GTVRENIILGANNDVTDEQIKFACQEANIYDFIMSLPDgmntLVGSKGALL--------SGGQKQRIAIARALIRDPKIL 1255
Cdd:CHL00131 98 GVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLK----LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1256 LLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAH--RLSTIQKADIIYVFDQGRIVEQGThSELMKK 1321
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD-AELAKE 241
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
423-649 |
9.43e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 72.65 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 423 RLENIKHIYPSRpdvVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNV--------R 494
Cdd:PRK11701 8 SVRGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 495 WL-RQQIALVSQEPT---LFACTIYDNIRHGLIGTKWESeseeqqreriYEAARKANAH---------DFITSLPegyet 561
Cdd:PRK11701 85 RLlRTEWGFVHQHPRdglRMQVSAGGNIGERLMAVGARH----------YGDIRATAGDwlerveidaARIDDLP----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 562 nvgeRGFllSGGQKQRIAIARAIVSDPKILLLDEATSALDTKsegvVQAAL------EVAAEGRTTITIAHRLSTIK-DA 634
Cdd:PRK11701 150 ----TTF--SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQARLldllrgLVRELGLAVVIVTHDLAVARlLA 219
|
250
....*....|....*
gi 164423939 635 HNIVVMAQGRIVEQG 649
Cdd:PRK11701 220 HRLLVMKQGRVVESG 234
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1111-1268 |
9.75e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.12 E-value: 9.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNvNEYRS-----FIALVSQE----PTL 1181
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD-EEARAklrakHVGFVFQSfmliPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1182 yqgTVRENIIL-----GANNDVTDEQIKFACQEANIYDFIMSLPdgmntlvgskgALLSGGQKQRIAIARALIRDPKILL 1256
Cdd:PRK10584 104 ---NALENVELpallrGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLF 169
|
170
....*....|..
gi 164423939 1257 LDEATSALDSES 1268
Cdd:PRK10584 170 ADEPTGNLDRQT 181
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1106-1290 |
1.01e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 71.24 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1106 RPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNvNEYRSFIALVSQEPTLYQG- 1184
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHLPGLKPEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 TVRENI-ILGANNDVTDEQIKFACQEANIYDFimslpdgMNTLVGSkgalLSGGQKQRIAIARALIRDPKILLLDEATSA 1263
Cdd:TIGR01189 89 SALENLhFWAAIHGGAQRTIEDALAAVGLTGF-------EDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*...
gi 164423939 1264 LDSESEHVVQAALDK-AAKGRTTIAVAH 1290
Cdd:TIGR01189 158 LDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1088-1318 |
1.02e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.88 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1088 KQVDGTIEFRDVHFrypTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLN--- 1164
Cdd:PRK11831 2 QSVANLVDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1165 VNEYRSFIALVSQEPTLYQG-TVRENII--LGANNDVTDEQIKFACqeaniydfIMSLpdgmnTLVGSKGAL------LS 1235
Cdd:PRK11831 79 LYTVRKRMSMLFQSGALFTDmNVFDNVAypLREHTQLPAPLLHSTV--------MMKL-----EAVGLRGAAklmpseLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1236 GGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDK--AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQ 1312
Cdd:PRK11831 146 GGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAH 225
|
....*.
gi 164423939 1313 GTHSEL 1318
Cdd:PRK11831 226 GSAQAL 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1094-1308 |
1.04e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.78 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPtrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTtiallerfydplsggifidgreisslnvneyrsFIA 1173
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKST---------------------------------LLK 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1174 LVSQEPTLYQGTVReniilganndvTDEQIKFAC--QeaniydfimslpdgmntlvgskgalLSGGQKQRIAIARALIRD 1251
Cdd:cd03221 45 LIAGELEPDEGIVT-----------WGSTVKIGYfeQ-------------------------LSGGEKMRLALAKLLLEN 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1252 PKILLLDEATSALDSESEHVVQAALdKAAKGrTTIAVAHRLSTIQK-ADIIYVFDQGR 1308
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1092-1318 |
1.19e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.12 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1092 GTIEFRDVHFRYPTRP--EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISS-----LN 1164
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1165 VNEYRSFIALVSQEP--TLYQGTVRENIILGANNDVTDEQIKFAcQEANIYDFImSLPDgmnTLVGSKGALLSGGQKQRI 1242
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYK-KVPELLKLV-QLPE---DYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1243 AIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1112-1328 |
1.20e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.74 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFY--DPLSGG-IFIDGREIS-----SLNVNEYRSFIALVSQEPTLYQ 1183
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQregrlARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1184 G-TVRENIILGANNDV----------TDEQIKFACQEANIYdfimslpdGMNTLVGSKGALLSGGQKQRIAIARALIRDP 1252
Cdd:PRK09984 100 RlSVLENVLIGALGSTpfwrtcfswfTREQKQRALQALTRV--------GMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1253 KILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLS-TIQKADIIYVFDQGRIVEQGTHSELmkKNGRYAEL 1328
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF--DNERFDHL 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1097-1318 |
1.24e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.05 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1097 RDVHFRYPTRPEQP--------------VLRGLNLSIQPGQYVALVGASGCGKSTTIALLerF-YDPLSGG-IFIDGREI 1160
Cdd:COG1129 239 RELEDLFPKRAAAPgevvleveglsvggVVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgADPADSGeIRLDGKPV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1161 SSLNVNE-YRSFIALVSQE-------PTLyqgTVRENIILGANNDVTDEQ-IKFACQEANIYDFIMSL---PDGMNTLVG 1228
Cdd:COG1129 317 RIRSPRDaIRAGIAYVPEDrkgeglvLDL---SIRENITLASLDRLSRGGlLDRRRERALAEEYIKRLrikTPSPEQPVG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1229 SkgalLSGGQKQRIAIARALIRDPKILLLDEATSALD--SESEhvVQAALDK-AAKGRTTI----------AVAHRlsti 1295
Cdd:COG1129 394 N----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAE--IYRLIRElAAEGKAVIvisselpellGLSDR---- 463
|
250 260
....*....|....*....|...
gi 164423939 1296 qkadiIYVFDQGRIVEQGTHSEL 1318
Cdd:COG1129 464 -----ILVMREGRIVGELDREEA 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1093-1313 |
1.25e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 71.14 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYP-TRPEQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERFYDPLSGGIFIDGREISSlNVNEY 1168
Cdd:cd03233 3 TLSWRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKE-FAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1169 RSFIALVSQE----PTLyqgTVRENIilganndvtdeqiKFACQeANIYDFImslpdgmntlvgsKGalLSGGQKQRIAI 1244
Cdd:cd03233 82 PGEIIYVSEEdvhfPTL---TVRETL-------------DFALR-CKGNEFV-------------RG--ISGGERKRVSI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1245 ARALIRDPKILLLDEATSALDSESehvvqaALDKAAKGRtTIAVAHRLSTI----QKADIIY-VFDQ------GRIVEQG 1313
Cdd:cd03233 130 AEALVSRASVLCWDNSTRGLDSST------ALEILKCIR-TMADVLKTTTFvslyQASDEIYdLFDKvlvlyeGRQIYYG 202
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
843-1064 |
1.44e-13 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 72.89 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 843 LIH-RVRDMAFRSFLRQDVEFFdrDENSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCI 921
Cdd:cd18589 66 RIHsRLQGLVFAAVLRQEIAFF--DSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 922 ATIPILlgcgfyrfWMIA----HYQR----RAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASlis 993
Cdd:cd18589 144 LGLPLL--------LLVPkfvgKFQQslavQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLN--- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 994 vLKSSLLFAAS---NSLMFLAFALG-FWYGGTLIAKHEY---DMFTFF---IVFSSVIfgaqsaGSVFSFAPDMGKATEA 1063
Cdd:cd18589 213 -KKEAAAYAVSmwtSSFSGLALKVGiLYYGGQLVTAGTVssgDLVTFVlyeLQFTSAV------EVLLSYYPSVMKAVGS 285
|
.
gi 164423939 1064 A 1064
Cdd:cd18589 286 S 286
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
422-657 |
2.41e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.45 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERF--YKPIEGKV-----------YLD---- 484
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVErpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 485 ---------------DVDISTLN---VRWLRQQIALVSQEPtlFAC----TIYDNIRHGL--IGtkweseseeqqreriY 540
Cdd:TIGR03269 78 vgepcpvcggtlepeEVDFWNLSdklRRRIRKRIAIMLQRT--FALygddTVLDNVLEALeeIG---------------Y 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 541 EAARKAN-AHDFITslpegyETNVGER----GFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALE-- 613
Cdd:TIGR03269 141 EGKEAVGrAVDLIE------MVQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEea 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 164423939 614 VAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAELLAK 657
Cdd:TIGR03269 215 VKASGISMVLTSHWPEVIEDlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1105-1290 |
2.61e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.29 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1105 TRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFI----ALvsqEPT 1180
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLghrnAM---KPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1181 LyqgTVRENI-----ILGANNDVTDEQIKFacqeaniydfiMSLPDgmntLVGSKGALLSGGQKQRIAIARALIRDPKIL 1255
Cdd:PRK13539 88 L---TVAENLefwaaFLGGEELDIAAALEA-----------VGLAP----LAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 164423939 1256 LLDEATSALDSESEHVVQAAL-DKAAKGRTTIAVAH 1290
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIrAHLAQGGIVIAATH 185
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
437-657 |
2.70e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.63 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 437 VVVMEDVSLVIPAGKTTALVGASGSGKS----TIVGLVERFYKPIEGKVYLDDVDISTLNVR----WLRQQIALVSQEPT 508
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRerrkIIGREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 509 lfAC-----TIYDNI-----RHGLIGTKWESESeeqqreriyeaARKANA-----------HDFI-TSLPegYEtnvger 566
Cdd:COG4170 100 --SCldpsaKIGDQLieaipSWTFKGKWWQRFK-----------WRKKRAiellhrvgikdHKDImNSYP--HE------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 567 gflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALE-VAAEGRTTIT-IAHRLSTI-KDAHNIVVMAQG 643
Cdd:COG4170 159 ---LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLArLNQLQGTSILlISHDLESIsQWADTITVLYCG 235
|
250
....*....|....
gi 164423939 644 RIVEQGTHAELLAK 657
Cdd:COG4170 236 QTVESGPTEQILKS 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1075-1313 |
3.01e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1075 PTVDTWSNEGDLIKQVDGTIEFRDVHFRYPTRP--------EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFY 1146
Cdd:PRK10261 295 PAKQEPPIEQDTVVDGEPILQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1147 DPLSGGIFIDGREISSLNVNEYRSF---IALVSQEPTLY---QGTVRENII--LGANNDVTDEQIkfACQEANIYDFIMS 1218
Cdd:PRK10261 375 ESQGGEIIFNGQRIDTLSPGKLQALrrdIQFIFQDPYASldpRQTVGDSIMepLRVHGLLPGKAA--AARVAWLLERVGL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1219 LPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKILLLDEATSALD-SESEHVVQAALD-KAAKGRTTIAVAHRLSTIQ 1296
Cdd:PRK10261 453 LPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDvSIRGQIINLLLDlQRDFGIAYLFISHDMAVVE 528
|
250
....*....|....*...
gi 164423939 1297 K-ADIIYVFDQGRIVEQG 1313
Cdd:PRK10261 529 RiSHRVAVMYLGQIVEIG 546
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1114-1318 |
3.15e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.43 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1114 GLNLSIQPGQYVALVGASGCGKST----TIALLErfydPLSGGIFIDGREISSLNVNEY---RSFIALVSQEPtLYQGTV 1186
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP-LASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 RENIilganNDVTDEQIKfacqeanIYDFIMSLPD------GMNTLVGskgaLL-----------SGGQKQRIAIARALI 1249
Cdd:PRK15079 114 RMTI-----GEIIAEPLR-------TYHPKLSRQEvkdrvkAMMLKVG----LLpnlinryphefSGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1250 RDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
160-354 |
4.32e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 71.77 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 160 YITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFVIGFV 239
Cdd:cd18564 72 YAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFW 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 240 SFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAHLTRAEHFGF 319
Cdd:cd18564 152 LDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGL 231
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 164423939 320 ---RLKGSIGVMVAGMMTVlylnyGLAF--WQGSRFLLSG 354
Cdd:cd18564 232 raaRLQALLSPVVDVLVAV-----GTALvlWFGAWLVLAG 266
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
439-661 |
5.87e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.91 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTL-NVRWLRQQIALVSQEPTLFA-CTIYD 516
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAIVPEGRRVFSrMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 517 NIRHGliGTKWESESEEQQRERIYEAarkanahdfitsLPEGYETNVgERGFLLSGGQKQRIAIARAIVSDPKILLLDEA 596
Cdd:PRK11614 100 NLAMG--GFFAERDQFQERIKWVYEL------------FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 597 TSALdtkSEGVVQAAL----EVAAEGRTTITIAHRLS-TIKDAHNIVVMAQGRIVEQGTHAELLAK---RGAY 661
Cdd:PRK11614 165 SLGL---APIIIQQIFdtieQLREQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANeavRSAY 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1093-1318 |
6.14e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYPTRpEQPVLRGLNLSIQPGQYVALVGASGCGKS-TTIALLERFYDP----LSGGIFIDGReiSSLNVNE 1167
Cdd:PRK15134 7 AIENLSVAFRQQQT-VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGE--SLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1168 YR------SFIALVSQEPTLYQGTVrENIilganndvtdeqikfacqEANIYDfIMSLPDGMNT------------LVGS 1229
Cdd:PRK15134 84 QTlrgvrgNKIAMIFQEPMVSLNPL-HTL------------------EKQLYE-VLSLHRGMRReaargeilncldRVGI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1230 KGAL---------LSGGQKQRIAIARALIRDPKILLLDEATSALDSesehVVQA---ALDKAAKGRTTIA---VAHRLST 1294
Cdd:PRK15134 144 RQAAkrltdyphqLSGGERQRVMIAMALLTRPELLIADEPTTALDV----SVQAqilQLLRELQQELNMGllfITHNLSI 219
|
250 260
....*....|....*....|....*
gi 164423939 1295 IQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK15134 220 VRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
815-1027 |
8.86e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 70.59 E-value: 8.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 815 CLMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTEtthVAGLSGV---T 891
Cdd:cd18550 42 ALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTR--TRTGEIQSRLNND---VGGAQSVvtgT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 892 LGTIIMVLTTLIAACTVALALGWKLALVCIATIPILLGCGFY---RFWMIAhyqRRAKSAYAGSASYASEAITA--MRTV 966
Cdd:cd18550 117 LTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRvgrRRRKLT---REQQEKLAELNSIMQETLSVsgALLV 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 967 ASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHE 1027
Cdd:cd18550 194 KLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGG 254
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1112-1311 |
9.43e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 9.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYdP---LSGGIFIDG--REISSLNVNEYRSfIALVSQE----PTLy 1182
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGevCRFKDIRDSEALG-IVIIHQElaliPYL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1183 qgTVRENIILG---ANNDVTDEQIKFAcqEANIYDFIMSLPDGMNTLVGSKGAllsgGQKQRIAIARALIRDPKILLLDE 1259
Cdd:NF040905 94 --SIAENIFLGnerAKRGVIDWNETNR--RARELLAKVGLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 164423939 1260 ATSAL-DSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVE 1311
Cdd:NF040905 166 PTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
434-625 |
9.85e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.75 E-value: 9.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 434 RPDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVerfyKPIEGKVYLDDVDISTLNVR----WLRQQIALvsq 505
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTllrlIAGLL----PPAAGTIKLDGGDIDDPDVAeachYLGHRNAM--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 506 EPTLfacTIYDNIR--HGLIGTkweseseeqQRERIYEAARKANAHDfITSLPEGYetnvgergflLSGGQKQRIAIARA 583
Cdd:PRK13539 85 KPAL---TVAENLEfwAAFLGG---------EELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 164423939 584 IVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIA 625
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1115-1319 |
1.01e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1115 LNLSIqPGQYV-ALVGASGCGKSTTIALLERFYDPLSGGIFIDGREI--SSLNVN---EYRSfIALVSQEPTLY-QGTVR 1187
Cdd:PRK11144 17 VNLTL-PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdAEKGIClppEKRR-IGYVFQDARLFpHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1188 ENIILGANNDVTDEqikfacqeaniYDFIMSLPdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSE 1267
Cdd:PRK11144 95 GNLRYGMAKSMVAQ-----------FDKIVALL-GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1268 SEHVVQAALDKAAKGRTT--IAVAHRLSTIQK-ADIIYVFDQGRIVEQGT-----HSELM 1319
Cdd:PRK11144 163 RKRELLPYLERLAREINIpiLYVSHSLDEILRlADRVVVLEQGKVKAFGPleevwASSAM 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1114-1318 |
1.16e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 69.63 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1114 GLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSL---------------NVNEYRSFIA----L 1174
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghqiarmgvvrtfqHVRLFREMTVienlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1175 VSQEPTLYQGTVRENIILGANNDVTDEQIKFAcqeANIYDFiMSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKI 1254
Cdd:PRK11300 103 VAQHQQLKTGLFSGLLKTPAFRRAESEALDRA---ATWLER-VGLLEHANRQAGN----LAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1255 LLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1111-1321 |
1.40e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.76 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERF--YDPLSGGI-----------FID------------GREISSLNV 1165
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVErpskvgepcpvcGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1166 N----------EYRSFIALVSQEP-TLY-QGTVRENIIlGANNDV---TDEQIKFAC---QEANIYDFIMSLPDGmntlv 1227
Cdd:TIGR03269 95 DfwnlsdklrrRIRKRIAIMLQRTfALYgDDTVLDNVL-EALEEIgyeGKEAVGRAVdliEMVQLSHRITHIARD----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1228 gskgalLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQK-ADIIYVF 1304
Cdd:TIGR03269 169 ------LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlSDKAIWL 242
|
250
....*....|....*..
gi 164423939 1305 DQGRIVEQGTHSELMKK 1321
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV 259
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
414-669 |
2.49e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.18 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 414 KLENV-----VGTIRLENIKHI-----YPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYL 483
Cdd:COG1134 6 EVENVsksyrLYHEPSRSLKELllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 484 DDvdistlNVRWLrqqIAL-VSQEPTLfacTIYDNIRhgLIGTkweseseeqqrerIY-----EAARKAnahDFITSLPE 557
Cdd:COG1134 86 NG------RVSAL---LELgAGFHPEL---TGRENIY--LNGR-------------LLglsrkEIDEKF---DEIVEFAE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 558 gyetnVGErgFL------LSGGQKQRIAIARAIVSDPKILLLDEATSALDT----KSEGVVQaalEVAAEGRTTITIAHR 627
Cdd:COG1134 136 -----LGD--FIdqpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARIR---ELRESGRTVIFVSHS 205
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 164423939 628 LSTIKD-AHNIVVMAQGRIVEQGTHAELLAkrgAYYKLVTAQA 669
Cdd:COG1134 206 MGAVRRlCDRAIWLEKGRLVMDGDPEEVIA---AYEALLAGRE 245
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1108-1299 |
2.94e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlNVNEYRSFIALVSQE----PTLyq 1183
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRsginPYL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1184 gTVRENIILGANNDVTDEQIKFACQeaniydfIMSLPDGMNTLVGskgaLLSGGQKQRIAIARALIRDPKILLLDEATSA 1263
Cdd:PRK13540 90 -TLRENCLYDIHFSPGAVGITELCR-------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 164423939 1264 LDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQKAD 1299
Cdd:PRK13540 158 LDELSLLTIITKIQEhRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
813-1027 |
2.96e-12 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 68.98 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 813 FWCLMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTL 892
Cdd:cd18541 41 RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQK--NRTGDLMARATNDLNAVRMALGPGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 893 GTIIMVLTTLIAACTVALALGWKLALVCIATIPILLGCgFYRFW-MIAHYQRRAKSAYAGSASYASEAITAMRTVASLTR 971
Cdd:cd18541 119 LYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALL-VYRLGkKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQ 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 972 EQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHE 1027
Cdd:cd18541 198 EEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGT 253
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1121-1305 |
3.11e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 65.47 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1121 PGQYVALVGASGCGKSTTIALLERFYDPLSGG-IFIDGREISSLNVNEYRsfialvsqeptlyqgtvreniilganndvt 1199
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1200 deqikfacqeaniydfimslpdgmNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALD-- 1277
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180 190
....*....|....*....|....*....|...
gi 164423939 1278 -----KAAKGRTTIAVAHRLSTIQKADIIYVFD 1305
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
443-650 |
3.19e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.50 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 443 VSLVIPAGKTTALVGASGSGKSTIV----GLVERFYKP------------IEGKVyLDDVDISTLNVRWLRQQIALVSQe 506
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAgshiellgrtvqREGRL-ARDIRKSRANTGYIFQQFNLVNR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 ptlfaCTIYDNIRHGLIGTK--WESESEEqqreriYEAARKANAHDFITSLpeGYETNVGERGFLLSGGQKQRIAIARAI 584
Cdd:PRK09984 101 -----LSVLENVLIGALGSTpfWRTCFSW------FTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 585 VSDPKILLLDEATSALDTKSEGVVQAALE--VAAEGRTTITIAHRLS-TIKDAHNIVVMAQGRIVEQGT 650
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
422-656 |
3.73e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.60 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPS--RPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYL---DD-VDISTLNVRW 495
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgDEwVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 ---LRQQIALVSQEPTLFA-CTIYDNIRHGlIGTKWEseseeqqreriYEAARKANAHDFITS-LPEGYETNVGER-GFL 569
Cdd:TIGR03269 360 rgrAKRYIGILHQEYDLYPhRTVLDNLTEA-IGLELP-----------DELARMKAVITLKMVgFDEEKAEEILDKyPDE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAE--GRTTITIAHRLSTIKDAHNIV-VMAQGRIV 646
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAaLMRDGKIV 507
|
250
....*....|
gi 164423939 647 EQGTHAELLA 656
Cdd:TIGR03269 508 KIGDPEEIVE 517
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
141-259 |
4.16e-12 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 68.57 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 141 LARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKV 220
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGL 119
|
90 100 110
....*....|....*....|....*....|....*....
gi 164423939 221 GLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVM 259
Cdd:cd18544 120 VTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLAT 158
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
833-984 |
4.25e-12 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 68.52 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 833 GWLFAKCSERLIHRVRDMAFRSFLRQDVEFFdrDENSAGALTSFLSTETTHVAglSGVTLGTIIMVLTTL--IAACTVAL 910
Cdd:cd18590 57 GGLFMCTLSRLNLRLRHQLFSSLVQQDIGFF--EKTKTGDLTSRLSTDTTLMS--RSVALNANVLLRSLVktLGMLGFML 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 911 ALGWKLALVCIATIPILlgcGFYRFWMIAHYQRRAKS---AYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLA 984
Cdd:cd18590 133 SLSWQLTLLTLIEMPLT---AIAQKVYNTYHQKLSQAvqdSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALE 206
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1108-1312 |
5.12e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKSTTI-ALLERFYDPLSGGIFidgrEISSLNVNEYRSFIALVSQEPTLYQGTV 1186
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLrLLAGALKGTPVAGCV----DVPDNQFGREASLIDAIGRKGDFKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 reniILGAnndvtdeqikfacqeaniydfiMSLPDgmNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDS 1266
Cdd:COG2401 118 ----LLNA----------------------VGLSD--AVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1267 ESEHVVQAALDKAAK--GRTTIAVAHR---LSTIQKADIIYVFDQGRIVEQ 1312
Cdd:COG2401 170 QTAKRVARNLQKLARraGITLVVATHHydvIDDLQPDLLIFVGYGGVPEEK 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
435-654 |
5.53e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 435 PDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVR-WLRQQIALVSQE----PTL 509
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 510 facTIYDNI-------RHGLIGTKweseseeqqrERIYEAAR--KANAHDFITSLPEGYetnvgergflLSGGQKQRIAI 580
Cdd:PRK11288 95 ---TVAENLylgqlphKGGIVNRR----------LLNYEAREqlEHLGVDIDPDTPLKY----------LSIGQRQMVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 581 ARAIVSDPKILLLDEATSALDTK-SEGVVQAALEVAAEGRTTITIAHRLSTI---KDAhnIVVMAQGRIVEqgTHAEL 654
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAReIEQLFRVIRELRAEGRVILYVSHRMEEIfalCDA--ITVFKDGRYVA--TFDDM 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1087-1314 |
6.01e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.83 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1087 IKQVDGTIEFRDVHFRYPTrPEQPVLR---GLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGI-------FID 1156
Cdd:TIGR03269 273 VEVGEPIIKVRNVSKRYIS-VDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1157 GREISSLNVNEYRSFIALVSQEPTLY-QGTVRENIILGANNDVTDE-----------QIKFACQEA-NIYDfimSLPDGm 1223
Cdd:TIGR03269 352 MTKPGPDGRGRAKRYIGILHQEYDLYpHRTVLDNLTEAIGLELPDElarmkavitlkMVGFDEEKAeEILD---KYPDE- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1224 ntlvgskgalLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAH----------R 1291
Cdd:TIGR03269 428 ----------LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHdmdfvldvcdR 497
|
250 260
....*....|....*....|...
gi 164423939 1292 LSTIQKADIIYVFDQGRIVEQGT 1314
Cdd:TIGR03269 498 AALMRDGKIVKIGDPEEIVEELT 520
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
419-656 |
7.93e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.91 E-value: 7.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 419 VGTIRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTlNVRWLRQ 498
Cdd:PRK13537 5 VAPIDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 499 QIALVSQEPTL---FacTIYDNIR-----HGLigtkwESESEEQQRERIYEAARKANAHDfitslpegyeTNVGErgflL 570
Cdd:PRK13537 81 RVGVVPQFDNLdpdF--TVRENLLvfgryFGL-----SAAAARALVPPLLEFAKLENKAD----------AKVGE----L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 571 SGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALE-VAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQ 648
Cdd:PRK13537 140 SGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRsLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAE 219
|
....*...
gi 164423939 649 GTHAELLA 656
Cdd:PRK13537 220 GAPHALIE 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
443-655 |
1.13e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 443 VSLVIPAGKTTALVGASGSGKST----IVGLVerfykPIEGKVYLDDVDISTLNVRWLRQQIA-LVSQEPTLFACTIYdn 517
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTllarMAGLL-----PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 518 irHGLIGTKWESESEEQQRERIYEAARKANAHDFItslpegyETNVGErgflLSGGQKQRIAIA-------RAIVSDPKI 590
Cdd:PRK03695 88 --QYLTLHQPDKTRTEAVASALNEVAEALGLDDKL-------GRSVNQ----LSGGEWQRVRLAavvlqvwPDINPAGQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 591 LLLDEATSALDtksegVVQAAL------EVAAEGRTTITIAHRLS-TIKDAHNIVVMAQGRIVEQGTHAELL 655
Cdd:PRK03695 155 LLLDEPMNSLD-----VAQQAAldrllsELCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
424-649 |
1.18e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 66.20 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 424 LENIKHIY-PSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIAL 502
Cdd:cd03267 20 IGSLKSLFkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 503 VSQEPTLfactIYD-NIRHGLigtkweseseeQQRERIY--EAARKANAHDFITSLPE-GYETNVGERGflLSGGQKQRI 578
Cdd:cd03267 100 FGQKTQL----WWDlPVIDSF-----------YLLAAIYdlPPARFKKRLDELSELLDlEELLDTPVRQ--LSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 579 AIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITI-AHRLSTI-KDAHNIVVMAQGRIVEQG 649
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLkEYNRERGTTVLLtSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
130-355 |
1.34e-11 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 67.05 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 130 GVTTYDDFTDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADT 209
Cdd:cd18541 28 ALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 210 NLIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVIS 289
Cdd:cd18541 108 NAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFS 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 290 SVRnAI-AFGTQDRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNYGLAFWQGSRFLLSGD 355
Cdd:cd18541 188 GIR-VIkAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGT 253
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1112-1318 |
1.47e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREIsslNVNEYRSF----IALVSQEPTLY-QGTV 1186
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV---TFNGPKSSqeagIGIIHQELNLIpQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 RENIILGANNDVTDEQIKFA--CQEANIYDFIMSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKILLLDEATSAL 1264
Cdd:PRK10762 97 AENIFLGREFVNRFGRIDWKkmYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1265 -DSESEHVVQAALDKAAKGRTTIAVAHRLSTI-QKADIIYVFDQGRIVEQGTHSEL 1318
Cdd:PRK10762 173 tDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDGQFIAEREVADL 228
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
813-1020 |
1.74e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 66.82 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 813 FWCLMYLMLA--LVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDrdENSAGALTSFLSTETTHVAGLSGV 890
Cdd:cd18565 53 LWLLGGLTVAafLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFE--DRQTGDLMSVLNNDVNQLERFLDD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 891 TLGTIIMVLTTLIAACTVALALGWKLALVCIATIPILLGCGFYrfwmiahYQRRAKSAY------AGS-ASYASEAITAM 963
Cdd:cd18565 131 GANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYW-------FQRRIEPRYravreaVGDlNARLENNLSGI 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 964 RTVASLTREQ-------DVLQHYKDslakqqhASLISVLKSSLLFAASNSLMFLAFALGFWYGG 1020
Cdd:cd18565 204 AVIKAFTAEDferervaDASEEYRD-------ANWRAIRLRAAFFPVIRLVAGAGFVATFVVGG 260
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
428-644 |
1.93e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 428 KHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYkP---IEGKVYLDDVDISTLNVRWL-RQQIALV 503
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTeRAGIAII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 504 SQEPTLFA-CTIYDNI-------RHGLIgtkweseseeqQRERIYEAARKANAHDFITSLPEgyeTNVGErgflLSGGQK 575
Cdd:PRK13549 88 HQELALVKeLSVLENIflgneitPGGIM-----------DYDAMYLRAQKLLAQLKLDINPA---TPVGN----LGLGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 576 QRIAIARAIVSDPKILLLDEATSALdTKSEGVVQAAL--EVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGR 644
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1106-1290 |
2.07e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1106 RPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNvNEYRSfiALvsqeptLYQG- 1184
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQ--DL------LYLGh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 --------TVREN--IILGANNDVTDEQIKFACQEANIYDFimslpdgMNTLVGSkgalLSGGQKQRIAIARALIRDPKI 1254
Cdd:PRK13538 82 qpgiktelTALENlrFYQRLHGPGDDEALWEALAQVGLAGF-------EDVPVRQ----LSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 164423939 1255 LLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAH 1290
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1112-1329 |
2.23e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.65 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGReISSLNVNEYRSFIALV----SQeptLYQG-TV 1186
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-VPFKRRKEFARRIGVVfgqrSQ---LWWDlPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1187 REN-IILGANNDVTDEQIKfacqeANIYDF--IMSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKILLLDEATSA 1263
Cdd:COG4586 114 IDSfRLLKAIYRIPDAEYK-----KRLDELveLLDLGELLDTPVRQ----LSLGQRMRCELAAALLHRPKILFLDEPTIG 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1264 LDSESEHVVQAALDK--AAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGTHSELMKKNGRYAELV 1329
Cdd:COG4586 185 LDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYKTIV 253
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
416-604 |
2.46e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.19 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 416 ENVVGTIRLEniKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRW 495
Cdd:PRK10584 4 ENIVEVHHLK--KSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 496 ---LR-QQIALVSQE----PTLFActiYDNIRHG--LIGTKweseseeqqreriyEAARKANAHDFITSLpegyetNVGE 565
Cdd:PRK10584 82 rakLRaKHVGFVFQSfmliPTLNA---LENVELPalLRGES--------------SRQSRNGAKALLEQL------GLGK 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 164423939 566 R----GFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKS 604
Cdd:PRK10584 139 RldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
422-647 |
3.24e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVErfykPIEGKVylddvDISTlNVRwlr 497
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTllklLAGELE----PDSGTV-----KLGE-TVK--- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 qqIALVSQEPTLFAC--TIYDNIRHGLigtkweseseeqqreriyeaarkanahdfitslPEGYETNVgeRGFL------ 569
Cdd:COG0488 380 --IGYFDQHQEELDPdkTVLDELRDGA---------------------------------PGGTEQEV--RGYLgrflfs 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 ----------LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEvAAEGrTTITIAH-R--LSTIkdAHN 636
Cdd:COG0488 423 gddafkpvgvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATR 498
|
250
....*....|.
gi 164423939 637 IVVMAQGRIVE 647
Cdd:COG0488 499 ILEFEDGGVRE 509
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
428-654 |
4.07e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 428 KHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQ-QIALVSQE 506
Cdd:PRK15439 15 RSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 PTLFA-CTIYDNIRHGLIGTkweseseeqqreriyeAARKANAHDFITSLpeGYETNVGERGFLLSGGQKQRIAIARAIV 585
Cdd:PRK15439 95 PLLFPnLSVKENILFGLPKR----------------QASMQKMKQLLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 586 SDPKILLLDEATSALD-TKSEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAEL 654
Cdd:PRK15439 157 RDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
401-632 |
4.31e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 67.47 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 401 RESPIDSSSEEG---------GKLENVVGTIRLENIKHIYPSrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVE 471
Cdd:TIGR00954 422 RVEEIESGREGGrnsnlvpgrGIVEYQDNGIKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILG 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 472 --------RFYKPIEGKV-YLDDVDISTLnvRWLRQQIalvsqeptLFACTIYDNIRHGLigtkweseseeqqreriyea 542
Cdd:TIGR00954 500 elwpvyggRLTKPAKGKLfYVPQRPYMTL--GTLRDQI--------IYPDSSEDMKRRGL-------------------- 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 543 arkaNAHDFITSLPEGYETNVGERGF----------LLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEG-VVQAA 611
Cdd:TIGR00954 550 ----SDKDLEQILDNVQLTHILEREGgwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGyMYRLC 625
|
250 260
....*....|....*....|.
gi 164423939 612 LEVaaeGRTTITIAHRLSTIK 632
Cdd:TIGR00954 626 REF---GITLFSVSHRKSLWK 643
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1106-1290 |
4.96e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 63.67 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1106 RPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNEYRSFIALVSQEPTLYQGT 1185
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1186 VRENIILGANnDVTDEQIKFACQEAniydfimslpdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALD 1265
Cdd:cd03231 90 VLENLRFWHA-DHSDEQVEEALARV-----------GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*.
gi 164423939 1266 SESEHVVQAAL-DKAAKGRTTIAVAH 1290
Cdd:cd03231 158 KAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1110-1310 |
5.76e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.59 E-value: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1110 PVLRGLNLSIQPGQYVALVGASGCGKSTTIALL--ERfyDPLSGGIFIDGREISSLNVNEYR----SFI-------ALVs 1176
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRrlgvAYIpedrlgrGLV- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1177 qePTLyqgTVRENIILG----------------ANNDVTDEQIKfacqEANIydfimsLPDGMNTLVGSkgalLSGGQKQ 1240
Cdd:COG3845 349 --PDM---SVAENLILGryrrppfsrggfldrkAIRAFAEELIE----EFDV------RTPGPDTPARS----LSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1241 RIAIARALIRDPKILLLDEATSALDSES-EHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIV 1310
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1111-1315 |
6.34e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 67.18 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIallerfyDPLSG---GIFIDGR-EISSL-NVNEYRSFIALVSQEPTLY--Q 1183
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLM-------DVLAGrktGGYIEGDiRISGFpKKQETFARISGYCEQNDIHspQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1184 GTVRENIILGA----NNDVT-DEQIKFACQEANIYDfIMSLPDGMNTLVGSKGalLSGGQKQRIAIARALIRDPKILLLD 1258
Cdd:PLN03140 968 VTVRESLIYSAflrlPKEVSkEEKMMFVDEVMELVE-LDNLKDAIVGLPGVTG--LSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1259 EATSALDSESEHVVQAAL-DKAAKGRTTIAVAHRLSTiqkaDIIYVFDQGRIVEQGTH 1315
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
422-613 |
8.75e-11 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 61.31 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdvvVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDvdistlnvrwlRQQIA 501
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LVSQeptlfactiydnirhgligtkweseseeqqreriyeaarkanahdfitslpegyetnvgergflLSGGQKQRIAIA 581
Cdd:cd03221 67 YFEQ----------------------------------------------------------------LSGGEKMRLALA 82
|
170 180 190
....*....|....*....|....*....|..
gi 164423939 582 RAIVSDPKILLLDEATSALDTKSegvvQAALE 613
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLES----IEALE 110
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
421-649 |
1.01e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQ- 499
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEPTLF-ACTIYDNIRHGLIGTK---------WEseseeqqreriyEAARKANAHDFITSLPEGYETNVGErgfl 569
Cdd:PRK09700 82 IGIIYQELSVIdELTVLENLYIGRHLTKkvcgvniidWR------------EMRVRAAMMLLRVGLKVDLDEKVAN---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVE 647
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMnQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVC 225
|
..
gi 164423939 648 QG 649
Cdd:PRK09700 226 SG 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1107-1290 |
1.15e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.73 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1107 PEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLerfydplsGGI--FIDGREISSLNVNeyrsfIALVSQEPTLYQG 1184
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM--------AGVdkDFNGEARPQPGIK-----VGYLPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 -TVRENIILG----------------ANNDVTDEQIKFACQEANIYDFI------------------MSLPDGmntlvGS 1229
Cdd:TIGR03719 83 kTVRENVEEGvaeikdaldrfneisaKYAEPDADFDKLAAEQAELQEIIdaadawdldsqleiamdaLRCPPW-----DA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1230 KGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALdKAAKGrTTIAVAH 1290
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1112-1310 |
1.22e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE-YRSFIALVSQEPTLY-QGTVREN 1189
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVlQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1190 IILG--ANNDVTDEQIKFACQEANIYDFImslpdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSAL-DS 1266
Cdd:PRK10982 94 MWLGryPTKGMFVDQDKMYRDTKAIFDEL-----DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 164423939 1267 ESEHVVQAALDKAAKGRTTIAVAHRLSTI-QKADIIYVFDQGRIV 1310
Cdd:PRK10982 169 EVNHLFTIIRKLKERGCGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
443-654 |
1.46e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.09 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 443 VSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTL---------------NVRWLRQQIA----LV 503
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghqiarmgvvrtfqHVRLFREMTVienlLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 504 SQEPTLFActiydNIRHGLIGTKweseseeqqreriyeAARKANAhdfitslpEGYE------TNVGERGFL------LS 571
Cdd:PRK11300 104 AQHQQLKT-----GLFSGLLKTP---------------AFRRAES--------EALDraatwlERVGLLEHAnrqagnLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 572 GGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAE--GRTTITIAHRLSTIKDAHN-IVVMAQGRIVEQ 648
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDrIYVVNQGTPLAN 235
|
....*.
gi 164423939 649 GTHAEL 654
Cdd:PRK11300 236 GTPEEI 241
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
166-313 |
1.88e-10 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 63.51 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 166 FIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLTLQALATfiaafVIGFVSF---- 241
Cdd:cd18590 60 FMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVK-----TLGMLGFmlsl 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 242 -WKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAHLTR 313
Cdd:cd18590 135 sWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALER 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
434-650 |
2.00e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 434 RPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDD----------VDISTLNVRWLRQ----Q 499
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHvrgaD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQEPT-----LFAC--TIYDNIR-HGLIGTKweseseeqqreriyEAARKANAHDFITSLPEGyETNVGERGFLLS 571
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRlHQGASRE--------------EAMVEAKRMLDQVRIPEA-QTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 572 GGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRT--TITIAHRLSTIKD-AHNIVVMAQGRIVEQ 648
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVET 250
|
..
gi 164423939 649 GT 650
Cdd:PRK10261 251 GS 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1106-1314 |
2.20e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1106 RPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGI-------------FIDGREISSLNVNEYR-SF 1171
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1172 IALVSQEPT------------------LYQGTVRENIILGANNDVtdEQIKfacqeaniydfimsLPDGmNTLVGSKGAL 1233
Cdd:PRK10261 106 MAMIFQEPMtslnpvftvgeqiaesirLHQGASREEAMVEAKRML--DQVR--------------IPEA-QTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1234 LSGGQKQRIAIARALIRDPKILLLDEATSALDSesehVVQAALDKAAK------GRTTIAVAHRLSTIQK-ADIIYVFDQ 1306
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDV----TIQAQILQLIKvlqkemSMGVIFITHDMGVVAEiADRVLVMYQ 244
|
....*...
gi 164423939 1307 GRIVEQGT 1314
Cdd:PRK10261 245 GEAVETGS 252
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
414-650 |
2.37e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.42 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 414 KLENVVGTIRLENIKHIY-PS-RPDVvvmEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTl 491
Cdd:TIGR01257 921 ELPGLVPGVCVKNLVKIFePSgRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET- 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 492 NVRWLRQQIALVSQEPTLFA-CTIYDNI--RHGLIGTKWEseseeqqreriyEAARKANAHDFITslpeGYETNVGERGF 568
Cdd:TIGR01257 997 NLDAVRQSLGMCPQHNILFHhLTVAEHIlfYAQLKGRSWE------------EAQLEMEAMLEDT----GLHHKRNEEAQ 1060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 569 LLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVE 647
Cdd:TIGR01257 1061 DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYC 1140
|
...
gi 164423939 648 QGT 650
Cdd:TIGR01257 1141 SGT 1143
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
436-650 |
2.61e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.59 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 DVVVMEDVSLVIPAGKTTALVGASGSGKS----TIVGLVERFYKpIEGKVYLDDVDISTLNVRWLR----QQIALVSQEP 507
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREILNLPEKELNklraEQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 508 tLFACTIYDNIRHGLI-----------GTKWESESEEQQRERIYEAARKAN--AHDFitslpegyetnvgergfllSGGQ 574
Cdd:PRK09473 107 -MTSLNPYMRVGEQLMevlmlhkgmskAEAFEESVRMLDAVKMPEARKRMKmyPHEF-------------------SGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALDTksegVVQAAL-----EVAAEGRTT-ITIAHRLST---IKDahNIVVMAQGRI 645
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDV----TVQAQImtllnELKREFNTAiIMITHDLGVvagICD--KVLVMYAGRT 240
|
....*
gi 164423939 646 VEQGT 650
Cdd:PRK09473 241 MEYGN 245
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
450-646 |
2.91e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 60.08 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 450 GKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIAlvsqeptlfactiydnirhgligtkwes 529
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 530 eseeqqreriyeaarkanahdfitslpegyetnVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQ 609
Cdd:smart00382 54 ---------------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLL 100
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 164423939 610 AALEVAA------EGRTTITIAHRLSTIKDAHNIVVMAQGRIV 646
Cdd:smart00382 101 LLEELRLllllksEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
433-625 |
2.94e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 61.22 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 433 SRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWlRQQIALVSQEPTL-FA 511
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLkPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 512 CTIYDNIRhgligtkWESESEEQQRERIYEAARKANAHDFiTSLPEGYetnvgergflLSGGQKQRIAIARAIVSDPKIL 591
Cdd:TIGR01189 88 LSALENLH-------FWAAIHGGAQRTIEDALAAVGLTGF-EDLPAAQ----------LSAGQQRRLALARLWLSRRPLW 149
|
170 180 190
....*....|....*....|....*....|....*
gi 164423939 592 LLDEATSALDtkSEGVVQAALEVAAE-GRTTITIA 625
Cdd:TIGR01189 150 ILDEPTTALD--KAGVALLAGLLRAHlARGGIVLL 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
424-646 |
3.21e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.08 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 424 LENIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYK--PIEGKVYLDDVDISTLNVRWL-RQQI 500
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTeRAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEPTLFA-CTIYDNIrhgLIGTKWESESEEQQRERIYEAARKANAHDFITSLPEgyETNVGERGfllsGGQKQRIA 579
Cdd:TIGR02633 81 VIIHQELTLVPeLSVAENI---FLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNV--TRPVGDYG----GGQQQLVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 580 IARAIVSDPKILLLDEATSAL-DTKSEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIV 646
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
138-341 |
4.57e-10 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 62.45 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 138 TDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGIS 217
Cdd:cd18542 35 RELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 218 EKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLvmgggsqFIIKFSKQNIAAY-----AEG--GSVADEVISS 290
Cdd:cd18542 115 FGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIAL-------FSYVFFKKVRPAFeeireQEGelNTVLQENLTG 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 291 VRNAIAFGTQ-------DRLARRY-DAHLTRAEHFGFRLkgSIGVMVAGMMTVLYLNYG 341
Cdd:cd18542 188 VRVVKAFAREdyeiekfDKENEEYrDLNIKLAKLLAKYW--PLMDFLSGLQIVLVLWVG 244
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
427-631 |
4.85e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQ-IALVSQ 505
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 506 EPTLFA-CTIYDNI--------RHGLIgtKWeseseeqqrERIYEAARKANAHdfiTSLPEGYETNVGErgflLSGGQKQ 576
Cdd:PRK10762 87 ELNLIPqLTIAENIflgrefvnRFGRI--DW---------KKMYAEADKLLAR---LNLRFSSDKLVGE----LSIGEQQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 577 RIAIARAIVSDPKILLLDEATSAL-DTKSEGVVQAALEVAAEGRTTITIAHRLSTI 631
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEI 204
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
766-1014 |
5.27e-10 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 62.04 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 766 MLVGIFFSAICGAGNPTQAVFFAKLISSLSRPIVNeeIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKCSERLIH 845
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGG--GGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 846 RVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIP 925
Cdd:cd18547 79 DLRKDLFEKLQRLPLSYFDT--HSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 926 ILLgcgFYRFWMIAHYQR--RAKSAYAGS-ASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFA 1002
Cdd:cd18547 157 LSL---LVTKFIAKRSQKyfRKQQKALGElNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMP 233
|
250
....*....|..
gi 164423939 1003 ASNSLMFLAFAL 1014
Cdd:cd18547 234 IMNFINNLGYVL 245
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
420-646 |
5.80e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 420 GTIRLEnIKHI-YPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKS----TIVGLVerfyKPIEGKVYLDDVDISTLNVR 494
Cdd:COG3845 254 GEVVLE-VENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSelaeALAGLR----PPASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 495 WLRQQ-IALVSQEPTLFAC----TIYDNI-----------RHGLIgtKWeseseeqqreriyeAARKANAHDFITSL--- 555
Cdd:COG3845 329 ERRRLgVAYIPEDRLGRGLvpdmSVAENLilgryrrppfsRGGFL--DR--------------KAIRAFAEELIEEFdvr 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 556 PEGYETNVGergfLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALEVAAEGRTTITIAHRLSTIKD- 633
Cdd:COG3845 393 TPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAl 468
|
250
....*....|...
gi 164423939 634 AHNIVVMAQGRIV 646
Cdd:COG3845 469 SDRIAVMYEGRIV 481
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
816-1034 |
9.49e-10 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 61.31 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 816 LMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFD-RdenSAGALTSFLStETTHV-AGLSGVTLG 893
Cdd:cd18570 46 IGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFEtR---KTGEIISRFN-DANKIrEAISSTTIS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 894 TIIMVLTTLIAACTVALaLGWKLALVCIATIPI--LLGCGFYRFwmIAHYQRRAKSAYAGSASYASEAITAMRTVASLTR 971
Cdd:cd18570 122 LFLDLLMVIISGIILFF-YNWKLFLITLLIIPLyiLIILLFNKP--FKKKNREVMESNAELNSYLIESLKGIETIKSLNA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 972 EQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHEY---DMFTFF 1034
Cdd:cd18570 199 EEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLslgQLIAFN 264
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
144-358 |
1.00e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 61.37 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 144 LVLYFVYLAiGEFVTMYITTVGfIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLT 223
Cdd:cd18563 47 LGLAGAYVL-SALLGILRGRLL-ARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 224 LQALATFIAAFVIGFVSFWKLTLILLST---VVALTLVMGggsQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQ 300
Cdd:cd18563 125 LTNILMIIGIGVVLFSLNWKLALLVLIPvplVVWGSYFFW---KKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 301 DRLARRYDA---HLTRAEHFGFRLKGSIG-----VMVAGMMTVLYLnyglafwqGSRFLLSGDTEL 358
Cdd:cd18563 202 KREIKRFDEanqELLDANIRAEKLWATFFplltfLTSLGTLIVWYF--------GGRQVLSGTMTL 259
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1087-1293 |
1.62e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.46 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1087 IKQVDGTIEFRDVHFRYPTrpEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYdPLSGGIFIDGREISslnvn 1166
Cdd:TIGR00954 445 VEYQDNGIKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGK----- 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1167 eyrsfIALVSQEPTLYQGTVRENIILganNDVTDEQIKFACQEANIYDFIMSLPdgMNTLVGSKGA---------LLSGG 1237
Cdd:TIGR00954 517 -----LFYVPQRPYMTLGTLRDQIIY---PDSSEDMKRRGLSDKDLEQILDNVQ--LTHILEREGGwsavqdwmdVLSGG 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1238 QKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAakGRTTIAVAHRLS 1293
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
442-649 |
1.72e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.20 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGKTTALVGASGSGKST----IVGLVERFYKPiEGKVYLDDVDISTLNVRWlRQQIALVSQE----PTLfact 513
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PGEIIYVSEEdvhfPTL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 514 iydNIRHGLigtkweseseeqqreriyEAARKANAHDFItslpegyetnvgeRGFllSGGQKQRIAIARAIVSDPKILLL 593
Cdd:cd03233 99 ---TVRETL------------------DFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 594 DEATSALDTKSegvvqaALEVAAEGRTTITIAhRLSTI-------KDAHN----IVVMAQGRIVEQG 649
Cdd:cd03233 143 DNSTRGLDSST------ALEILKCIRTMADVL-KTTTFvslyqasDEIYDlfdkVLVLYEGRQIYYG 202
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
111-395 |
3.01e-09 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 59.72 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 111 PLMTVIFGNLQGTFQNYFAGvttyddftdeLARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNI 190
Cdd:cd18547 24 KAIDLIIEGLGGGGGVDFSG----------LLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 191 GFFDKLGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLIllstVVALTLVMGGGSQFIIK-- 268
Cdd:cd18547 94 SYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLI----VLVTVPLSLLVTKFIAKrs 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 269 ---FSKQ-----NIAAYAEggsvadEVISSVRNAIAFGTQDRLARRYDAHLTRAEHFGFRLKGSIGVMVAGMMTVLYLNY 340
Cdd:cd18547 170 qkyFRKQqkalgELNGYIE------EMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGY 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 341 GLAFWQGSRFLLSGdtelrkiltvMMSV-MIGAF---------NLGNIAPNLQAFVTALGAAAKI 395
Cdd:cd18547 244 VLVAVVGGLLVING----------ALTVgVIQAFlqysrqfsqPINQISQQINSLQSALAGAERV 298
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
426-655 |
3.59e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 426 NIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVG-LVERFYKP-------IEGKVYLDDVDISTLNVRWLR 497
Cdd:PRK13547 3 TADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 QQIALVSQ--EPTlFACTIYDNIrhgLIGTkweseseeqqreriYEAARKANA-----HDFITSLPE--GYETNVGERGF 568
Cdd:PRK13547 83 RLRAVLPQaaQPA-FAFSAREIV---LLGR--------------YPHARRAGAlthrdGEIAWQALAlaGATALVGRDVT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 569 LLSGGQKQRIAIARAI---------VSDPKILLLDEATSALD-TKSEGVVQAALEVAAEGRT-TITIAHRLS-TIKDAHN 636
Cdd:PRK13547 145 TLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADR 224
|
250
....*....|....*....
gi 164423939 637 IVVMAQGRIVEQGTHAELL 655
Cdd:PRK13547 225 IAMLADGAIVAHGAPADVL 243
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
422-601 |
3.73e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRpdvVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDvdisTLNVRWLRQQIA 501
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 LvsqEPTLfactiydnirhGLIGTKWESESEEQQRERIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIAIA 581
Cdd:PRK09544 78 L---DTTL-----------PLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLA 132
|
170 180
....*....|....*....|
gi 164423939 582 RAIVSDPKILLLDEATSALD 601
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1118-1305 |
4.50e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.57 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1118 SIQPGQYVALVGASGCGKSTTIALLerfydplSGGIFIDGREISSLNVNeyrsfialVSQEPTL----YQGTVReniilg 1193
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIELDT--------VSYKPQYikadYEGTVR------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1194 annDVTDEQIKFACQEANIYDFIMSlPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQ 1273
Cdd:cd03237 80 ---DLLSSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190
....*....|....*....|....*....|....*
gi 164423939 1274 AALDKAA--KGRTTIAVAHRLSTIQK-ADIIYVFD 1305
Cdd:cd03237 156 KVIRRFAenNEKTAFVVEHDIIMIDYlADRLIVFE 190
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
427-659 |
6.60e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 427 IKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGlvERFYKPIEGKVYLDDVDISTLNVRwLRQQ--I 500
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTlskvIAG--HPAYKILEGDILFKGESILDLEPE-ERAHlgI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEP-TLFACTIYDNIRhgligtkweseseeqqreRIYEAARKANAHDFITSLpEGYET-----------------N 562
Cdd:CHL00131 87 FLAFQYPiEIPGVSNADFLR------------------LAYNSKRKFQGLPELDPL-EFLEIineklklvgmdpsflsrN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 563 VGErGFllSGGQKQRIAIARAIVSDPKILLLDEATSALDTKsegvvqaALEVAAEG--------RTTITIAHR---LSTI 631
Cdd:CHL00131 148 VNE-GF--SGGEKKRNEILQMALLDSELAILDETDSGLDID-------ALKIIAEGinklmtseNSIILITHYqrlLDYI 217
|
250 260 270
....*....|....*....|....*....|
gi 164423939 632 KDAHnIVVMAQGRIVEQG--THAELLAKRG 659
Cdd:CHL00131 218 KPDY-VHVMQNGKIIKTGdaELAKELEKKG 246
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
789-1027 |
6.96e-09 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 58.71 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 789 KLISSLSR--PIVNEEIRASIKSDASFWCLMYLMLALVQCLAFSvqgwLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRd 866
Cdd:cd18574 21 DLVNVISRslKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYIS----LLSVVGERVAARLRNDLFSSLLRQDIAFFDT- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 867 eNSAGALTSFLST---ETTHVAGLSgVTLGtiimvL--TTLIAACTVAL-ALGWKLALVCIATIPILLGCGfyrfWMIA- 939
Cdd:cd18574 96 -HRTGELVNRLTAdvqEFKSSFKQC-VSQG-----LrsVTQTVGCVVSLyLISPKLTLLLLVIVPVVVLVG----TLYGs 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 940 ---HYQRRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASlisvLKSSL---LFAASNSLMFLAFA 1013
Cdd:cd18574 165 flrKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLN----EKLGLgigIFQGLSNLALNGIV 240
|
250
....*....|....*
gi 164423939 1014 LG-FWYGGTLIAKHE 1027
Cdd:cd18574 241 LGvLYYGGSLVSRGE 255
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1105-1299 |
1.14e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.78 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1105 TRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlnvNEYRSFIALVSQEPTLYQg 1184
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHLPGLKA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 tvreniilgannDV-TDEQIKFAC--------QEANIYDFIMSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKIL 1255
Cdd:PRK13543 96 ------------DLsTLENLHFLCglhgrrakQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLW 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1256 LLDEATSALDSESEHVVQ-----------AALDKAAKGRTTIAVAHRLSTIQKAD 1299
Cdd:PRK13543 160 LLDEPYANLDLEGITLVNrmisahlrgggAALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1112-1313 |
1.14e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.63 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREisslnvNEYRSFIALVSQEPTLYQ----GTVR 1187
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD------GQLRDLYALSEAERRRLLrtewGFVH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1188 ENIILGANNDVTdeqikfacQEANIYDFIMSL----------------------PDGMNTLVGSkgalLSGGQKQRIAIA 1245
Cdd:PRK11701 96 QHPRDGLRMQVS--------AGGNIGERLMAVgarhygdiratagdwlerveidAARIDDLPTT----FSGGMQQRLQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1246 RALIRDPKILLLDEATSALDSEsehvVQAALDKAAKGRTT------------IAVAHRLstiqkADIIYVFDQGRIVEQG 1313
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVRelglavvivthdLAVARLL-----AHRLLVMKQGRVVESG 234
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
439-633 |
1.18e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYK--PIEGKVYLDDVDIStlnvrwlrqqialvsQEptlfaCTIYD 516
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG---------------RE-----ASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 517 NIrhGLIGTKweseseeQQRERIYEAARKANAHDFITSLPEgyetnvgergflLSGGQKQRIAIARAIVSDPKILLLDEA 596
Cdd:COG2401 105 AI--GRKGDF-------KDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 164423939 597 TSALDTKSEGVVQAAL-EVAAEGRTTITIA-HRLSTIKD 633
Cdd:COG2401 164 CSHLDRQTAKRVARNLqKLARRAGITLVVAtHHYDVIDD 202
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
138-373 |
1.23e-08 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 57.79 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 138 TDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGIS 217
Cdd:cd18548 35 LSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 218 EKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRnAI-A 296
Cdd:cd18548 115 MLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIR-VIrA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 297 FGTQDRLARRYDA---HLTRAEHFGFRLkgsIGVMVAGMMTVLYLNYGLAFWQGSRFLLSGDTELRKI-------LTVMM 366
Cdd:cd18548 194 FNREDYEEERFDKandDLTDTSLKAGRL---MALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILM 270
|
....*..
gi 164423939 367 SVMIGAF 373
Cdd:cd18548 271 SLMMLSM 277
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1107-1268 |
1.91e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1107 PEQPVLRGLNLSIQPGQYVALVGASGCGKST---TIALLERFYDplsggifidGREISSLNVNeyrsfIALVSQEPTLYQ 1183
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTllrIMAGVDKEFE---------GEARPAPGIK-----VGYLPQEPQLDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1184 G-TVRENIILGAnndvtdEQIKFACQEAN-IYDfIMSLPDG-MNTLVGSKGAL--------------------------- 1233
Cdd:PRK11819 84 EkTVRENVEEGV------AEVKAALDRFNeIYA-AYAEPDAdFDALAAEQGELqeiidaadawdldsqleiamdalrcpp 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 164423939 1234 -------LSGGQKQRIAIARALIRDPKILLLDEATSALDSES 1268
Cdd:PRK11819 157 wdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1094-1265 |
2.15e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.72 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1094 IEFRDVHFRYPTRPeqPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIF--------------IDGRE 1159
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1160 ISSlnvneyrsfialvsqEPTLYqgtvreniILGANNDVTDEQIKfacqeANIYDFIMSlpdgmNTLVGSKGALLSGGQK 1239
Cdd:PLN03073 587 LSS---------------NPLLY--------MMRCFPGVPEQKLR-----AHLGSFGVT-----GNLALQPMYTLSGGQK 633
|
170 180
....*....|....*....|....*.
gi 164423939 1240 QRIAIARALIRDPKILLLDEATSALD 1265
Cdd:PLN03073 634 SRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
141-388 |
2.23e-08 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 57.07 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 141 LARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITaDTNLIQEGISEkv 220
Cdd:cd18570 41 LNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISS-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 221 gLTLQALATFIAAFVIGFVSF---WKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEVISSVRNAIAF 297
Cdd:cd18570 118 -TTISLFLDLLMVIISGIILFfynWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 298 GTQDRLARRYDAHLTRAEHFGFRL------KGSIGVMVAGMMTVLYLnyglafWQGSRFLLSGDT---ELRKILTVMMSV 368
Cdd:cd18570 197 NAEEQFLKKIEKKFSKLLKKSFKLgklsnlQSSIKGLISLIGSLLIL------WIGSYLVIKGQLslgQLIAFNALLGYF 270
|
250 260
....*....|....*....|
gi 164423939 369 MIGAFNLGNIAPNLQAFVTA 388
Cdd:cd18570 271 LGPIENLINLQPKIQEAKVA 290
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
433-605 |
2.36e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 55.58 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 433 SRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQIALVSQEPTLFAC 512
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 513 TIYDNIR--HGLIGTKweseseeqqreRIYEAARKANAHDFiTSLPEGYetnvgergflLSGGQKQRIAIARAIVSDPKI 590
Cdd:cd03231 89 SVLENLRfwHADHSDE-----------QVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPL 146
|
170
....*....|....*
gi 164423939 591 LLLDEATSALDTKSE 605
Cdd:cd03231 147 WILDEPTTALDKAGV 161
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
138-313 |
2.43e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 57.11 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 138 TDELARLVLYFVYLAIGEFVTMYI---TTVGFIYSGEHisgKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQE 214
Cdd:cd18543 35 RSALWPLVLLLLALGVAEAVLSFLrryLAGRLSLGVEH---DLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 215 GISeKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMgggsqfiIKFSKQNIAA-------YAEGGSVADEV 287
Cdd:cd18543 112 FLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVA-------RRFRRRYFPAsrraqdqAGDLATVVEES 183
|
170 180
....*....|....*....|....*.
gi 164423939 288 ISSVRNAIAFGTQDRLARRYDAHLTR 313
Cdd:cd18543 184 VTGIRVVKAFGRERRELDRFEAAARR 209
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
422-656 |
2.51e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.50 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPdVVVMEDVSLVIPAGKTTALVGASGSGKS----TIVGLVERFYKPIEGKVYLDDVDISTLNVRWLR 497
Cdd:PRK15093 6 IRNLTIEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSliakAICGVTKDNWRVTADRMRFDDIDLLRLSPRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 498 Q----QIALVSQEPTlfAC-TIYDNIRHGLIGT--------KWESESEEQQRERIYEAARKA--NAHDFITSLPegYEtn 562
Cdd:PRK15093 85 KlvghNVSMIFQEPQ--SClDPSERVGRQLMQNipgwtykgRWWQRFGWRKRRAIELLHRVGikDHKDAMRSFP--YE-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 563 vgergflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTI-TIAHRLSTI-KDAHNIVV 639
Cdd:PRK15093 159 -------LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtRLNQNNNTTIlLISHDLQMLsQWADKINV 231
|
250
....*....|....*..
gi 164423939 640 MAQGRIVEQGTHAELLA 656
Cdd:PRK15093 232 LYCGQTVETAPSKELVT 248
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
435-647 |
4.86e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.11 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 435 PDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYkPI---EGKVYLDDvdiSTLNVRWLR-----------QQI 500
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDG---EVCRFKDIRdsealgiviihQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVsqePTLfacTIYDNI-------RHGLIGtkWEseseeqqreriyEAARKANAHDFITSLPEGYETNVGERGFllsgG 573
Cdd:NF040905 88 ALI---PYL---SIAENIflgneraKRGVID--WN------------ETNRRARELLAKVGLDESPDTLVTDIGV----G 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 574 QKQRIAIARAIVSDPKILLLDEATSAL-DTKSEGVVQAALEVAAEGRTTITIAHRLSTI-KDAHNIVVMAQGRIVE 647
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
442-643 |
5.06e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.56 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGKTTALVGASGSGKSTIVG-LVERfyKP---IEGKVYLD--DVDIStlnvrwLRQQIALVSQEPTLFACtiy 515
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDvLAGR--KTagvITGEILINgrPLDKN------FQRSTGYVEQQDVHSPN--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 516 dnirhgligtkweseseeqqrERIYEAARkanahdFITSLpegyetnvgeRGflLSGGQKQRIAIARAIVSDPKILLLDE 595
Cdd:cd03232 94 ---------------------LTVREALR------FSALL----------RG--LSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 164423939 596 ATSALDTKS-EGVVQAALEVAAEGRTTITIAHRLS--TIKDAHNIVVMAQG 643
Cdd:cd03232 135 PTSGLDSQAaYNIVRFLKKLADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1108-1301 |
9.57e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 53.72 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLnvneyrsfialvsQEPtlYQGTVR 1187
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------------AKP--YCTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1188 ENiiLGANNDVT-DEQIKFAcqeANIYDFIMSLPDG-----MNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEAT 1261
Cdd:PRK13541 77 HN--LGLKLEMTvFENLKFW---SEIYNSAETLYAAihyfkLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 164423939 1262 SALDSESEHVVQAALD-KAAKGRTTIAVAHRLSTIQKADII 1301
Cdd:PRK13541 152 TNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1102-1309 |
9.66e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1102 RYPTRPEQPVL----------RGLNLSIQPGQYVALVGASGCGKSTtiaLLERFY---DPLSGGIFIDGREISSLNVNE- 1167
Cdd:PRK15439 259 RRQQAAGAPVLtvedltgegfRNISLEVRAGEILGLAGVVGAGRTE---LAETLYglrPARGGRIMLNGKEINALSTAQr 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1168 -----------------------YRSFIALVSQEPTLYQGTVRENIILganndvtdEQ------IKF--ACQEANIydfi 1216
Cdd:PRK15439 336 larglvylpedrqssglyldaplAWNVCALTHNRRGFWIKPARENAVL--------ERyrralnIKFnhAEQAART---- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1217 mslpdgmntlvgskgalLSGGQKQRIAIARALIRDPKILLLDEATSALD-SESEHVVQAALDKAAKGRTTIAVAHRLSTI 1295
Cdd:PRK15439 404 -----------------LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDvSARNDIYQLIRSIAAQNVAVLFISSDLEEI 466
|
250
....*....|....*
gi 164423939 1296 -QKADIIYVFDQGRI 1309
Cdd:PRK15439 467 eQMADRVLVMHQGEI 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
422-645 |
1.02e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.37 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKS-TIVGLVERFYKPIEGKVYLDDVDISTLN-VRWLRQQ 499
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVDIRNpAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 500 IALVSQeptlfactiyDNIRHGLIG----------------TKWESESEEQQRERIYEAARKANAHDFITSLPEGYetnv 563
Cdd:TIGR02633 338 IAMVPE----------DRKRHGIVPilgvgknitlsvlksfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR---- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 564 gergflLSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVM 640
Cdd:TIGR02633 404 ------LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDvgAKYE-IYKLINQLAQEGVAIIVVSSELAEVLGlSDRVLVI 476
|
....*
gi 164423939 641 AQGRI 645
Cdd:TIGR02633 477 GEGKL 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
439-653 |
1.23e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVR-WLRQQIALV----SQEPTLFACT 513
Cdd:PRK11288 268 LREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdAIRAGIMLCpedrKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 514 IYDNI-----RH-----GLIGTKWeseseeqqreriyeaaRKANAHDFITSL----PEGyETNVGergfLLSGGQKQRIA 579
Cdd:PRK11288 348 VADNInisarRHhlragCLINNRW----------------EAENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAI 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 580 IARAIVSDPKILLLDEATSALD--TKSEgVVQAALEVAAEGRTTITIAHRL-STIKDAHNIVVMAQGRIVEQGTHAE 653
Cdd:PRK11288 407 LGRWLSEDMKVILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
436-627 |
1.35e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 DVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWlRQQIALVSQE----PTLfa 511
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGHRsginPYL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 512 cTIYDNIRHGLigtkweseSEEQQRERIYEAARKANAHDFItSLPEGyetnvgergfLLSGGQKQRIAIARAIVSDPKIL 591
Cdd:PRK13540 90 -TLRENCLYDI--------HFSPGAVGITELCRLFSLEHLI-DYPCG----------LLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 164423939 592 LLDEATSALDTKSEGVVQAALEV-AAEGRTTITIAHR 627
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEhRAKGGAVLLTSHQ 186
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1118-1305 |
1.40e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1118 SIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGReisslnvneyrsfialVSQEP----TLYQGTVRENIILG 1193
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK----------------ISYKPqyisPDYDGTVEEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1194 ANNDVTD----EQIKFACQEANIYDfiMSLPDgmntlvgskgalLSGGQKQRIAIARALIRDPKILLLDEATSALDSESE 1269
Cdd:COG1245 426 NTDDFGSsyykTEIIKPLGLEKLLD--KNVKD------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180 190
....*....|....*....|....*....|....*....
gi 164423939 1270 HVVQAALDKAA--KGRTTIAVAHRLSTIQK-ADIIYVFD 1305
Cdd:COG1245 492 LAVAKAIRRFAenRGKTAMVVDHDIYLIDYiSDRLMVFE 530
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
819-1027 |
1.59e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 54.52 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 819 LMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGVTLGTIIMV 898
Cdd:cd18782 49 LVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDK--RPVGELSTRISELDTIRGFLTGTALTTLLDV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 899 LTTLIAAcTVALALGWKLALVCIATIPILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTRE----QD 974
Cdd:cd18782 127 LFSVIYI-AVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAElkarWR 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 164423939 975 VLQHYKDSLAKQQHASLISVLKSSLlfaaSNSLMFLAFALGFWYGGTLIAKHE 1027
Cdd:cd18782 206 WQNRYARSLGEGFKLTVLGTTSGSL----SQFLNKLSSLLVLWVGAYLVLRGE 254
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
421-664 |
1.65e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 421 TIRLENIKHIYPSRPDVVvmEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLNVRWLRQQI 500
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSV--GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQEPTLFactiydnirHGLIGTKWeseseeqqreriyEAARKANAHDFITSLPEGYETNVGERGFL---LSGGQKQR 577
Cdd:PRK10522 400 SAVFTDFHLF---------DQLLGPEG-------------KPANPALVEKWLERLKMAHKLELEDGRISnlkLSKGQKKR 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 578 IAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL--EVAAEGRTTITIAHRLSTIKDAHNIVVMAQGRIVEQGTHAELL 655
Cdd:PRK10522 458 LALLLALAEERDILLLDEWAADQDPHFRREFYQVLlpLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDA 537
|
....*....
gi 164423939 656 AKRGAYYKL 664
Cdd:PRK10522 538 ASRDAVART 546
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1065-1309 |
2.47e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.83 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1065 RDLKELFDRKPtvdtwSNEGDLIkqvdgtIEFRDVHFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTI-ALLE 1143
Cdd:TIGR02633 240 REITSLYPHEP-----HEIGDVI------LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVqALFG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1144 RFYDPLSGGIFIDGREISSLN-VNEYRSFIALVSQE-------PTLyqgTVRENIILGANNDVTDE-QIKFACQEANIYD 1214
Cdd:TIGR02633 309 AYPGKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDrkrhgivPIL---GVGKNITLSVLKSFCFKmRIDAAAELQIIGS 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1215 FIMSL------PDgmnTLVGSkgalLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIA 1287
Cdd:TIGR02633 386 AIQRLkvktasPF---LPIGR----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIV 458
|
250 260
....*....|....*....|...
gi 164423939 1288 VAHRLSTIQK-ADIIYVFDQGRI 1309
Cdd:TIGR02633 459 VSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
422-660 |
3.39e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 422 IRLENIKHIYPsrpDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDIStlNVRWLRQ--- 498
Cdd:NF033858 2 ARLEGVSHRYG---KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAvcp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 499 QIALVSQ------EPTLfacTIYDNIR-HG-LIGTKweseseeqqreriyEAARKANAHDFITSlpegyetnVGERGFL- 569
Cdd:NF033858 77 RIAYMPQglgknlYPTL---SVFENLDfFGrLFGQD--------------AAERRRRIDELLRA--------TGLAPFAd 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 -----LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGvvQ-----AALEVAAEGRTTITiahrlST--IKDAHN- 636
Cdd:NF033858 132 rpagkLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR--QfweliDRIRAERPGMSVLV-----ATayMEEAERf 204
|
250 260
....*....|....*....|....*.
gi 164423939 637 --IVVMAQGRIVEQGTHAELLAKRGA 660
Cdd:NF033858 205 dwLVAMDAGRVLATGTPAELLARTGA 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1110-1310 |
3.70e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1110 PVLRGLNLSIQPGQYVALVGASGCGKSTTIALLerfydplSGGIFID-GREISSLNVNeyrsfIALVSQEPTLY-QGTVR 1187
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQDLI-----VARLQQDPPRNvEGTVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1188 ENIILG-------------ANNDV-TDEQIKFACQ----------------EANIYDFIMSL---PDgmntlvgSKGALL 1234
Cdd:PRK11147 85 DFVAEGieeqaeylkryhdISHLVeTDPSEKNLNElaklqeqldhhnlwqlENRINEVLAQLgldPD-------AALSSL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 1235 SGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALdKAAKGrTTIAVAHRLSTIQK-ADIIYVFDQGRIV 1310
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1116-1265 |
3.95e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1116 NLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVnEYRSFIALVSQEPTLYQG-TVRENIILGA 1194
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDI-ATRRRVGYMSQAFSLYGElTVRQNLELHA 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 1195 N-NDVTDEQIKFACQEAnIYDFimSLPDGMNTLVGSkgalLSGGQKQRIAIARALIRDPKILLLDEATSALD 1265
Cdd:NF033858 365 RlFHLPAAEIAARVAEM-LERF--DLADVADALPDS----LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
887-1041 |
4.33e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 53.33 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 887 LSGVTLGTIIMVLTTLIAACtVALALGWKLALVCIATIPILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTV 966
Cdd:cd18568 115 LTRSALTTILDLLMVFIYLG-LMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 967 ASLTREQDVLQHYKDSLAK-------QQHASLISVLKSSLLFAASNSLMflafalgFWYGGTLIAKHEY---DMFTFFIV 1036
Cdd:cd18568 194 KALAAERPIRWRWENKFAKalntrfrGQKLSIVLQLISSLINHLGTIAV-------LWYGAYLVISGQLtigQLVAFNML 266
|
....*
gi 164423939 1037 FSSVI 1041
Cdd:cd18568 267 FGSVI 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1119-1305 |
4.69e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1119 IQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGReisslnvneyrsfialVSQEP----TLYQGTVREniILGA 1194
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK----------------ISYKPqyikPDYDGTVED--LLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1195 NNDVTDEqikfacqeaNIYDFIMSLPDGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQA 1274
Cdd:PRK13409 424 ITDDLGS---------SYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 494
|
170 180 190
....*....|....*....|....*....|....
gi 164423939 1275 ALDKAAKGR--TTIAVAHRLSTIQK-ADIIYVFD 1305
Cdd:PRK13409 495 AIRRIAEEReaTALVVDHDIYMIDYiSDRLMVFE 528
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
433-613 |
5.33e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.73 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 433 SRPDVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVErfykPIEGKVYLDDVDISTL------NVRWLRQQIA- 501
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSllriLAGLAR----PDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 502 ---LVSQEPTLFACTIydnirHGLIGTkweseseeqqreriyEAARKANAHdfitslpegyetnVGERGFL------LSG 572
Cdd:PRK13538 86 kteLTALENLRFYQRL-----HGPGDD---------------EALWEALAQ-------------VGLAGFEdvpvrqLSA 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 164423939 573 GQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALE 613
Cdd:PRK13538 133 GQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLA 173
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
569-656 |
5.64e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 569 LLSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgVVQAALEVAAEGRTTITIAHRLSTI---KDahNIVVMAQG 643
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgAKKE-IYQLINQFKAEGLSIILVSSEMPEVlgmSD--RILVMHEG 471
|
90
....*....|....*...
gi 164423939 644 RI-----VEQGTHAELLA 656
Cdd:PRK10762 472 RIsgeftREQATQEKLMA 489
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
141-259 |
6.50e-07 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 52.47 E-value: 6.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 141 LARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGISEKV 220
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGL 118
|
90 100 110
....*....|....*....|....*....|....*....
gi 164423939 221 GLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVM 259
Cdd:cd18545 119 INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVV 157
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
439-656 |
6.83e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 439 VMEDVSLVIPAGKTTALVGASGSGKSTIV-GLVERFY-KPIEGKVYLDDVDIStlnvRWLRQQIALVSQEPTLFActiYD 516
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLnALAGRIQgNNFTGTILANNRKPT----KQILKRTGFVTQDDILYP---HL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 517 NIRHGLIGTKWESESEEQQRERIYEAARKANAHDFITSLPEGYETNVGERGflLSGGQKQRIAIARAIVSDPKILLLDEA 596
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRG--ISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 597 TSALD-TKSEGVVQAALEVAAEGRTTITIAHRLST--IKDAHNIVVMAQGRIVEQGTHAELLA 656
Cdd:PLN03211 234 TSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1112-1295 |
7.02e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.19 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGReisSLNVNEYRSFIALVSQEPTL---YQGTVRE 1188
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ---PTRQALQKNLVAYVPQSEEVdwsFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1189 NIILGANNDVTDEQIKFACQEANIYDFIMSLpdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSES 1268
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKRDRQIVTAALARV--DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180
....*....|....*....|....*...
gi 164423939 1269 EHVVQAALDK-AAKGRTTIAVAHRLSTI 1295
Cdd:PRK15056 178 EARIISLLRElRDEGKTMLVSTHNLGSV 205
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1110-1292 |
8.28e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1110 PVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSlNVNEYRSFIALVSQEPTLYQG-TVRE 1188
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLlTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1189 NIILGAN-NDVTDEQIKFACQEAniydfIMSLpdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSE 1267
Cdd:TIGR01257 2032 HLYLYARlRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180
....*....|....*....|....*.
gi 164423939 1268 SEHVV-QAALDKAAKGRTTIAVAHRL 1292
Cdd:TIGR01257 2105 ARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
129-310 |
8.48e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 52.11 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 129 AGVTTYDdfTDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITAD 208
Cdd:cd18546 28 SGVRAGD--LGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 209 ----TNLIQEGISEkvglTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMgggsqfiIKFSKQNIAAYAE----- 279
Cdd:cd18546 106 idalSELLQTGLVQ----LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT-------RWFRRRSSRAYRRareri 174
|
170 180 190
....*....|....*....|....*....|...
gi 164423939 280 GGSVAD--EVISSVRNAIAFGTQDRLARRYDAH 310
Cdd:cd18546 175 AAVNADlqETLAGIRVVQAFRRERRNAERFAEL 207
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1108-1323 |
8.72e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1108 EQPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLerfydplsggifidgreisslnVNEYrsfialvsqEPTlyQGTVR 1187
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL----------------------VGEL---------EPD--SGTVK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1188 --ENIILG-ANNDVTDEqikFAcQEANIYDFI---MSLPDGMNTLVGSKGALL-------------SGGQKQRIAIARAL 1248
Cdd:PRK15064 378 wsENANIGyYAQDHAYD---FE-NDLTLFDWMsqwRQEGDDEQAVRGTLGRLLfsqddikksvkvlSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1249 IRDPKILLLDEATSALDSESEHVVQAALDKaAKGrTTIAVAH------RLSTiqkaDIIYVFDQGRIVEQGTHSELMKKN 1322
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESLNMALEK-YEG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQ 527
|
.
gi 164423939 1323 G 1323
Cdd:PRK15064 528 G 528
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1111-1265 |
1.18e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.27 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIfidgreisslnVNEYRSFIALVSQ----EPTL----- 1181
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQklylDTTLpltvn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1182 ----YQGTVRENIILGANNDVtdeqikfacQEANIYDFIMSLpdgmntlvgskgalLSGGQKQRIAIARALIRDPKILLL 1257
Cdd:PRK09544 88 rflrLRPGTKKEDILPALKRV---------QAGHLIDAPMQK--------------LSGGETQRVLLARALLNRPQLLVL 144
|
....*...
gi 164423939 1258 DEATSALD 1265
Cdd:PRK09544 145 DEPTQGVD 152
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1110-1319 |
1.73e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1110 PVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE-YRSFIALVSQEPT---LYQG- 1184
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRKrdgLVLGm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1185 TVRENIILGANNDVTDE--QIKFACQEANIYDFIMSL----PdGMNTLVGskgaLLSGGQKQRIAIARALIRDPKILLLD 1258
Cdd:PRK10762 346 SVKENMSLTALRYFSRAggSLKHADEQQAVSDFIRLFniktP-SMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 1259 EATSALDSESEHVVQAALDK-AAKGRTTIAVAHRL-STIQKADIIYVFDQGRI-----VEQGTHSELM 1319
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQfKAEGLSIILVSSEMpEVLGMSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1065-1320 |
1.88e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1065 RDLKELF-DRKPTVdtwsneGDLIkqvdgtIEFRDVHFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKsTTIA--L 1141
Cdd:NF040905 240 RDLEDRYpERTPKI------GEVV------FEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGR-TELAmsV 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1142 LERFYDP-LSGGIFIDGREISSLNVNE-YRSFIALVSQEPTLY----QGTVRENIILG-----ANNDVTDEQIKFacQEA 1210
Cdd:NF040905 307 FGRSYGRnISGTVFKDGKEVDVSTVSDaIDAGLAYVTEDRKGYglnlIDDIKRNITLAnlgkvSRRGVIDENEEI--KVA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1211 NIYDfimslpDGMNTL---VGSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTI 1286
Cdd:NF040905 385 EEYR------KKMNIKtpsVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINElAAEGKGVI 458
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 164423939 1287 AVAHRL-STIQKADIIYVFDQGRIV-----EQGTHSELMK 1320
Cdd:NF040905 459 VISSELpELLGMCDRIYVMNEGRITgelprEEASQERIMR 498
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
430-604 |
1.90e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.24 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 430 IYPsrPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDvdisTLNVRWLRQQIALvsqEPTL 509
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP----GIKVGYLPQEPQL---DPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 510 facTIYDNIRHGLIGTKweseSEEQQRERIYE------------AARKA---------NAHDFITSL---------PEGy 559
Cdd:TIGR03719 84 ---TVRENVEEGVAEIK----DALDRFNEISAkyaepdadfdklAAEQAelqeiidaaDAWDLDSQLeiamdalrcPPW- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 164423939 560 ETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKS 604
Cdd:TIGR03719 156 DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1115-1314 |
2.08e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.26 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1115 LNLSIQPGQYVALVGASGCGKSTT----IALLERfYDPLSGGIFIDGREISSLN---VNEYRS-FIALVSQEP-TLYQGT 1185
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTafalMGLLAA-NGRIGGSATFNGREILNLPekeLNKLRAeQISMIFQDPmTSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1186 VR------ENIILG---ANNDVTDEQIKF--------ACQEANIY--DFimslpdgmntlvgskgallSGGQKQRIAIAR 1246
Cdd:PRK09473 114 MRvgeqlmEVLMLHkgmSKAEAFEESVRMldavkmpeARKRMKMYphEF-------------------SGGMRQRVMIAM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1247 ALIRDPKILLLDEATSALDSesehVVQAALD------KAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGRIVEQGT 1314
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDV----TVQAQIMtllnelKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1111-1313 |
2.11e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1111 VLRGLNLSIQPGQYVALVGASGCGKST---TIAL-LERFYDPLSGGIFIDG---REIsslnVNEYRSFIALVSQE----P 1179
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllkTIASnTDGFHIGVEGVITYDGitpEEI----KKHYRGDVVYNAETdvhfP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1180 TLyqgTVRENIILGAN--------NDVTDEQikFACQEANIYDFIMSLPDGMNTLVGS---KGalLSGGQKQRIAIARAL 1248
Cdd:TIGR00956 152 HL---TVGETLDFAARcktpqnrpDGVSREE--YAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1249 IRDPKILLLDEATSALDSESehvvqaALD--KAAKGRTTIAVAHRLSTI----QKA----DIIYVFDQGRIVEQG 1313
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSAT------ALEfiRALKTSANILDTTPLVAIyqcsQDAyelfDKVIVLYEGYQIYFG 293
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
112-336 |
2.18e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 50.97 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 112 LMTVIFGNLQGTFQNYFAGVTTYDDFTDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIG 191
Cdd:cd18580 9 LLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 192 FFDKLGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAF-VIGFVSFWkltlillstVVALTLVMGGGSQFIIKF- 269
Cdd:cd18580 89 FFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLiVIAIVSPY---------FLIVLPPLLVVYYLLQRYy 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 270 ---SKQ--------------NIAAYAEGgsvadevISSVRnaiAFGTQDRLARRYDAHL---TRAEH--------FGFRL 321
Cdd:cd18580 160 lrtSRQlrrlesesrsplysHFSETLSG-------LSTIR---AFGWQERFIEENLRLLdasQRAFYlllavqrwLGLRL 229
|
250
....*....|....*
gi 164423939 322 kgsiGVMVAGMMTVL 336
Cdd:cd18580 230 ----DLLGALLALVV 240
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1120-1303 |
2.66e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.44 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1120 QPGQYVALVGASGCGKSTTIALLE--------RFYDPlsggifIDGREIsslnVNEYRS------FIAL----------- 1174
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDP------PDWDEI----LDEFRGselqnyFTKLlegdvkvivkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1175 --VSQEPTLYQGTVRENIilgannDVTDEQIKFacqeaniyDFIMSLPDgMNTLVGSKGALLSGGQKQRIAIARALIRDP 1252
Cdd:cd03236 94 qyVDLIPKAVKGKVGELL------KKKDERGKL--------DELVDQLE-LRHVLDRNIDQLSGGELQRVAIAAALARDA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1253 KILLLDEATSALDSESEHVVQAALDKAAK-GRTTIAVAHRLSTIQK-ADIIYV 1303
Cdd:cd03236 159 DFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLAVLDYlSDYIHC 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
570-601 |
3.52e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 3.52e-06
10 20 30
....*....|....*....|....*....|..
gi 164423939 570 LSGGQKQRIAIARAIVSDPKILLLDEATSALD 601
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1093-1320 |
3.59e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1093 TIEFRDVHFRYPTRPEQPVLRgLNLSIQPGQYVALVGASGCGKS-TTIALLERFYDP---LSGGIFIDGREISSLNVNEY 1168
Cdd:PRK11022 5 NVDKLSVHFGDESAPFRAVDR-ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1169 RSFI----ALVSQEPTLYQG---TVRENIIlganndvtdEQIKF------ACQEANIYDFI--MSLPDGMNTLvGSKGAL 1233
Cdd:PRK11022 84 RNLVgaevAMIFQDPMTSLNpcyTVGFQIM---------EAIKVhqggnkKTRRQRAIDLLnqVGIPDPASRL-DVYPHQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1234 LSGGQKQRIAIARALIRDPKILLLDEATSALD-SESEHVVQAALD-KAAKGRTTIAVAHRLSTI-QKADIIYVFDQGRIV 1310
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVV 233
|
250
....*....|
gi 164423939 1311 EQGTHSELMK 1320
Cdd:PRK11022 234 ETGKAHDIFR 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
442-645 |
3.96e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGKTTALVGASGSGKS----TIVGLverfYKPIEGKVYLDDVDISTLNVR--------WL---RQQIALVSQE 506
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTelaeTLYGL----RPARGGRIMLNGKEINALSTAqrlarglvYLpedRQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 P-TLFACTIYDNIRHGLIGTKweseseeqqreriYEAARKANAHDFITSLPEGYETNVGErgflLSGGQKQRIAIARAIV 585
Cdd:PRK15439 357 PlAWNVCALTHNRRGFWIKPA-------------RENAVLERYRRALNIKFNHAEQAART----LSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 586 SDPKILLLDEATSALDTKSEG-VVQAALEVAAEGRTTITIAHRLSTI-KDAHNIVVMAQGRI 645
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
798-1024 |
4.57e-06 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 50.09 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 798 IVNEEIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRDenSAGALTSFL 877
Cdd:cd18548 25 IIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKF--GTSSLITRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 878 STETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATIPILLGCGFYRFWMIAHYQRRAKSAYAGSASYAS 957
Cdd:cd18548 103 TNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVR 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 958 EAITAMRTVASLTREQDVLQHYK---DSLAKQQhaslisvLKSSLLFAASNSLMFLAFALG----FWYGGTLIA 1024
Cdd:cd18548 183 ENLTGIRVIRAFNREDYEEERFDkanDDLTDTS-------LKAGRLMALLNPLMMLIMNLAivaiLWFGGHLIN 249
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1234-1305 |
4.78e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 4.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1234 LSGGQKQRIAIARALIRDPKILLLDEATSALDSESE-HVVQAALDKAAKG-RTTIAVAHRLSTIQK-ADIIYVFD 1305
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlNAARAIRRLSEEGkKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
441-689 |
5.62e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.09 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 441 EDVSLVIPAGKTTALVGASGSGKSTIV----GLVerfyKPIEGKVYLDDVDISTLNVRWLRQqIALV----SQ----EP- 507
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIkmltGIL----VPTSGEVRVLGYVPFKRRKEFARR-IGVVfgqrSQlwwdLPa 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 508 ----TLFACtIYDnirhgligtkweseseeqqrerIYEAARKANAHDFITSLpegyetNVGErgFL------LSGGQKQR 577
Cdd:COG4586 114 idsfRLLKA-IYR----------------------IPDAEYKKRLDELVELL------DLGE--LLdtpvrqLSLGQRMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 578 IAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-EVAAEGRTTI--TiAHRLSTIKD-AHNIVVMAQGRIVEQGTHAE 653
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLkEYNRERGTTIllT-SHDMDDIEAlCDRVIVIDHGRIIYDGSLEE 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 164423939 654 LLaKRGAYYKLVTAQAIAAVNEMTAEEEAALDQQEE 689
Cdd:COG4586 242 LK-ERFGPYKTIVLELAEPVPPLELPRGGEVIEREG 276
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1119-1303 |
5.75e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1119 IQPGQYVALVGASGCGKSTTIALLE--------RFYDPLSGGIFID---GREI----SSLNVNEYRSF--IALVSQEPTL 1181
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSgelipnlgDYEEEPSWDEVLKrfrGTELqnyfKKLYNGEIKVVhkPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1182 YQGTVREniiLGANNDvtdeqikfacqEANIYDFIMSLPdGMNTLVGSKGALLSGGQKQRIAIARALIRDPKILLLDEAT 1261
Cdd:PRK13409 176 FKGKVRE---LLKKVD-----------ERGKLDEVVERL-GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 164423939 1262 SALDSESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYV 1303
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHI 283
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1118-1265 |
5.75e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1118 SIQPGQYVALVGASGCGKSTTIALLErfydplsGGIFIDGREISSLNVNEyrsfIALVSQE-PTLYQGTVrENIILGann 1196
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSYTFPGNWQ----LAWVNQEtPALPQPAL-EYVIDG--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1197 DVTDEQIKFACQEANIYD---FIMSLPDGMNTL----VGSKGALL------------------SGGQKQRIAIARALIRD 1251
Cdd:PRK10636 88 DREYRQLEAQLHDANERNdghAIATIHGKLDAIdawtIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQALICR 167
|
170
....*....|....
gi 164423939 1252 PKILLLDEATSALD 1265
Cdd:PRK10636 168 SDLLLLDEPTNHLD 181
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1120-1304 |
6.11e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1120 QPGQYVALVGASGCGKSTTIALLerfydplSG------GIFidGREISSLNVNEYRS-------FIALVSQE-------- 1178
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-------SGelkpnlGDY--DEEPSWDEVLKRFRgtelqdyFKKLANGEikvahkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1179 -----PTLYQGTVREniiLGANNDvtdeqikfacqEANIYDFIMSLPdGMNTLVGSKGALLSGGQKQRIAIARALIRDPK 1253
Cdd:COG1245 168 yvdliPKVFKGTVRE---LLEKVD-----------ERGKLDELAEKL-GLENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 164423939 1254 ILLLDEATSALD-SESEHVVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVF 1304
Cdd:COG1245 233 FYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1109-1325 |
6.23e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1109 QPVLRGLNLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE-YRSFIALVSQEptlyqgtvR 1187
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEaINHGFALVTEE--------R 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1188 ENIILGANNDVTdeqikFACQEANIYDFIMSLP---------------DGMN-------TLVGSkgalLSGGQKQRIAIA 1245
Cdd:PRK10982 333 RSTGIYAYLDIG-----FNSLISNIRNYKNKVGlldnsrmksdtqwviDSMRvktpghrTQIGS----LSGGNQQKVIIG 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1246 RALIRDPKILLLDEATSALDSESEH-VVQAALDKAAKGRTTIAVAHRLSTIQK-ADIIYVFDQGR---IVE--QGTHSEL 1318
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFeIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLvagIVDtkTTTQNEI 483
|
....*..
gi 164423939 1319 MKKNGRY 1325
Cdd:PRK10982 484 LRLASLH 490
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
138-348 |
6.65e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 49.40 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 138 TDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGIS 217
Cdd:cd18550 35 LGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 218 EKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFIIKFSKQNIAAYAEGGSVADEV--ISSVRNAI 295
Cdd:cd18550 115 GTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVK 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 296 AFGTQDRLARRYDAH------LTRAEHFGFRLKGSIGVMVAGMMTVL-YLNYGLAFWQGS 348
Cdd:cd18550 195 LFGREDDEAARFARRsrelrdLGVRQALAGRWFFAALGLFTAIGPALvYWVGGLLVIGGG 254
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
423-645 |
7.35e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 423 RLENIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYK-PIEGKVYLDDVDISTLNVR-WLRQQI 500
Cdd:PRK13549 261 EVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQqAIAQGI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 501 ALVSQeptlfactiyDNIRHGLI-------GTKWESESEEQQRERIYEAARKANAHDFI------TSLPEGYETNvgerg 567
Cdd:PRK13549 341 AMVPE----------DRKRDGIVpvmgvgkNITLAALDRFTGGSRIDDAAELKTILESIqrlkvkTASPELAIAR----- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 568 flLSGGQKQRIAIARAIVSDPKILLLDEATSALDtksegvVQAALEV-------AAEGRTTITIAHRLSTIKD-AHNIVV 639
Cdd:PRK13549 406 --LSGGNQQKAVLAKCLLLNPKILILDEPTRGID------VGAKYEIyklinqlVQQGVAIIVISSELPEVLGlSDRVLV 477
|
....*.
gi 164423939 640 MAQGRI 645
Cdd:PRK13549 478 MHEGKL 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
558-655 |
7.40e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 558 GYETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgVVQAALEVAAEGRTTITIAH---RLSTIK 632
Cdd:PRK10982 384 GHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFE-IYQLIAELAKKDKGIIIISSempELLGIT 458
|
90 100
....*....|....*....|....*...
gi 164423939 633 DahNIVVMAQGR---IVE--QGTHAELL 655
Cdd:PRK10982 459 D--RILVMSNGLvagIVDtkTTTQNEIL 484
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
767-1015 |
9.53e-06 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 49.03 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 767 LVGIFFSAICGAGNPtqaVFFAKLISSLSRPIvneeirASIKSDASFWCLMY-LMLALVQCLAfSVQGWLFAKCSERLIH 845
Cdd:cd18582 2 LLLLVLAKLLNVAVP---FLLKYAVDALSAPA------SALLAVPLLLLLAYgLARILSSLFN-ELRDALFARVSQRAVR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 846 RVRDMAFRSFLRQDVEFFDrdENSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTV-ALALGWKLALVCIATI 924
Cdd:cd18582 72 RLALRVFRHLHSLSLRFHL--SRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGIlWYLYGWSYALITLVTV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 925 pillgcGFYRFWMI------AHYQRRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASlisvLKSS 998
Cdd:cd18582 150 ------ALYVAFTIkvtewrTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAA----VKSQ 219
|
250
....*....|....*..
gi 164423939 999 LLFAASNSLMFLAFALG 1015
Cdd:cd18582 220 TSLALLNIGQALIISLG 236
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
784-1024 |
1.36e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 48.63 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 784 AVFFAKLISSLSRPIVNEEIRASIKSDASFWCLMYLMLALVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFF 863
Cdd:cd18543 11 ATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 864 DRdeNSAGALTSFLSTETTHVAGLSGVtLGTIIMVLTTLIAACTVALALGWKLALVCIATIPILlgcGFYRFWMIAHYQ- 942
Cdd:cd18543 91 DR--WQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPL---VLVARRFRRRYFp 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 943 --RRAKSAYAGSASYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGG 1020
Cdd:cd18543 165 asRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGG 244
|
....
gi 164423939 1021 TLIA 1024
Cdd:cd18543 245 WLVA 248
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
571-685 |
1.43e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 571 SGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVV-QAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQ 648
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIAD 225
|
90 100 110
....*....|....*....|....*....|....*...
gi 164423939 649 GTHAELLAKRGAYYKLVTAQAIAAVNEMT-AEEEAALD 685
Cdd:NF000106 226 GKVDELKTKVGGRTLQIRPAHAAELDRMVgAIAQAGLD 263
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
570-656 |
1.57e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALE-VAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVE 647
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAsLHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAE 215
|
....*....
gi 164423939 648 QGTHAELLA 656
Cdd:PRK10938 216 TGEREEILQ 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1112-1313 |
2.18e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTiaLLERFYDPLSGgifidgREISSLNVNEYRSFIAlVSQEPTLyqgtvrenII 1191
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKA------RLISFLPKFSRNKLIF-IDQLQFL--------ID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1192 LGANndvtdeqikfacqeaniYdfiMSLPDGMNTLvgskgallSGGQKQRIAIARALIRDPK--ILLLDEATSALD-SES 1268
Cdd:cd03238 74 VGLG-----------------Y---LTLGQKLSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHqQDI 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 164423939 1269 EHVVQAALDKAAKGRTTIAVAHRLSTIQKADIIYVF------DQGRIVEQG 1313
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1065-1265 |
3.16e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1065 RDLKELFDRKPtvdtwSNEGDLIKQVdgtiefRDVHFRYPTRPEQPVLRGLNLSIQPGQYVALVGASGCGKSTTI-ALLE 1143
Cdd:PRK13549 242 RELTALYPREP-----HTIGEVILEV------RNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVqCLFG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1144 RFYDPLSGGIFIDGREISSLNVNE-YRSFIALVSQE-------PTLyqgTVRENIILGANNDVTD-EQIKFACQEANIYD 1214
Cdd:PRK13549 311 AYPGRWEGEIFIDGKPVKIRNPQQaIAQGIAMVPEDrkrdgivPVM---GVGKNITLAALDRFTGgSRIDDAAELKTILE 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1215 FIMSL----PDGMNTlVGSkgalLSGGQKQRIAIARALIRDPKILLLDEATSALD 1265
Cdd:PRK13549 388 SIQRLkvktASPELA-IAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
794-1023 |
3.49e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 47.15 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 794 LSRPIVNEEIRASIKSDASFWCLMYLMLA-LVQCLAFSVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGA 872
Cdd:cd18778 21 LIRELVDLVTIGSKSLGLLLGLALLLLGAyLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDD--RQTGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 873 LTSFLSTETTHV-AGLSGVTLGTIIMVLTTLIAACtVALALGWKLALVCIATIPILLGCGFyRFWMIAH-YQRRAKSAYA 950
Cdd:cd18778 99 LMSRVINDVANVeRLIADGIPQGITNVLTLVGVAI-ILFSINPKLALLTLIPIPFLALGAW-LYSKKVRpRYRKVREALG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 951 GSASYASEAITAMRTVASLTREQDVLQHYKDsLAKQQHASLISVLKSSLLFaaSNSLMFLAfALGF----WYGGTLI 1023
Cdd:cd18778 177 ELNALLQDNLSGIREIQAFGREEEEAKRFEA-LSRRYRKAQLRAMKLWAIF--HPLMEFLT-SLGTvlvlGFGGRLV 249
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
430-604 |
3.72e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 430 IYPsrPDVVVMEDVSLVIPAGKTTALVGASGSGKST---IVGLVErfyKPIEGKVYLDDvdisTLNVRWLrqqialvSQE 506
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTllrIMAGVD---KEFEGEARPAP----GIKVGYL-------PQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 PTL-FACTIYDNIRHGLIGTKweseSEEQQRERIYE------------AARKA---------NAHDfITS---------- 554
Cdd:PRK11819 79 PQLdPEKTVRENVEEGVAEVK----AALDRFNEIYAayaepdadfdalAAEQGelqeiidaaDAWD-LDSqleiamdalr 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 164423939 555 LPEGyETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKS 604
Cdd:PRK11819 154 CPPW-DAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1228-1323 |
4.16e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.42 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1228 GSKGALLSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKGRTTIAVAHRL--STIQKADIIYVFD 1305
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVID 218
|
90
....*....|....*...
gi 164423939 1306 QGRIVEQGTHSELMKKNG 1323
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
816-1027 |
5.95e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 46.42 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 816 LMYLMLALVQCLAF-----SVQGWLFAKCSERLIHRVRDMAFRSFLRQDVEFFDRdeNSAGALTSFLSTETTHVAGLSGV 890
Cdd:cd18566 41 LQVLVIGVVIAILLesllrLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFER--EPSGAHLERLNSLEQIREFLTGQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 891 TLgTIIMVLTTLIAACTVALALGWKLALVCIATIPILLGCGfyrfWMIA-HYQRRAKSAYAGSA---SYASEAITAMRTV 966
Cdd:cd18566 119 AL-LALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVA----ILLGpILRRALKERSRADErrqNFLIETLTGIHTI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 967 ASLTREQDVLQHYKDSLAKQQHASLISVLKSSLLFAASNSLMFLAFALGFWYGGTLIAKHE 1027
Cdd:cd18566 194 KAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGD 254
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
436-660 |
5.98e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 436 DVVVMEDVSLVIPAGKTTALVGASGSGKST----IVGLVErfykPIEGKVYL-----DDVDISTlnvrwlRQQIALVSQE 506
Cdd:NF033858 278 DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTtmkmLTGLLP----ASEGEAWLfgqpvDAGDIAT------RRRVGYMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 PTLFA-CTIYDNIR-H----GLIGTKWESEseeqqrerIYEAARKANAHDFITSLPEGyetnvgergflLSGGQKQRIAI 580
Cdd:NF033858 348 FSLYGeLTVRQNLElHarlfHLPAAEIAAR--------VAEMLERFDLADVADALPDS-----------LPLGIRQRLSL 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 581 ARAIVSDPKILLLDEATSaldtkseGVVQAA--------LEVAAEGRTTITIahrlSTikdaH--N-------IVVMAQG 643
Cdd:NF033858 409 AVAVIHKPELLILDEPTS-------GVDPVArdmfwrllIELSREDGVTIFI----ST----HfmNeaercdrISLMHAG 473
|
250
....*....|....*..
gi 164423939 644 RIVEQGTHAELLAKRGA 660
Cdd:NF033858 474 RVLASDTPAALVAARGA 490
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
417-662 |
7.02e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.70 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 417 NVVGTIRLENIKHIYP--SRPDVvvmEDVSLVIPAGKTTALVGASGSGKSTIvglverfYKPIEGKVYLDDVDiSTLNVR 494
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSgtSSPAV---DRLCVGVRPGECFGLLGVNGAGKTTT-------FKMLTGDTTVTSGD-ATVAGK 2001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 495 WLRQQIALVSQepTLFACTIYDNIRHGLIGTKWESESEEQQRERIYEAARKANAHdfITSLpeGYETNVGERGFLLSGGQ 574
Cdd:TIGR01257 2002 SILTNISDVHQ--NMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWS--IQSL--GLSLYADRLAGTYSGGN 2075
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALDTKSEGVV-QAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHA 652
Cdd:TIGR01257 2076 KRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQ 2155
|
250
....*....|
gi 164423939 653 ELLAKRGAYY 662
Cdd:TIGR01257 2156 HLKSKFGDGY 2165
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
570-640 |
7.09e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 7.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164423939 570 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSE-GVVQAALEVAAEGRTTITIAHRLsTIKD--AHNIVVM 640
Cdd:COG1245 213 LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRlNVARLIRELAEEGKYVLVVEHDL-AILDylADYVHIL 285
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
432-646 |
8.66e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 432 PSRPDVVVMEDVSLVIPAGKTTALVGASGSGKS----TIVGlveRFY-KPIEGKVYLDDVDISTLNV-RWLRQQIALVSQ 505
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTelamSVFG---RSYgRNISGTVFKDGKEVDVSTVsDAIDAGLAYVTE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 506 EPTLFACTIYDNIRH-------GLIGTKWEseseeqqrerIYEAARKANAHDFITSL----PeGYETNVGErgflLSGGQ 574
Cdd:NF040905 345 DRKGYGLNLIDDIKRnitlanlGKVSRRGV----------IDENEEIKVAEEYRKKMniktP-SVFQKVGN----LSGGN 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 575 KQRIAIARAIVSDPKILLLDEATSALD--TKSE--GVVQaalEVAAEGRTTITIAHRLST---IKDahNIVVMAQGRIV 646
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGIDvgAKYEiyTIIN---ELAAEGKGVIVISSELPEllgMCD--RIYVMNEGRIT 483
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
382-660 |
1.09e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 382 LQAFVTALGA-AAKIYNTIDRESPID--------SSS--------EEGGKLENVVgtIRLENIKHIYPSRPdvvVMEDVS 444
Cdd:PRK15064 265 LQSFVSRFSAnASKAKQATSRAKQIDkikleevkPSSrqnpfirfEQDKKLHRNA--LEVENLTKGFDNGP---LFKNLN 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 445 LVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVylddvdistlnvRWLRQ-QIALVSQEPTL-FAC--TIYDNIrh 520
Cdd:PRK15064 340 LLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSENaNIGYYAQDHAYdFENdlTLFDWM-- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 521 gligTKWeseseeqqreriyeaarKANAHDfitslpegyETNVgeRGFL----------------LSGGQKQRIAIARAI 584
Cdd:PRK15064 406 ----SQW-----------------RQEGDD---------EQAV--RGTLgrllfsqddikksvkvLSGGEKGRMLFGKLM 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 585 VSDPKILLLDEATSALDTKSEGVVQAALEVaAEGrTTITIAH------RLSTikdaHNIVVMAQGRIVEQGTHAELLAKR 658
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESLNMALEK-YEG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQ 527
|
..
gi 164423939 659 GA 660
Cdd:PRK15064 528 GI 529
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
431-609 |
1.18e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 431 YPSRPdvVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYlddvdistlnvRWLRQQIALVSQE---- 506
Cdd:PLN03073 518 YPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVFSQHhvdg 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 507 ------PTLFACTIYDNIrhgligtkweseseeqqreriyeAARKANAHdfITSLpeGYETNVG-ERGFLLSGGQKQRIA 579
Cdd:PLN03073 585 ldlssnPLLYMMRCFPGV-----------------------PEQKLRAH--LGSF--GVTGNLAlQPMYTLSGGQKSRVA 637
|
170 180 190
....*....|....*....|....*....|.
gi 164423939 580 IARAIVSDPKILLLDEATSALDTKS-EGVVQ 609
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
914-1023 |
1.75e-04 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 45.18 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 914 WKLALVCIATIPILLgcgFYRFWMIAHYQRRAKSAYAGSA---SYASEAITAMRTVASLTREQDVLQHYKDSLAKQQHAS 990
Cdd:cd18588 141 PTLTLIVLASLPLYA---LLSLLVTPILRRRLEEKFQRGAenqSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKAS 217
|
90 100 110
....*....|....*....|....*....|...
gi 164423939 991 LISVLKSSLLFAASNSLMFLAFALGFWYGGTLI 1023
Cdd:cd18588 218 FKTANLSNLASQIVQLIQKLTTLAILWFGAYLV 250
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1235-1290 |
1.77e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 164423939 1235 SGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAKgrTTIAVAH 1290
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSH 399
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1116-1317 |
1.82e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1116 NLSIQPGQYVALVGASGCGKSTTIALLERFYDPLSGGIFIDGREISSLNVNE-YRSFIALV----SQEPTLYQGTVRENI 1190
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGIMLCpedrKAEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1191 ILGANNdvtdEQIKFAC-----QEANIYD-FIMSL----PDGmNTLVGSkgalLSGGQKQRIAIARALIRDPKILLLDEA 1260
Cdd:PRK11288 353 NISARR----HHLRAGClinnrWEAENADrFIRSLniktPSR-EQLIMN----LSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 164423939 1261 TSALDSESEHVVQAAL-DKAAKGRTTIAVAHRL-STIQKADIIYVFDQGRIVEQGTHSE 1317
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
570-640 |
2.13e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 2.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423939 570 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAEGRTTITIAHRLsTIKD--AHNIVVM 640
Cdd:PRK13409 213 LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA 284
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
570-629 |
2.26e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 44.66 E-value: 2.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 570 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSE-GVVQAALEVAAEGRTTITIAHRLS 629
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1112-1314 |
2.30e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1112 LRGLNLSIQPGQYVALVGASGCGKSTTI-----ALLERF----------YDPLSGGIFID----------GREISSlNVN 1166
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRlhlkkeqpgnHDRIEGLEHIDkvividqspiGRTPRS-NPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1167 EYRSFIALVSQ------------EPTL---YQGtvrENI--ILgannDVT-DEQIKFACQEANIYDFIMSLPD-GMNTL- 1226
Cdd:cd03271 90 TYTGVFDEIRElfcevckgkrynRETLevrYKG---KSIadVL----DMTvEEALEFFENIPKIARKLQTLCDvGLGYIk 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1227 VGSKGALLSGGQKQRIAIARALIR---DPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQKADiiY 1302
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCAD--W 240
|
250 260
....*....|....*....|
gi 164423939 1303 VFD--------QGRIVEQGT 1314
Cdd:cd03271 241 IIDlgpeggdgGGQVVASGT 260
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
442-647 |
3.23e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.78 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN-VRWLRQQIALVSQ---EPTLFA------ 511
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFPnfsiaq 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 512 -CTIYDNIRHGLIGTKWESESEEqqreriyEAARKANAHDFITSLP-EGYETNVGErgflLSGGQKQRIAIARAIVSDPK 589
Cdd:PRK09700 361 nMAISRSLKDGGYKGAMGLFHEV-------DEQRTAENQRELLALKcHSVNQNITE----LSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 590 ILLLDEATSALD--TKSEgVVQAALEVAAEGRTTITIAHRLSTIKDA-HNIVVMAQGRIVE 647
Cdd:PRK09700 430 VIIFDEPTRGIDvgAKAE-IYKVMRQLADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1234-1318 |
4.82e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1234 LSGGQKQRIAIARALIRD---PKILLLDEATSALDSES----EHVVQAALDkaaKGRTTIAVAHRLSTIQKADiiYVFD- 1305
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDikklLEVLQRLVD---KGNTVVVIEHNLDVIKTAD--YIIDl 904
|
90 100
....*....|....*....|
gi 164423939 1306 -------QGRIVEQGTHSEL 1318
Cdd:TIGR00630 905 gpeggdgGGTVVASGTPEEV 924
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
442-634 |
5.32e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.55 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVYLDDVDISTLN---VRWLRQQIALVSQeptlfaCTIYDNI 518
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGLKLE------MTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 519 RHgligtkWESESEEQQRerIYEAARKANAHDFITslpegyetnvgERGFLLSGGQKQRIAIARAIVSDPKILLLDEATS 598
Cdd:PRK13541 92 KF------WSEIYNSAET--LYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 164423939 599 ALDTKSEGVVQAALEVAA-EGRTTITIAHRLSTIKDA 634
Cdd:PRK13541 153 NLSKENRDLLNNLIVMKAnSGGIVLLSSHLESSIKSA 189
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
570-629 |
5.69e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 5.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 570 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALEVAAE-GRTTITIAHRLS 629
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPS 1080
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
570-654 |
6.82e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 570 LSGGQKQRIAIARAI---VSDPKILLLDEATSALDTKSegvVQAALEV----AAEGRTTITIAHRLSTIKDAHNIVVM-- 640
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDD---IKKLLEVlqrlVDKGNTVVVIEHNLDVIKTADYIIDLgp 906
|
90
....*....|....*...
gi 164423939 641 ----AQGRIVEQGTHAEL 654
Cdd:TIGR00630 907 eggdGGGTVVASGTPEEV 924
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
442-650 |
7.91e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.99 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGKTTALVGASGSGKSTIVGlvERFYKPIEGKVYLDDVDISTLNVRWLRQQI---ALVSQEP---TLFACT-- 513
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLIN--DTLYPALARRLHLKKEQPGNHDRIEGLEHIdkvIVIDQSPigrTPRSNPat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 514 ---IYDNIR-------HG-------LIGTKWESESEEQQRERIYEAarkanaHDFITSLPE-------------GYETnV 563
Cdd:cd03271 91 ytgVFDEIRelfcevcKGkrynretLEVRYKGKSIADVLDMTVEEA------LEFFENIPKiarklqtlcdvglGYIK-L 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 564 GERGFLLSGGQKQRIAIARAI---VSDPKILLLDEATSALDTKSegvVQAALEV----AAEGRTTITIAHRLSTIKDAHN 636
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHD---VKKLLEVlqrlVDKGNTVVVIEHNLDVIKCADW 240
|
250 260
....*....|....*....|
gi 164423939 637 IVVM------AQGRIVEQGT 650
Cdd:cd03271 241 IIDLgpeggdGGGQVVASGT 260
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
570-633 |
1.06e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 1.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164423939 570 LSGGQkQRIA-IARAIVSDPKILLLDEATSALDTKSEGVVQAALEV-AAEGRTTI------------TIAHRLSTIKD 633
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLlfvshhaedapaCITHRLEFVPD 478
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
426-658 |
1.10e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 426 NIKHIYPSRPDVVVMEDVSLVIPAGKTTALVGASGSGKSTIVGLV--ERFYKPIEGKVYLDDVDISTLNVR-WLRQQIAL 502
Cdd:PRK09580 3 SIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEdRAGEGIFM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 503 VSQEPT--------LFACTIYDNIRhgligtKWESEseeqqreriyEAARKANAHDFIT------SLPEGYETNVGERGF 568
Cdd:PRK09580 83 AFQYPVeipgvsnqFFLQTALNAVR------SYRGQ----------EPLDRFDFQDLMEekiallKMPEDLLTRSVNVGF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 569 llSGGQKQRIAIARAIVSDPKILLLDEATSALDTKsegvvqaALEVAAEG--------RTTITIAHR---LSTIKDAHnI 637
Cdd:PRK09580 147 --SGGEKKRNDILQMAVLEPELCILDESDSGLDID-------ALKIVADGvnslrdgkRSFIIVTHYqriLDYIKPDY-V 216
|
250 260
....*....|....*....|.
gi 164423939 638 VVMAQGRIVEQGTHAelLAKR 658
Cdd:PRK09580 217 HVLYQGRIVKSGDFT--LVKQ 235
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
187-310 |
1.17e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 42.52 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 187 RQNIGFFDKLGAGEVTTRITADTNLIQEGISEKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVMGGGSQFI 266
Cdd:cd18778 85 RLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKV 164
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 164423939 267 IKFSKQNIAAYAEGGSVADEVISSVRNAIAFGTQDRLARRYDAH 310
Cdd:cd18778 165 RPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEAL 208
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
440-688 |
1.33e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 440 MEDVSLVIPAGKTTALVGASGSGKSTIVGLVERFYKPIEGKVylddvDIstlnvrwlRQQIALVSQEPTLfactiyDNIR 519
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DI--------KGSAALIAISSGL------NGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 520 HGLIGTKWESESEEQQRERIYEAARK----ANAHDFITSLPEGYetnvgergfllSGGQKQRIAIARAIVSDPKILLLDE 595
Cdd:PRK13545 101 TGIENIELKGLMMGLTKEKIKEIIPEiiefADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 596 ATSALD-TKSEGVVQAALEVAAEGRTTITIAHRLSTIKD-AHNIVVMAQGRIVEQGTHAELLAKRGAYYKlvtaqaiaAV 673
Cdd:PRK13545 170 ALSVGDqTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLK--------KY 241
|
250
....*....|....*
gi 164423939 674 NEMTAEEEAALDQQE 688
Cdd:PRK13545 242 NQMSVEERKDFREEQ 256
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1234-1319 |
1.46e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1234 LSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDKAAK--GRTTIAVAHRLSTIQK-ADIIYVFDQGRIV 1310
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQTV 238
|
....*....
gi 164423939 1311 EQGTHSELM 1319
Cdd:PRK15093 239 ETAPSKELV 247
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1234-1319 |
1.62e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.85 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 1234 LSGGQKQRIAIARALIRDPKILLLDEATSALDSESEHVVQAALDK-AAKGRTTIAVAHRLSTIQKA-DIIYVFDQGRIVE 1311
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
....*...
gi 164423939 1312 QGTHSELM 1319
Cdd:PRK09700 490 ILTNRDDM 497
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
442-649 |
2.14e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.38 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 442 DVSLVIPAGKTTALVGASGSGKSTIVglVERFYKpiEGKVYLddvdISTLNvRWLRQQIALVSQEPTLfactiydnIRHG 521
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYA--SGKARL----ISFLP-KFSRNKLIFIDQLQFL--------IDVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 522 LigtkweseseeqqreriyeaarkanahdfitslpeGYETnVGERGFLLSGGQKQRIAIARAIVSDPK--ILLLDEATSA 599
Cdd:cd03238 76 L-----------------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 164423939 600 LD-TKSEGVVQAALEVAAEGRTTITIAHRLSTIKDAHNIVVMAQ------GRIVEQG 649
Cdd:cd03238 120 LHqQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
571-601 |
2.32e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.32e-03
10 20 30
....*....|....*....|....*....|.
gi 164423939 571 SGGQKQRIAIARAIVSDPKILLLDEATSALD 601
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
138-259 |
2.53e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 41.40 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 138 TDELARLVLYFVYLAIGEFVTMYITTVGFIYSGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQEGIS 217
Cdd:cd18565 50 RGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLD 129
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 164423939 218 EKVGLTLQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVM 259
Cdd:cd18565 130 DGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGT 171
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
848-1034 |
3.93e-03 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 40.90 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 848 RDM---AFRSFLRQDVEFFDrdENSAGALTSFLSTETTHVAGLSGVTLGTIIMVLTTLIAACTVALALGWKLALVCIATI 924
Cdd:cd18549 75 TDMrrdLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 925 PILLGCGFYRFWMIAHYQRRAKSAYAGSASYASEAITAMRTVASLTRE-------QDVLQHYKDSlaKQQHASLISVLKS 997
Cdd:cd18549 153 PLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEeyeiekfDEGNDRFLES--KKKAYKAMAYFFS 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 164423939 998 SLLFaaSNSLMFLAfALGFwyGGTLIAKHE---YDMFTFF 1034
Cdd:cd18549 231 GMNF--FTNLLNLV-VLVA--GGYFIIKGEitlGDLVAFL 265
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1234-1302 |
4.77e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.27 E-value: 4.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 1234 LSGGQKQRIAIA-----RALIRDPkILLLDEATSALDSESEH-VVQAALDKAAKGRTTIAVAHRLSTIQKADIIY 1302
Cdd:cd03227 78 LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQaLAEAILEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
440-486 |
5.67e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 5.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164423939 440 MEDVSLVIPAGKTTALVGASGSGKSTIV------GLVERF---------YKPIEGKVYLDDV 486
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIndtlypALANRLngaktvpgrYTSIEGLEHLDKV 685
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
138-354 |
6.53e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 40.16 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 138 TDELARLVLYFVYLAIGEFVTMYIttvgFIYsgehISGKIrEHYLESCMRQN---------IGFFDKLGAGEVTTRITAD 208
Cdd:cd18540 38 LDGLTGFILLYLGLILIQALSVFL----FIR----LAGKI-EMGVSYDLRKKafehlqtlsFSYFDKTPVGWIMARVTSD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 209 TNLIQEGISEkvGLT--LQALATFIAAFVIGFVSFWKLTLILLSTVVALTLVmggGSQF---IIKFS----KQN---IAA 276
Cdd:cd18540 109 TQRLGEIISW--GLVdlVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVV---SIYFqkkILKAYrkvrKINsriTGA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 277 YAEGgsvadevISSVRNAIAFGTQDR-------LARRYDAHLTRAEHFGfrlkgsiGVMVAGMMTVLYLNYGLAFWQGSR 349
Cdd:cd18540 184 FNEG-------ITGAKTTKTLVREEKnlrefkeLTEEMRRASVRAARLS-------ALFLPIVLFLGSIATALVLWYGGI 249
|
....*
gi 164423939 350 FLLSG 354
Cdd:cd18540 250 LVLAG 254
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1234-1265 |
9.02e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 9.02e-03
10 20 30
....*....|....*....|....*....|..
gi 164423939 1234 LSGGQKQRIAIARALIRDPKILLLDEATSALD 1265
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
570-634 |
9.04e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.49 E-value: 9.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164423939 570 LSGGQKQRIAIA-----RAIVSDPkILLLDEATSALDTKS-EGVVQAALEVAAEGRTTITIAHRLSTIKDA 634
Cdd:cd03227 78 LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELA 147
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
144-279 |
9.47e-03 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 39.74 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423939 144 LVLYFVYLaigeFVTMYITTVGFIYsGEHISGKIREHYLESCMRQNIGFFDKLGAGEVTTRITADTNLIQE----G---- 215
Cdd:cd18549 49 LALYILRT----LLNYFVTYWGHVM-GARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGpedl 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164423939 216 -ISekvgltlqaLATFIAAFVIGFVSFWKLTLILLSTVVALTLvmgggsqFIIKFSKQNIAAYAE 279
Cdd:cd18549 124 fIS---------IITIIGSFIILLTINVPLTLIVFALLPLMII-------FTIYFNKKMKKAFRR 172
|
|
| |
