|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
181-758 |
4.66e-172 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 507.01 E-value: 4.66e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 181 APVRRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPdkeEQRSQINGVCLLFVAMGCVSLFTQFLQGY 260
Cdd:COG1132 7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAG---GDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 261 AFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSW 340
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 341 KLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKA 420
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 421 NIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQ 500
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 501 PPISVYNTAGEKwDNFQGKIDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVM 580
Cdd:COG1132 322 PEIPDPPGAVPL-PPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 581 IDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQ 660
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGR--PDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 661 LSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKG 740
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570
....*....|....*...
gi 767920345 741 THEELMAQKGAYYKLVTT 758
Cdd:COG1132 557 THEELLARGGLYARLYRL 574
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
520-759 |
6.58e-145 |
|
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: 424.26 E-value: 6.58e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 599
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPVLFACSIMDNIKYGDNtkEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDP 679
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP--DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 680 KILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTG 759
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
187-503 |
9.52e-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: 408.76 E-value: 9.52e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 187 LKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSG 266
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 267 ELLTKRLRKFGFRAMLGQDIAWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVI 346
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 347 LCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFC 426
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 427 FAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQPPI 503
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
175-756 |
1.49e-126 |
|
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: 393.82 E-value: 1.49e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 175 QEEVEPAPVRRILKFSAPEWPYM---LVGSVGAAVNGTVTPLyaflFSQILGTFSIPDKeeQRSQINGVCLLFVAMGCVS 251
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLlqvLLASLLINLLALATPL----FTQVVIDRVLPNQ--DLSTLWVLAIGLLLALLFE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 252 LFTQFLQGYAFAKSGELLTKRL-RKFgFRAMLGQDIAWFDdlRNSPGALTTRLaTDASQVQGAAGSQIGMIVNSFTNVTV 330
Cdd:COG2274 210 GLLRLLRSYLLLRLGQRIDLRLsSRF-FRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 331 AMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLtgfASRDKQALEMVGQITN---EALSNIRTVAGIGKERRFIEALET 407
Cdd:COG2274 286 FLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRL---RRLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRWEN 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 408 ELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHF-------SYVFRVISAVvlsatalGRAFSYT 480
Cdd:COG2274 363 LLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLgqliafnILSGRFLAPV-------AQLIGLL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 481 PSYAKAKISAARFFQLLDrQPPISVYNTAGEKWDNFQGKIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCG 560
Cdd:COG2274 436 QRFQDAKIALERLDDILD-LPPEREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 561 KSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLH 640
Cdd:COG2274 514 KSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD--PDATDEEIIEAARLAGLH 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 641 DFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLS 720
Cdd:COG2274 592 DFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLS 671
|
570 580 590
....*....|....*....|....*....|....*.
gi 767920345 721 TIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLV 756
Cdd:COG2274 672 TIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELV 707
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
175-756 |
7.77e-125 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 389.47 E-value: 7.77e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 175 QEEVEPAP-VRRILKFSAPEWPYMLVGSVG---AAVNGTVTPLY-AFLFSQILGTFSIPDkeeQRSQINGVCLLFVAmgc 249
Cdd:TIGR00958 140 QGQSETADlLFRLLGLSGRDWPWLISAFVFltlSSLGEMFIPFYtGRVIDTLGGDKGPPA---LASAIFFMCLLSIA--- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 250 vSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVT 329
Cdd:TIGR00958 214 -SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 330 VAMIIAFSFSWKLSLVILCFFPFLALSG---ATQTRMLtgfASRDKQALEMVGQITNEALSNIRTVAGIGKE----RRFI 402
Cdd:TIGR00958 291 GLLGFMLWLSPRLTMVTLINLPLVFLAEkvfGKRYQLL---SEELQEAVAKANQVAEEALSGMRTVRSFAAEegeaSRFK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 403 EALETELEKPFKTAIQKAniyGFCFAFAQCIMFIANSASYrYGGYLI-----SNEGLhfsyvfrviSAVVLSATALGRAF 477
Cdd:TIGR00958 368 EALEETLQLNKRKALAYA---GYLWTTSVLGMLIQVLVLY-YGGQLVltgkvSSGNL---------VSFLLYQEQLGEAV 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 478 SYT----PSYAKAKISAARFFQLLDRQPPISvyNTAGEKWDNFQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAF 553
Cdd:TIGR00958 435 RVLsyvySGMMQAVGASEKVFEYLDRKPNIP--LTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVAL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 554 VGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTKeiPMERVIAA 633
Cdd:TIGR00958 513 VGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDT--PDEEIMAA 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 634 AKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQValDKAREGRTCI 713
Cdd:TIGR00958 591 AKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVL 668
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 767920345 714 VIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLV 756
Cdd:TIGR00958 669 LIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
181-757 |
3.92e-112 |
|
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: 352.08 E-value: 3.92e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 181 APVRRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEQrsqINGVCLLFVAMGCVSLFTQFLQGY 260
Cdd:TIGR02204 4 RPLAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGL---LNRYFAFLLVVALVLALGTAARFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 261 AFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSW 340
Cdd:TIGR02204 81 LVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 341 KLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKA 420
Cdd:TIGR02204 159 KLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 421 NIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQ 500
Cdd:TIGR02204 239 RTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 501 PPISVYNTAGEKWDNFQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVM 580
Cdd:TIGR02204 319 PDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 581 IDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYG--DNTKEipmeRVIAAAKQAQLHDFVMSLPEKYETNVGSQG 658
Cdd:TIGR02204 399 LDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGrpDATDE----EVEAAARAAHAHEFISALPEGYDTYLGERG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 659 SQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIE 738
Cdd:TIGR02204 475 VTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVA 554
|
570
....*....|....*....
gi 767920345 739 KGTHEELMAQKGAYYKLVT 757
Cdd:TIGR02204 555 QGTHAELIAKGGLYARLAR 573
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
184-755 |
3.77e-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: 341.31 E-value: 3.77e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 184 RRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQIL-GTFSipdkEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAF 262
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFG----GRDRSVLWWVPLVVIGLAVLRGICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 263 AKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKL 342
Cdd:TIGR02203 79 SWVSNKVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 343 SLVILCFFPFLALSGATQTRMLTGFaSRDKQalEMVGQITN---EALSNIRTVAGIGKE----RRFIEALETELEKPFKT 415
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRVSKRLRRI-SKEIQ--NSMGQVTTvaeETLQGYRVVKLFGGQayetRRFDAVSNRNRRLAMKM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 416 AiQKANIYGfcfAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQ 495
Cdd:TIGR02203 234 T-SAGSISS---PITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 496 LLDRQPPIsvyNTAGEKWDNFQGKIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD 575
Cdd:TIGR02203 310 LLDSPPEK---DTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 576 QGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDnTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVG 655
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 656 SQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGV 735
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570 580
....*....|....*....|
gi 767920345 736 VIEKGTHEELMAQKGAYYKL 755
Cdd:TIGR02203 545 IVERGTHNELLARNGLYAQL 564
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
520-755 |
1.53e-106 |
|
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: 324.95 E-value: 1.53e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 599
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPVLFACSIMDNIKYGdnTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDP 679
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG--RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 680 KILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 755
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
520-755 |
2.46e-104 |
|
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: 319.56 E-value: 2.46e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 599
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPVLFACSIMDNIKYGD-NTKEipmERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRD 678
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRpDATD---EEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 679 PKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 755
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-756 |
8.18e-104 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 348.56 E-value: 8.18e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH---TIIsVAHRLSTVRAADTI--------- 68
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnriTII-IAHRLSTIRYANTIfvlsnrerg 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 69 --------------------------------------IGFEHGTAVERGTHEELLERK-GVYFTLVTLQS-QGNQALNE 108
Cdd:PTZ00265 659 stvdvdiigedptkdnkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKvSSKKSSNN 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 109 EDIKDATEDDMLARTFSRGSYQDSLRASIRQRSKSqlsylvhepplaVVDHKSTYEEDRKDKDIPVQEEVepAPVRRILK 188
Cdd:PTZ00265 739 DNDKDSDMKSSAYKDSERGYDPDEMNGNSKHENES------------ASNKKSCKMSDENASENNAGGKL--PFLRNLFK 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 189 fSAPEWPYML---------------VGSVGAAVNGTVTPLYAFLFSQILGT-FSIPDKEEQRSQINgvclLFVAMGCVSL 252
Cdd:PTZ00265 805 -RKPKAPNNLrivyreifsykkdvtIIALSILVAGGLYPVFALLYAKYVSTlFDFANLEANSNKYS----LYILVIAIAM 879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 253 F-TQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVA 331
Cdd:PTZ00265 880 FiSETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVS 959
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 332 MIIAFSFSWKLSLVIL-CFFPFLALSgATQTRmLTGFASRDKQALEMVGQI----------------TNEALSNIRTVAG 394
Cdd:PTZ00265 960 MVMSFYFCPIVAAVLTgTYFIFMRVF-AIRAR-LTANKDVEKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVII 1037
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 395 IGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALG 474
Cdd:PTZ00265 1038 YGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAG 1117
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 475 RAFSYTPSYAKAKISAARFFQLLDRQPPISVYNTAGEKWDN---FQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTL 551
Cdd:PTZ00265 1118 KLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTT 1197
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 552 AFVGSSGCGKSTSIQLLERFYD------------------------------------------------------PDQG 577
Cdd:PTZ00265 1198 AIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSG 1277
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 578 KVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGdnTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQ 657
Cdd:PTZ00265 1278 KILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG--KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPY 1355
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 658 GSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVAL----DKAreGRTCIVIAHRLSTIQNADIIAVMAQ 733
Cdd:PTZ00265 1356 GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNN 1433
|
890 900
....*....|....*....|....*....
gi 767920345 734 -----GVVIEKGTHEELM-AQKGAYYKLV 756
Cdd:PTZ00265 1434 pdrtgSFVQAHGTHEELLsVQDGVYKKYV 1462
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
492-755 |
2.88e-103 |
|
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: 329.86 E-value: 2.88e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 492 RFFQLLDRQPPISVYNTAGE-KWDnfQGKIDFVDCKFTYpsRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLER 570
Cdd:COG5265 331 RMFDLLDQPPEVADAPDAPPlVVG--GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 571 FYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNtkEIPMERVIAAAKQAQLHDFVMSLPEKY 650
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP--DASEEEVEAAARAAQIHDFIESLPDGY 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 651 ETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAV 730
Cdd:COG5265 485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILV 564
|
250 260
....*....|....*....|....*
gi 767920345 731 MAQGVVIEKGTHEELMAQKGAYYKL 755
Cdd:COG5265 565 LEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
518-750 |
3.12e-103 |
|
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: 316.47 E-value: 3.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 518 GKIDFVDCKFTYpsRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSN 597
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 598 IGIVSQEPVLFACSIMDNIKYGDNTkeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVR 677
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 678 DPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKG 750
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
269-755 |
7.96e-89 |
|
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: 290.51 E-value: 7.96e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 269 LTKRLRKFGFRAMLGQDIAWFDDLRNspGALTTRLATDASQVQGA-------AGSQIGMIVnsftnvtVAMIIAFSFSWK 341
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGLARLRS--GDLLNRLVADVDALDNLylrvllpLLVALLVIL-------AAVAFLAFFSPA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 342 LSLVILCFFPFLALSGATQTRMLTGFASRDKQAL--EMVGQITnEALSNIRTVAGIGKERRF---IEALETELekpfkTA 416
Cdd:COG4987 157 LALVLALGLLLAGLLLPLLAARLGRRAGRRLAAAraALRARLT-DLLQGAAELAAYGALDRAlarLDAAEARL-----AA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 417 IQK--ANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYvfrvISAVVLSA-------TALGRAFSYTPSYAKAk 487
Cdd:COG4987 231 AQRrlARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPL----LALLVLAAlalfealAPLPAAAQHLGRVRAA- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 488 isAARFFQLLDRQPPISvyNTAGEKWDNFQGKIDFVDCKFTYPSRPdSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQL 567
Cdd:COG4987 306 --ARRLNELLDAPPAVT--EPAEPAPAPGGPSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 568 LERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNtkEIPMERVIAAAKQAQLHDFVMSLP 647
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP--DATDEELWAALERVGLGDWLAALP 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 648 EKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADI 727
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDR 538
|
490 500
....*....|....*....|....*...
gi 767920345 728 IAVMAQGVVIEKGTHEELMAQKGAYYKL 755
Cdd:COG4987 539 ILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
489-759 |
2.71e-87 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 287.24 E-value: 2.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 489 SAAR---FFQLLDRQPPISVYNTAGEKwDNFQGKIDFVDCKFTYPSRpdSQVLNGLSVSISPGQTLAFVGSSGCGKSTSI 565
Cdd:PRK13657 302 AAPKleeFFEVEDAVPDVRDPPGAIDL-GRVKGAVEFDDVSFSYDNS--RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 566 QLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYG--DNTKEipmeRVIAAAKQAQLHDFV 643
Cdd:PRK13657 379 NLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGrpDATDE----EMRAAAERAQAHDFI 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 644 MSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQ 723
Cdd:PRK13657 455 ERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVR 534
|
250 260 270
....*....|....*....|....*....|....*.
gi 767920345 724 NADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTG 759
Cdd:PRK13657 535 NADRILVFDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
184-750 |
8.56e-87 |
|
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: 285.11 E-value: 8.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 184 RRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIpdKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFA 263
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLII--GGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 264 KSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTnVTVAMIIA-FSFSWKL 342
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLR--GKSTGELATLLTEGVEALDGYFARYLPQLFLAAL-VPLLILVAvFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 343 SLVILCFFP----FLALSG-ATQTRMltgfasrDKQALEMvgqitnEALSN--IRTVAGI------GKERRFIEALETEL 409
Cdd:COG4988 161 GLILLVTAPliplFMILVGkGAAKAS-------RRQWRAL------ARLSGhfLDRLRGLttlklfGRAKAEAERIAEAS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 410 EKpFKTA------IQKANIYGFCFAFAQCIMFIANSASYRYggyliSNEGLHFsyvFRVISAVVLSA------TALGRAF 477
Cdd:COG4988 228 ED-FRKRtmkvlrVAFLSSAVLEFFASLSIALVAVYIGFRL-----LGGSLTL---FAALFVLLLAPefflplRDLGSFY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 478 sytpsYAKAK-ISAA-RFFQLLDRQPPISVYNTAGEKWDNfQGKIDFVDCKFTYPSRPdsQVLNGLSVSISPGQTLAFVG 555
Cdd:COG4988 299 -----HARANgIAAAeKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 556 SSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAK 635
Cdd:COG4988 371 PSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAALE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 636 QAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVI 715
Cdd:COG4988 449 AAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILI 528
|
570 580 590
....*....|....*....|....*....|....*
gi 767920345 716 AHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKG 750
Cdd:COG4988 529 THRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
520-756 |
1.03e-83 |
|
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: 265.89 E-value: 1.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYpsRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNI 598
Cdd:cd03252 1 ITFEHVRFRY--KPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 599 GIVSQEPVLFACSIMDNIKYGDNTkeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRD 678
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 679 PKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLV 756
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
242-755 |
5.10e-83 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 275.36 E-value: 5.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 242 LLFVAMGCVSLFTQFLQGYAFA-KSGELLTkRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGM 320
Cdd:PRK11176 69 LVVIGLMILRGITSFISSYCISwVSGKVVM-TMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALIT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 321 IVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS-GATQTRmltgFASRDKQALEMVGQITNEA---LSNIRTVAGIG 396
Cdd:PRK11176 146 VVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAiRVVSKR----FRNISKNMQNTMGQVTTSAeqmLKGHKEVLIFG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 397 ----KERRFIEALETELEKPFKTAIQKAniygfcfAFAQCIMFIAnSASYRYGGYLISneglhFSYVFRVISA----VVL 468
Cdd:PRK11176 222 gqevETKRFDKVSNRMRQQGMKMVSASS-------ISDPIIQLIA-SLALAFVLYAAS-----FPSVMDTLTAgtitVVF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 469 SAT-ALGRAF----SYTPSYAKAKISAARFFQLLDRQPPIsvyNTAGEKWDNFQGKIDFVDCKFTYPSRpDSQVLNGLSV 543
Cdd:PRK11176 289 SSMiALMRPLksltNVNAQFQRGMAACQTLFAILDLEQEK---DEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 544 SISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGdNTK 623
Cdd:PRK11176 365 KIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYA-RTE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 624 EIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVAL 703
Cdd:PRK11176 444 QYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 767920345 704 DKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 755
Cdd:PRK11176 524 DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
514-736 |
2.59e-82 |
|
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: 261.64 E-value: 2.59e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 514 DNFQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQF 593
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 594 LRSNIGIVSQEPVLFACSIMDNIKYGDNTKeiPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIAR 673
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSC--SFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 674 AIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVV 736
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
213-755 |
2.94e-82 |
|
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: 276.62 E-value: 2.94e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 213 LYAFLFSQILGTFS------IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQG---YAFAKSGELLTKRLRKFGFRAMLG 283
Cdd:TIGR01846 145 LLISLALQLFALVTpllfqvVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGlrtYLFAHLTSRIDVELGARLYRHLLG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 284 QDIAWFDDLRNspGALTTRLATDASQVQGAAGSQIGMIVNSFTnVTVAMIIAFSFSWKLSLVILCFFPFLAL-----SGA 358
Cdd:TIGR01846 225 LPLGYFESRRV--GDTVARVRELEQIRNFLTGSALTVVLDLLF-VVVFLAVMFFYSPTLTGVVIGSLVCYALlsvfvGPI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 359 TQTRMLTGFaSRDKQALEMVgqitNEALSNIRTVAGIGKERRFIEALETELEKPFKT---AIQKANIYGFCFAFAQCIMF 435
Cdd:TIGR01846 302 LRKRVEDKF-ERSAAATSFL----VESVTGIETIKATATEPQFQNRWDRQLAAYVAAsfrVTNLGNIAGQAIELIQKLTF 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 436 IAN---SASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTpsyakaKISAARFFQLLDRqpPISVYNTAGEK 512
Cdd:TIGR01846 377 AILlwfGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQT------GIALERLGDILNS--PTEPRSAGLAA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 513 WDNFQGKIDFVDCKFTYpsRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNV 591
Cdd:TIGR01846 449 LPELRGAITFENIRFRY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADP 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 592 QFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAI 671
Cdd:TIGR01846 527 AWLRRQMGVVLQENVLFSRSIRDNIALCN--PGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAI 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 672 ARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGA 751
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGL 684
|
....
gi 767920345 752 YYKL 755
Cdd:TIGR01846 685 YARL 688
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
157-763 |
2.59e-77 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 272.29 E-value: 2.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 157 VDHKSTYEEDRKDKD--IP--VQEEVEPAPVRRILkfsapewpymLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDkee 232
Cdd:PTZ00265 28 LNKKGTFELYKKIKTqkIPffLPFKCLPASHRKLL----------GVSFVCATISGGTLPFFVSVFGVIMKNMNLGE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 233 qrsQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlrNSPGA-LTTRLATDASQVQ 311
Cdd:PTZ00265 95 ---NVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHD---NNPGSkLTSDLDFYLEQVN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 312 GAAGSQIgMIVNSFTNVTVAMIIAFSF-SWKLSLVILCFFPFLALSGATQTRMLTgfaSRDKQAL---EMVGQITNEALS 387
Cdd:PTZ00265 169 AGIGTKF-ITIFTYASAFLGLYIWSLFkNARLTLCITCVFPLIYICGVICNKKVK---INKKTSLlynNNTMSIIEEALV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 388 NIRTVAGIGKERRFIEALETElEKPFKTAIQKAN---------IYGF-----CFAFAQCIMFIANSASYRYggyliSNEG 453
Cdd:PTZ00265 245 GIRTVVSYCGEKTILKKFNLS-EKLYSKYILKANfmeslhigmINGFilasyAFGFWYGTRIIISDLSNQQ-----PNND 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 454 LHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQPPISvYNTAGEKWDNFQgKIDFVDCKFTYPSRP 533
Cdd:PTZ00265 319 FHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVE-NNDDGKKLKDIK-KIQFKNVRFHYDTRK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMI-DGHDSKKVNVQFLRSNIGIVSQEPVLFACSI 612
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIKYG----------------------------------------------DNTKEIPMER---------VIAAAKQA 637
Cdd:PTZ00265 477 KNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttDSNELIEMRKnyqtikdseVVDVSKKV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 638 QLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALD--KAREGRTCIVI 715
Cdd:PTZ00265 557 LIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIII 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 716 AHRLSTIQNADIIAVM-----------------------------------------------AQGVVIEKGTHEELMAQ 748
Cdd:PTZ00265 637 AHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnAGSYIIEQGTHDALMKN 716
|
730
....*....|....*
gi 767920345 749 KGAYYKLVTTGSPIS 763
Cdd:PTZ00265 717 KNGIYYTMINNQKVS 731
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
197-492 |
4.12e-74 |
|
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: 242.77 E-value: 4.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 197 MLVGSVGAAVNGTVTPLYAFLFSQILGTFS-----IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTK 271
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 272 RLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFP 351
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 352 FLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQ 431
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 432 CIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAAR 492
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAK 299
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
520-734 |
2.67e-72 |
|
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: 233.04 E-value: 2.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPDsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 599
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPVLFACSIMDNIkygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDP 679
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 680 KILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQG 734
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
517-756 |
4.89e-72 |
|
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: 249.09 E-value: 4.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 517 QGKIDFVDCKFTYpSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS 596
Cdd:TIGR03796 475 SGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLAN 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 597 NIGIVSQEPVLFACSIMDNIKYGDNTkeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIV 676
Cdd:TIGR03796 554 SVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALV 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 677 RDPKILLLDEATSALDTESEKTVQVALdkAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLV 756
Cdd:TIGR03796 632 RNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
197-490 |
1.30e-66 |
|
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: 223.31 E-value: 1.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 197 MLVGSVGAAVNGTVTPLYAFLFSQILGTF-------------SIPDK----EEQRSQINGVCLLFVAMGCVSLFTQFLQG 259
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnggmtnitgnssGLNSSagpfEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 260 YAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFS 339
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 340 WKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQK 419
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 420 ANIYGFCFAFAQCIMFIANSASYRYGGYLI-SNEGLHFSYVFRVISAVVLSATALGRAFSYTPsYAKAKISA 490
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVtQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAA 309
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
183-755 |
4.00e-66 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 229.99 E-value: 4.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 183 VRRILKFSAPeWP-------YMLVGSVGAAVNGTVtpLYAFLFSQILGTFSIPDKeeqrsQINGVCLLFVAMGCVSLFTQ 255
Cdd:PRK10790 11 LKRLLAYGSP-WRkplglavLMLWVAAAAEVSGPL--LISYFIDNMVAKGNLPLG-----LVAGLAAAYVGLQLLAAGLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 256 FLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlrNSP-GALTTRLATDASQVQGAAGSQIGMIVNSFTNVtVAMII 334
Cdd:PRK10790 83 YAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFD---TQPvGQLISRVTNDTEVIRDLYVTVVATVLRSAALI-GAMLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 335 A-FSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPF 413
Cdd:PRK10790 159 AmFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 414 KTAIQKANIYGFC--------FAFAQCIMFIAnsasyrYGgylISNEGlhfsyvfrVISAVVLSA--TALGRA------- 476
Cdd:PRK10790 239 MARMQTLRLDGFLlrpllslfSALILCGLLML------FG---FSASG--------TIEVGVLYAfiSYLGRLnepliel 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 477 FSYTPSYAKAKISAARFFQLLDRqpPISVYNTAGEKWDnfQGKIDFVDCKFTYpsRPDSQVLNGLSVSISPGQTLAFVGS 556
Cdd:PRK10790 302 TTQQSMLQQAVVAGERVFELMDG--PRQQYGNDDRPLQ--SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGH 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 557 SGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGdntKEIPMERVIAAAKQ 636
Cdd:PRK10790 376 TGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG---RDISEEQVWQALET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 637 AQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIA 716
Cdd:PRK10790 453 VQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
570 580 590
....*....|....*....|....*....|....*....
gi 767920345 717 HRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 755
Cdd:PRK10790 533 HRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
324-759 |
1.15e-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: 225.92 E-value: 1.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 324 SFTNVTVAMIIAFSFSWKLSLVILCF-FPFLALSGATQTRMLTGFASRDKQALEMVGQITnEALSNIRTVAGIGKERRFI 402
Cdd:TIGR01192 140 TFVALFLLIPTAFAMDWRLSIVLMVLgILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVS-DSISNVSVVHSYNRIEAET 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 403 EALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHfsyVFRVISAVVLSATALGR-----AF 477
Cdd:TIGR01192 219 SALKQFTNNLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTVLVIKGELS---VGEVIAFIGFANLLIGRldqmsGF 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 478 SYTPSYAKAKISaaRFFQLLDRQPPISVYNTAGEkWDNFQGKIDFVDCKFTYPSrpDSQVLNGLSVSISPGQTLAFVGSS 557
Cdd:TIGR01192 296 ITQIFEARAKLE--DFFDLEDSVFQREEPADAPE-LPNVKGAVEFRHITFEFAN--SSQGVFDVSFEAKAGQTVAIVGPT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 558 GCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTKEipMERVIAAAKQA 637
Cdd:TIGR01192 371 GAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGAT--DEEVYEAAKAA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 638 QLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAH 717
Cdd:TIGR01192 449 AAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAH 528
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 767920345 718 RLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTG 759
Cdd:TIGR01192 529 RLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRS 570
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
518-741 |
4.84e-62 |
|
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: 207.35 E-value: 4.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 518 GKIDFVDCKFTYpsRPDSQ-VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS 596
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 597 NIGIVSQEPVLFACSIMDNI----KYGDntkeipmERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIA 672
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdpfgEYSD-------EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 673 RAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGT 741
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
518-740 |
1.85e-60 |
|
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: 203.20 E-value: 1.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 518 GKIDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSN 597
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 598 IGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVR 677
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 678 DPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKG 740
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
489-755 |
3.57e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 210.45 E-value: 3.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 489 SAARFFQLLDRQPPISVYNTAGEKWDnfQGKIDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL 568
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 569 ERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTkeIPMERVIAAAKQAQLHDFVMSlPE 648
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPN--ASDEALIEVLQQVGLEKLLED-DK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 649 KYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADII 728
Cdd:PRK11160 464 GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRI 543
|
250 260
....*....|....*....|....*..
gi 767920345 729 AVMAQGVVIEKGTHEELMAQKGAYYKL 755
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-755 |
1.85e-58 |
|
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: 216.35 E-value: 1.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNE-SEAMVQEVLSK--IQHGHTIISVAHRLSTVRAADTIIGFEHGTAV 77
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPegVLKNKTRILVTHGISYLPQVDVIIVMSGGKIS 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 78 ERGTHEELLERKGVYFTLVTLQSQGNQALNEEDI---------KDA--TEDDMLARTFSRGSYQDSLRASirqrSKSQLS 146
Cdd:TIGR00957 841 EMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSwtalvsgegKEAklIENGMLVTDVVGKQLQRQLSAS----SSDSGD 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 147 YLVHEPPLAVVDHKSTYEEDRKdkdipvQEEVEPAPVRRIlKFSApEWPYMlvgsvgAAVNGTVTPLYAFLF-------- 218
Cdd:TIGR00957 917 QSRHHGSSAELQKAEAKEETWK------LMEADKAQTGQV-ELSV-YWDYM------KAIGLFITFLSIFLFvcnhvsal 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 219 -SQILGTFSIPDKEEQRSQINGVCLLFV--AMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNS 295
Cdd:TIGR00957 983 aSNYWLSLWTDDPMVNGTQNNTSLRLSVygALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTP 1060
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 296 PGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVIlcffPFLALSGATQTRMLTGfASRDKQAL 375
Cdd:TIGR00957 1061 SGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVII----PPLGLLYFFVQRFYVA-SSRQLKRL 1135
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 376 EMVGQIT-----NEALSNIRTVAGIGKERRFIEALETELEkpfktAIQKAniygfcfafaqCIMFIANSASYRYGGYLIS 450
Cdd:TIGR00957 1136 ESVSRSPvyshfNETLLGVSVIRAFEEQERFIHQSDLKVD-----ENQKA-----------YYPSIVANRWLAVRLECVG 1199
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 451 NEGLHFSYVFRVISAVVLSATALGRAFSYT-------------PSYAKAKISAA---RFFQLLDRQPPISVYNTAG-EKW 513
Cdd:TIGR00957 1200 NCIVLFAALFAVISRHSLSAGLVGLSVSYSlqvtfylnwlvrmSSEMETNIVAVerlKEYSETEKEAPWQIQETAPpSGW 1279
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 514 DNfQGKIDFVDCKFTYpsRPD-SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQ 592
Cdd:TIGR00957 1280 PP-RGRVEFRNYCLRY--REDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH 1356
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 593 FLRSNIGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIA 672
Cdd:TIGR00957 1357 DLRFKITIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLA 1433
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 673 RAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAY 752
Cdd:TIGR00957 1434 RALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
...
gi 767920345 753 YKL 755
Cdd:TIGR00957 1514 YSM 1516
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
537-748 |
3.92e-55 |
|
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: 199.20 E-value: 3.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI 616
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 617 -KYGDntkeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 695
Cdd:COG4618 427 aRFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEG 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767920345 696 EKTVQVALDKARE-GRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:COG4618 503 EAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
195-731 |
2.98e-54 |
|
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: 195.97 E-value: 2.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 195 PYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDkeEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLR 274
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLISAG--EPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 275 KFGFRAMLGQDIAWFddLRNSPGALTTRLATDASQVQG-AAGSQIGMIVNSFtnVTVAMIIA-FSFSWKLSLVILCFFP- 351
Cdd:TIGR02857 81 ERLLEAVAALGPRWL--QGRPSGELATLALEGVEALDGyFARYLPQLVLAVI--VPLAILAAvFPQDWISGLILLLTAPl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 352 ---FLALSG-ATQTRmltgfASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELE-------KPFKTAIQKA 420
Cdd:TIGR02857 157 ipiFMILIGwAAQAA-----ARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEeyrertmRVLRIAFLSS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 421 NIYGFcFAfAQCIMFIANSASYRY-GGYLISNEGLhfsYVFRVISAVVLSATALGRAFSYTpsyAKAKISAARFFQLLDR 499
Cdd:TIGR02857 232 AVLEL-FA-TLSVALVAVYIGFRLlAGDLDLATGL---FVLLLAPEFYLPLRQLGAQYHAR---ADGVAAAEALFAVLDA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 500 QPPIsVYNTAGEKWDNFQGkIDFVDCKFTYPSRPdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV 579
Cdd:TIGR02857 304 APRP-LAGKAPVTAAPASS-LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 580 MIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGS 659
Cdd:TIGR02857 380 AVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGA 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 660 QLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVM 731
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
197-470 |
6.30e-53 |
|
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: 184.77 E-value: 6.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 197 MLVGSVGAAVNGTVTPLYAFLFSQILGTFsIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 276
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL-LPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 277 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS 356
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 357 GATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFI 436
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 767920345 437 ANSASYRYGGYLISNEGLHFS--YVFRVISAVVLSA 470
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGdlVAFLSLFAQLFGP 273
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
292-752 |
6.60e-53 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 193.01 E-value: 6.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 292 LRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFT-NVTVAMIIAFSFSWKLSLVILCFFPFLALsgaTQTRMLTGFASR 370
Cdd:PRK10789 88 LRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVmGCAVLIVMSTQISWQLTLLALLPMPVMAI---MIKRYGDQLHER 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 371 DKQALEMVGQITN---EALSNIRTVAGIGKE----RRFIEALETELEKPFKTAIQKA----NIYgfcFAFAqcimfIANS 439
Cdd:PRK10789 165 FKLAQAAFSSLNDrtqESLTSIRMIKAFGLEdrqsALFAADAEDTGKKNMRVARIDArfdpTIY---IAIG-----MANL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 440 ASYRYGGYLISNEGLHF----SYVFrVISAVVLSATALGRAFSYTpsyakAKISAA--RFFQLLDRQPpisVYNTAGEKW 513
Cdd:PRK10789 237 LAIGGGSWMVVNGSLTLgqltSFVM-YLGLMIWPMLALAWMFNIV-----ERGSAAysRIRAMLAEAP---VVKDGSEPV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 514 DNFQGKIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQF 593
Cdd:PRK10789 308 PEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 594 LRSNIGIVSQEPVLFACSIMDNIKYG--DNTKEipmeRVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAI 671
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSDTVANNIALGrpDATQQ----EIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 672 ARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGA 751
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGW 542
|
.
gi 767920345 752 Y 752
Cdd:PRK10789 543 Y 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
533-755 |
4.95e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 188.13 E-value: 4.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 533 PDSQVLNG-LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACS 611
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 612 IMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 691
Cdd:PRK11174 439 LRDNVLLGN--PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920345 692 DTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 755
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1-99 |
5.04e-50 |
|
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: 175.42 E-value: 5.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:cd03249 140 LSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQG 219
|
90
....*....|....*....
gi 767920345 81 THEELLERKGVYFTLVTLQ 99
Cdd:cd03249 220 THDELMAQKGVYAKLVKAQ 238
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
462-748 |
1.09e-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: 183.32 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 462 VISAVVLSATALG---RAFSYTPSYAKAKISAARFFQLLDRQPPisvyNTAGEKWDNFQGKIDfVDCKFTYPSRPDSQVL 538
Cdd:TIGR01842 260 MIAGSILVGRALApidGAIGGWKQFSGARQAYKRLNELLANYPS----RDPAMPLPEPEGHLS-VENVTIVPPGGKKPTL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 539 NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI-K 617
Cdd:TIGR01842 335 RGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaR 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 618 YGDNTKEipmERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK 697
Cdd:TIGR01842 415 FGENADP---EKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQ 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767920345 698 TVQVALDKAR-EGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:TIGR01842 492 ALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
297-757 |
4.54e-48 |
|
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: 181.48 E-value: 4.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 297 GALTTRLaTDASQVQGAAGSqigMIVNSFTNVTVAMIIAFSFSW---KLSLVILCFFPFLALSGATQTRMLTGFASRDKQ 373
Cdd:TIGR01193 253 GEIVSRF-TDASSIIDALAS---TILSLFLDMWILVIVGLFLVRqnmLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQ 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 374 ALEMVGQITNEALSNIRTVAGIGKERRFIEALETE----LEKPFKTAIQKANIYgfcfAFAQCIMFIANSASYRYGGYLI 449
Cdd:TIGR01193 329 ANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEfgdyLNKSFKYQKADQGQQ----AIKAVTKLILNVVILWTGAYLV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 450 SNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQ--LLDRQPPISVYNTAGEkwdNFQGKIDFVDCKF 527
Cdd:TIGR01193 405 MRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSEFINKKKRTELN---NLNGDIVINDVSY 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL 607
Cdd:TIGR01193 482 SYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYI 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 608 FACSIMDNIKYGDNTKeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 687
Cdd:TIGR01193 560 FSGSILENLLLGAKEN-VSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 688 TSALDTESEKTVQVALDKAREgRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVT 757
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
461-719 |
9.73e-45 |
|
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: 168.69 E-value: 9.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 461 RVISAVVLSATALGRAFSYTP----SYAKAKISAARFFQLLDRQPPISVYNTAGEKwDNFQGKIDFV--DCKFTYPsrPD 534
Cdd:TIGR02868 271 VTLAVLVLLPLAAFEAFAALPaaaqQLTRVRAAAERIVEVLDAAGPVAEGSAPAAG-AVGLGKPTLElrDLSAGYP--GA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 535 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMD 614
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 615 NIKYGdnTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 694
Cdd:TIGR02868 428 NLRLA--RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
250 260
....*....|....*....|....*
gi 767920345 695 SEKTVQVALDKAREGRTCIVIAHRL 719
Cdd:TIGR02868 506 TADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
518-741 |
6.20e-44 |
|
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: 157.19 E-value: 6.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 518 GKIDFVDCKFTYpsRPD-SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS 596
Cdd:cd03369 5 GEIEVENLSVRY--APDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 597 NIGIVSQEPVLFACSIMDNI----KYGDntkeipmERVIAAAKqaqlhdfvmslpekyetnVGSQGSQLSRGEKQRIAIA 672
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdpfdEYSD-------EEIYGALR------------------VSEGGLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 673 RAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGT 741
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
534-745 |
9.17e-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: 157.73 E-value: 9.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD-----PDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 606
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVLELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 LFACSIMDNIKYGDN-----TKEIPMERVIAAAKQAQLHDfvmslpekyETNVGSQGSQLSRGEKQRIAIARAIVRDPKI 681
Cdd:cd03260 92 PFPGSIYDNVAYGLRlhgikLKEELDERVEEALRKAALWD---------EVKDRLHALGLSGGQQQRLCLARALANEPEV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 682 LLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 745
Cdd:cd03260 163 LLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-761 |
3.94e-43 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 169.39 E-value: 3.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEvlSKIQH---GHTIISVAHRLSTVRAADTIIGFEHGTAV 77
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD--SCMKDelkGKTRVLVTNQLHFLPLMDRIILVSEGMIK 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 78 ERGTHEELLERKGVYFTLVTlqsqgNQALNEEDIKDATEDDMLARTFSRGSYQDSLR--ASIRQrSKSQLSYLVHeppla 155
Cdd:PLN03232 819 EEGTFAELSKSGSLFKKLME-----NAGKMDATQEVNTNDENILKLGPTVTIDVSERnlGSTKQ-GKRGRSVLVK----- 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 156 vvdhkstyeedrkdkdipvQEEVEPAPVrrilkfsapEWPYMLvgSVGAAVNG--TVTPLYA-FLFSQILGTFSIP---- 228
Cdd:PLN03232 888 -------------------QEERETGII---------SWNVLM--RYNKAVGGlwVVMILLVcYLTTEVLRVSSSTwlsi 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 229 --DKEEQRSQINGVCLLFVAM-GCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLAT 305
Cdd:PLN03232 938 wtDQSTPKSYSPGFYIVVYALlGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHT--NPTGRVINRFSK 1015
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 306 DASQVQGAAGSQIGMIVNSF-----TNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQ--------TR---------M 363
Cdd:PLN03232 1016 DIGDIDRNVANLMNMFMNQLwqllsTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSRevrrldsvTRspiyaqfgeA 1095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 364 LTGFAS-RDKQALEMVGQITNEAL-SNIR-TVAGIGKERRFIEALETelekpfktaiqkanIYGFCFAFAQCIMFIANSA 440
Cdd:PLN03232 1096 LNGLSSiRAYKAYDRMAKINGKSMdNNIRfTLANTSSNRWLTIRLET--------------LGGVMIWLTATFAVLRNGN 1161
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 441 SYRYGGYlISNEGLHFSY----------VFRVISAVVLSATALGRAFSYT--PSYAKAKISAARffqlldrqPPISvynt 508
Cdd:PLN03232 1162 AENQAGF-ASTMGLLLSYtlnittllsgVLRQASKAENSLNSVERVGNYIdlPSEATAIIENNR--------PVSG---- 1228
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 509 agekWDNfQGKIDFVDCKFTYpsRPD-SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSK 587
Cdd:PLN03232 1229 ----WPS-RGSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA 1301
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 588 KVNVQFLRSNIGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQ 667
Cdd:PLN03232 1302 KFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQ 1378
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 668 RIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMA 747
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
810
....*....|....*
gi 767920345 748 QKG-AYYKLVTTGSP 761
Cdd:PLN03232 1459 RDTsAFFRMVHSTGP 1473
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-102 |
1.05e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 163.80 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 81
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
90 100
....*....|....*....|.
gi 767920345 82 HEELLERKGVYFTLVTLQSQG 102
Cdd:COG1132 558 HEELLARGGLYARLYRLQFGE 578
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
520-749 |
2.35e-41 |
|
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: 150.95 E-value: 2.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 599
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPV--LFACSIMDNIKYG----DNTKEIPMERVIAAAKQAQLHDFvmslpekYETNVgsqgSQLSRGEKQRIAIAR 673
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlGLPREEIRERVEEALELVGLEHL-------ADRPP----HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 674 AIVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELMAQK 749
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
538-689 |
2.44e-41 |
|
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: 147.79 E-value: 2.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLF-ACSIMDNI 616
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 617 KYGdntkeIPMERVIAAAKQAQLHDFV--MSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATS 689
Cdd:pfam00005 81 RLG-----LLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
527-736 |
3.21e-41 |
|
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: 148.52 E-value: 3.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYP--SRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQE 604
Cdd:cd03246 8 FRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 605 PVLFACSIMDNIkygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLL 684
Cdd:cd03246 85 DELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767920345 685 DEATSALDTESEKTVQVALDKARE-GRTCIVIAHRLSTIQNADIIAVMAQGVV 736
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
520-740 |
5.08e-41 |
|
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: 148.23 E-value: 5.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQfLRSNIG 599
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPVLFACSIMDNIkygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqGSQLSRGEKQRIAIARAIVRDP 679
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 680 KILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKG 740
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
534-745 |
2.90e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.22 E-value: 2.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLF 608
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 609 A-CSIMDNIKYG---------DNTKEIPME---RViaaakqaQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAI 675
Cdd:COG1126 90 PhLTVLENVTLApikvkkmskAEAEERAMElleRV-------GLADKADAYP-----------AQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 676 VRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 745
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVlDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-105 |
3.61e-40 |
|
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: 156.90 E-value: 3.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 81
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGT 575
|
90 100
....*....|....*....|....
gi 767920345 82 HEELLERKGVYFTLVTLQSQGNQA 105
Cdd:COG5265 576 HAELLAQGGLYAQMWARQQEEEEA 599
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
537-717 |
5.36e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.50 E-value: 5.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI 616
Cdd:COG4619 15 ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 617 KYGDNTKEIP--MERVIAAAKQAQLHDFVMslpekyETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 694
Cdd:COG4619 95 PFPFQLRERKfdRERALELLERLGLPPDIL------DKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
170 180
....*....|....*....|....*
gi 767920345 695 SEKTVQVALDK--AREGRTCIVIAH 717
Cdd:COG4619 165 NTRRVEELLREylAEEGRAVLWVSH 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
520-748 |
1.42e-39 |
|
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: 153.52 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPDS--QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---SKKVNVQFL 594
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltkLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 595 RSNIGIVSQEPV--LFAC-SIMDNI-----KYGDNTKEIPMERVIAAAKQAQLH-DFVMSLPekyetnvgsqgSQLSRGE 665
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIaeplrLHGLLSRAERRERVAELLERVGLPpDLADRYP-----------HELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 666 KQRIAIARAIVRDPKILLLDEATSALDTesekTVQVA-LD-----KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIE 738
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDV----SVQAQiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
250
....*....|
gi 767920345 739 KGTHEELMAQ 748
Cdd:COG1123 486 DGPTEEVFAN 495
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-99 |
1.50e-39 |
|
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: 156.15 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 81
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692
|
90
....*....|....*...
gi 767920345 82 HEELLERKGVYFTLVTLQ 99
Cdd:COG2274 693 HEELLARKGLYAELVQQQ 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1-95 |
1.75e-39 |
|
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: 145.84 E-value: 1.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:cd03251 139 LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERG 218
|
90
....*....|....*
gi 767920345 81 THEELLERKGVYFTL 95
Cdd:cd03251 219 THEELLAQGGVYAKL 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
536-748 |
4.19e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.82 E-value: 4.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQfLRSNIGIVSQEPVLFA-CSIMD 614
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVPQEPALYPdLTVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 615 NIK-----YGDNTKEIPmERVIAAAKQAQLHDFvmslpekYETNVGsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATS 689
Cdd:COG1131 93 NLRffarlYGLPRKEAR-ERIDELLELFGLTDA-------ADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 690 ALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:COG1131 161 GLDPEARRELwELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
520-748 |
2.94e-38 |
|
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: 142.33 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQ---LLERfydPDQGKVMIDGHDSKKVN---VQ 592
Cdd:cd03258 2 IELKNVSKVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 593 FLRSNIGIVSQEPVLFAC-SIMDNIKY-----GDNTKEIPmERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEK 666
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALpleiaGVPKAEIE-ERVLELLELVGLEDKADAYP-----------AQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 667 QRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHE 743
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 767920345 744 ELMAQ 748
Cdd:cd03258 227 EVFAN 231
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
537-758 |
3.15e-38 |
|
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: 143.13 E-value: 3.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI 616
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 617 kygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESE 696
Cdd:cd03288 116 ---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 697 KTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQK-GAYYKLVTT 758
Cdd:cd03288 193 NILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVRT 255
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
522-734 |
7.73e-38 |
|
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: 140.29 E-value: 7.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 522 FVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIV 601
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 602 SQEP--VLFACSIMDNIKYG-----DNTKEIPmERVIAAAKQAQLHDFvmslpEKYETnvgsqgSQLSRGEKQRIAIARA 674
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGlenlgLPEEEIE-ERVEEALELVGLEGL-----RDRSP------FTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 675 IVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQG 734
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
528-740 |
2.83e-37 |
|
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: 139.18 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFL---RSNIGIVSQ 603
Cdd:cd03257 10 SFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 604 EPvlFAC-----SIMDNIK-----YGDNTKEipmerviAAAKQAQLHDFV-MSLPEKYETnvgSQGSQLSRGEKQRIAIA 672
Cdd:cd03257 90 DP--MSSlnprmTIGEQIAeplriHGKLSKK-------EARKEAVLLLLVgVGLPEEVLN---RYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 673 RAIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 740
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-759 |
5.95e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 149.89 E-value: 5.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDneseAMV-QEVLSKI----QHGHTIISVAHRLSTVRAADTIIGFEHGT 75
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD----AHVgRQVFDKCikdeLRGKTRVLVTNQLHFLSQVDRIILVHEGM 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 76 AVERGTHEELLERKGVYFTLvtLQSQGNQALNEEDIKDATEDDMLARTFSRGSYQD-SLRASIRQRSKSQLSYLVHeppl 154
Cdd:PLN03130 817 IKEEGTYEELSNNGPLFQKL--MENAGKMEEYVEENGEEEDDQTSSKPVANGNANNlKKDSSSKKKSKEGKSVLIK---- 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 155 avvdhkstyeedrkdkdipvQEEVEPAPVR-RILKfsapewpymlvgSVGAAVNGTVTPLYAFLFSQILGTFSIP----- 228
Cdd:PLN03130 891 --------------------QEERETGVVSwKVLE------------RYKNALGGAWVVMILFLCYVLTEVFRVSsstwl 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 229 ----DKEEQRSQ----INGV-CLLFVAMGCVSLftqfLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGAL 299
Cdd:PLN03130 939 sewtDQGTPKTHgplfYNLIyALLSFGQVLVTL----LNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFH--TNPLGRI 1012
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 300 TTRLATDASQVQGAAGSQIGMIVNSFTNV--TVAMI-IAFSFS-WK-LSLVILCFFPFLALSGATQ--TRM--------- 363
Cdd:PLN03130 1013 INRFAKDLGDIDRNVAVFVNMFLGQIFQLlsTFVLIgIVSTISlWAiMPLLVLFYGAYLYYQSTARevKRLdsitrspvy 1092
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 364 ------LTGFAS-RDKQALEMVGQITNEAL-SNIR-TVAGIGKERRFIEALETelekpfktaiqkanIYGFCFAFAQCIM 434
Cdd:PLN03130 1093 aqfgeaLNGLSTiRAYKAYDRMAEINGRSMdNNIRfTLVNMSSNRWLAIRLET--------------LGGLMIWLTASFA 1158
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 435 FIANSASYRYGGYlISNEGLHFSY----------VFRVISAVVLSATALGRAFSYT--PSYAKAKISaarffqllDRQPP 502
Cdd:PLN03130 1159 VMQNGRAENQAAF-ASTMGLLLSYalnitslltaVLRLASLAENSLNAVERVGTYIdlPSEAPLVIE--------NNRPP 1229
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 503 isvyntagEKWDNfQGKIDFVDCKFTYpsRPD-SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMI 581
Cdd:PLN03130 1230 --------PGWPS-SGSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILI 1298
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 582 DGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQL 661
Cdd:PLN03130 1299 DGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENF 1375
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 662 SRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKarEGRTC--IVIAHRLSTIQNADIIAVMAQGVVIEK 739
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCtmLIIAHRLNTIIDCDRILVLDAGRVVEF 1453
|
810 820
....*....|....*....|..
gi 767920345 740 GTHEELMAQKG-AYYKLV-TTG 759
Cdd:PLN03130 1454 DTPENLLSNEGsAFSKMVqSTG 1475
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
536-738 |
7.16e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 138.25 E-value: 7.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQL---LERfydPDQGKVMIDGHD----SKKVNVQFLRSNIGIVSQE---- 604
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDisslSERELARLRRRHIGFVFQFfnll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 605 PVLfacSIMDNI----KYGDNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPK 680
Cdd:COG1136 99 PEL---TALENValplLLAGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 681 ILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTIQNADIIAVMAQGVVIE 738
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
534-740 |
5.32e-36 |
|
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: 134.95 E-value: 5.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSI 612
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIKYG-----DNTKEIPmERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEA 687
Cdd:cd03259 90 AENIAFGlklrgVPKAEIR-ARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 688 TSALDTESEKTVQVALDK--AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKG 740
Cdd:cd03259 158 LSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
520-750 |
8.47e-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: 135.76 E-value: 8.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFlRSNIG 599
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-RRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPVLFA-CSIMDNIKY-----GDNTKEIPmERVIAAAKQAQLHDFvmsLPEKYETnvgsqgsqLSRGEKQRIAIAR 673
Cdd:COG4555 78 VLPDERGLYDrLTVRENIRYfaelyGLFDEELK-KRIEELIELLGLEEF---LDRRVGE--------LSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 674 AIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIA-HRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQKG 750
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
534-745 |
9.45e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.93 E-value: 9.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD--PDQ---GKVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 606
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDiyDPDVDVVELRRRVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 LFACSIMDNIKYG-----DNTKEIPMERVIAAAKQAQLHDFVmslpekyETNVGSQGSQLSRGEKQRIAIARAIVRDPKI 681
Cdd:COG1117 103 PFPKSIYDNVAYGlrlhgIKSKSELDEIVEESLRKAALWDEV-------KDRLKKSALGLSGGQQQRLCIARALAVEPEV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 682 LLLDEATSALDTESEKTVQVALDKAREgRTCIVI-------AHRLStiqnaDIIAVMAQGVVIEKGTHEEL 745
Cdd:COG1117 176 LLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
214-451 |
1.02e-35 |
|
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: 136.92 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 214 YAFLFSQILGTFSIP-------D---KEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLG 283
Cdd:cd18557 2 LLFLLISSAAQLLLPyligrliDtiiKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 284 QDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRM 363
Cdd:cd18557 82 QEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 364 LTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYR 443
Cdd:cd18557 160 IRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLW 239
|
....*...
gi 767920345 444 YGGYLISN 451
Cdd:cd18557 240 YGGYLVLS 247
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
522-734 |
1.20e-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: 131.98 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 522 FVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIV 601
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 602 SQepvlfacsimdnikygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKI 681
Cdd:cd00267 79 PQ---------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 682 LLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQNA-DIIAVMAQG 734
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1-99 |
2.62e-35 |
|
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: 134.15 E-value: 2.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQG 218
|
90
....*....|....*....
gi 767920345 81 THEELLERKGVYFTLVTLQ 99
Cdd:cd03252 219 SHDELLAENGLYAYLYQLQ 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
531-734 |
2.82e-35 |
|
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: 131.93 E-value: 2.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDG--HDSKKVNVQFLRSNIGIVSQEPVLF 608
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedLTDLEDELPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 609 A-CSIMDNIKYGdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEA 687
Cdd:cd03229 89 PhLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767920345 688 TSALDTESEKTVQVALD--KAREGRTCIVIAHRLSTIQN-ADIIAVMAQG 734
Cdd:cd03229 128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
520-748 |
3.77e-35 |
|
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: 140.42 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGKVMIDGHDSKKVNVQFLRS 596
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 597 NIGIVSQEP--VLFACSIMDNI----KYGDNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIA 670
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIaealENLGLSRAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 671 IARAIVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELMA 747
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 767920345 748 Q 748
Cdd:COG1123 233 A 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
514-749 |
7.61e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 133.58 E-value: 7.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 514 DNFQGKIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQF 593
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 594 LRSNIGIVSQEP--VLFACSIMDNIKYGDNTKEIP---MERVIA-AAKQAQLHDFVMSLPEKyetnvgsqgsqLSRGEKQ 667
Cdd:PRK13632 81 IRKKIGIIFQNPdnQFIGATVEDDIAFGLENKKVPpkkMKDIIDdLAKKVGMEDYLDKEPQN-----------LSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 668 RIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGR--TCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
....
gi 767920345 746 MAQK 749
Cdd:PRK13632 230 LNNK 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
520-731 |
1.06e-34 |
|
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: 131.83 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflrsnI 598
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 599 GIVSQEPVLFA-CSIMDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIAR 673
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKaearERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 674 AIVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLS-TIQNADIIAVM 731
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVL 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1-99 |
2.10e-34 |
|
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: 131.20 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERG 217
|
90
....*....|....*....
gi 767920345 81 THEELLERKGVYFTLVTLQ 99
Cdd:cd03253 218 THEELLAKGGLYAEMWKAQ 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
534-736 |
6.63e-34 |
|
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: 127.90 E-value: 6.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIGIVSQEPVLFA-CSI 612
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYEnLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIKYgdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqlSRGEKQRIAIARAIVRDPKILLLDEATSALD 692
Cdd:cd03230 91 RENLKL-------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767920345 693 TESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVV 736
Cdd:cd03230 128 PESRREFwELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
520-747 |
6.90e-34 |
|
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: 130.11 E-value: 6.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 599
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPVLFA-CSIMDNIKYGDNTKEIPMERVIAAAKQAqLHDfvMSLPEkyETNVGSQGSQLSRGEKQRIAIARAIVRD 678
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIALVPKLLKWPKEKIRERADEL-LAL--VGLDP--AEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 679 PKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRL-STIQNADIIAVMAQGVVIEKGTHEELMA 747
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1-99 |
7.60e-34 |
|
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: 137.54 E-value: 7.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
|
90
....*....|....*....
gi 767920345 81 THEELLERKGVYFTLVTLQ 99
Cdd:TIGR02203 550 THNELLARNGLYAQLHNMQ 568
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
534-745 |
1.02e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.91 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSI 612
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALFPhLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 688
Cdd:COG3842 95 AENVAFGLRMRGVPKaeirARVAELLELVGLEGLADRYP-----------HQLSGGQQQRVALARALAPEPRVLLLDEPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 689 SALDTESEKTVQVALDK--AREGRTCIVIAHRLS---TIqnADIIAVMAQGVVIEKGTHEEL 745
Cdd:COG3842 164 SALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
534-736 |
1.13e-33 |
|
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: 128.42 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGH--DSKKVNVQFLRSNIGIVSQEPVLF 608
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTIIIDGLklTDDKKNINELRQKVGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 609 A-CSIMDNIKYGD-NTKEIPMERVIAAAKQA----QLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKIL 682
Cdd:cd03262 89 PhLTVLENITLAPiKVKGMSKAEAEERALELlekvGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 683 LLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVV 736
Cdd:cd03262 158 LFDEPTSALDPELVGEVlDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
520-747 |
1.51e-33 |
|
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: 128.77 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNV---QFLRS 596
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 597 NIGIVSQEPVLF-ACSIMDNI-----KYGDNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIA 670
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVafplrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 671 IARAIVRDPKILLLDEATSALD-TESEKTVQVALD-KAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELMA 747
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1-99 |
4.45e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 135.15 E-value: 4.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG 560
|
90
....*....|....*....
gi 767920345 81 THEELLERKGVYFTLVTLQ 99
Cdd:PRK11176 561 THAELLAQNGVYAQLHKMQ 579
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
528-747 |
5.08e-33 |
|
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: 127.61 E-value: 5.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPSRPDSQ-VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEP- 605
Cdd:COG1124 10 SYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 606 ---------------VLFACSIMDNikygdntkeipMERVIAAAKQAQLHDfvmSLPEKYetnvgsqGSQLSRGEKQRIA 670
Cdd:COG1124 90 aslhprhtvdrilaePLRIHGLPDR-----------EERIAELLEQVGLPP---SFLDRY-------PHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 671 IARAIVRDPKILLLDEATSALDTesekTVQVA-LD-----KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHE 743
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDV----SVQAEiLNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVA 224
|
....
gi 767920345 744 ELMA 747
Cdd:COG1124 225 DLLA 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
528-748 |
5.73e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 130.20 E-value: 5.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGHDSKKVNVQFL---RSNIGI 600
Cdd:COG1135 10 TFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELraaRRKIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 601 VSQEPVLF-ACSIMDNIKY-----GDNTKEIPmERViaaakqAQLHDFVmSLPEK---YEtnvgsqgSQLSRGEKQRIAI 671
Cdd:COG1135 87 IFQHFNLLsSRTVAENVALpleiaGVPKAEIR-KRV------AELLELV-GLSDKadaYP-------SQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 672 ARAIVRDPKILLLDEATSALDTESekTVQVA--LDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELM 746
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPET--TRSILdlLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDVF 229
|
..
gi 767920345 747 AQ 748
Cdd:COG1135 230 AN 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
534-745 |
7.54e-33 |
|
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: 126.97 E-value: 7.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSkkVNVQFLRSNIGIVSQEPVLFA-CSI 612
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 688
Cdd:cd03300 90 FENIAFGLRLKKLPKaeikERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 689 SALDTESEKTVQVALDK--AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEEL 745
Cdd:cd03300 159 GALDLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1-90 |
8.04e-33 |
|
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: 126.57 E-value: 8.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:cd03254 140 LSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEG 219
|
90
....*....|
gi 767920345 81 THEELLERKG 90
Cdd:cd03254 220 THDELLAKKG 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
534-747 |
9.00e-33 |
|
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: 126.63 E-value: 9.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNV---QFLRSNIGIVSQEPVLF-A 609
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFdS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNI-----KYGDNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLL 684
Cdd:COG1127 97 LTVFENVafplrEHTDLSEAEIRELVLEKLELVGLPGAADKMP-----------SELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 685 DEATSALD--TeSEKTVQVALD-KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 747
Cdd:COG1127 166 DEPTAGLDpiT-SAVIDELIRElRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-74 |
1.60e-32 |
|
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: 123.65 E-value: 1.60e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHG 74
Cdd:cd03228 98 SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
520-734 |
2.63e-32 |
|
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: 124.12 E-value: 2.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPDSQ--VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL--ErfYDPDQGKVmidghdskkvnvqFLR 595
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSV-------------SVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 596 SNIGIVSQEPVLFACSIMDNIKYGdntKEIPMERVIAAAKQAQLH-DFVMsLPEKYETNVGSQGSQLSRGEKQRIAIARA 674
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFG---KPFDEERYEKVIKACALEpDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 675 IVRDPKILLLDEATSALDTESEKTV--QVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQG 734
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
520-736 |
5.79e-32 |
|
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: 123.75 E-value: 5.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGHDSKKVN----V 591
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSekelA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 592 QFLRSNIGIVSQE----PVLfacSIMDNIkygdntkEIPMErvIAAAKQAQLHDFVMSLPEKyetnVGSQG------SQL 661
Cdd:cd03255 78 AFRRRHIGFVFQSfnllPDL---TALENV-------ELPLL--LAGVPKKERRERAEELLER----VGLGDrlnhypSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 662 SRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIA-HRLSTIQNADIIAVMAQGVV 736
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVmELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
520-740 |
7.10e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 123.62 E-value: 7.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN---VQFLRS 596
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 597 NIGIVSQE-PVLFACSIMDNIKY-----GDNTKEIpMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIA 670
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEI-RRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 671 IARAIVRDPKILLLDEATSALDTE-SEKTVQVaLDKAREGRTCIVIA-HrlstiqNADIIAVMAQGVV-IEKG 740
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPEtSWEIMEL-LEEINRRGTTVLIAtH------DLELVDRMPKRVLeLEDG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
520-740 |
7.97e-32 |
|
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: 123.29 E-value: 7.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDS---KKVNVQFLRS 596
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 597 NIGIVSQE-PVLFACSIMDNIKY-----GDNTKEIPmERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIA 670
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFalevtGVPPREIR-KRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 671 IARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAhrlstIQNADIIAVMAQGV-VIEKG 740
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA-----THAKELVDTTRHRViALERG 212
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
197-454 |
1.63e-31 |
|
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: 124.59 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 197 MLVGSVGAAVNGTVTPLYAFLFSQILGTFsIPDKeeQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 276
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV-IPAG--DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 277 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS 356
Cdd:cd07346 78 LFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 357 GATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFI 436
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250
....*....|....*...
gi 767920345 437 ANSASYRYGGYLISNEGL 454
Cdd:cd07346 236 GTALVLLYGGYLVLQGSL 253
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
538-748 |
2.06e-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: 123.91 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN---VQFLRSN-IGIVSQEPVLFA-CSI 612
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLPhRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIKYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 688
Cdd:cd03294 120 LENVAFGLEVQGVPraerEERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 689 SALDTESEKTVQVALDK--AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:cd03294 189 SALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
537-744 |
2.08e-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: 122.83 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSIMDN 615
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 616 IKYG-----DNTKEIPmERVIAAAKQAQLHDFvmsLPEKYETnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSA 690
Cdd:cd03299 92 IAYGlkkrkVDKKEIE-RKVLEIAEMLGIDHL---LNRKPET--------LSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 691 LDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEE 744
Cdd:cd03299 160 LDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-90 |
2.61e-31 |
|
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: 129.49 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 81
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGT 554
|
....*....
gi 767920345 82 HEELLERKG 90
Cdd:COG4988 555 HEELLAKNG 563
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-96 |
2.78e-31 |
|
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: 130.83 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSkiQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 81
Cdd:TIGR03796 617 SGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
90
....*....|....*
gi 767920345 82 HEELLERKGVYFTLV 96
Cdd:TIGR03796 695 HEELWAVGGAYARLI 709
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
519-748 |
4.66e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.20 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 519 KIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNI 598
Cdd:PRK13635 5 IIRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 599 GIVSQEP--VLFACSIMDNIKYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIA 672
Cdd:PRK13635 84 GMVFQNPdnQFVGATVQDDVAFGLENIGVPreemVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 673 RAIVRDPKILLLDEATSALDTESEKTV--QVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVleTVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
519-734 |
5.15e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 122.51 E-value: 5.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 519 KIDFVDCKFTYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQFLRSN 597
Cdd:COG1116 7 ALELRGVSKRFPTGGGGvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 598 IGIVSQEPVLFA-CSIMDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIA 672
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGLELRGVPKaerrERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 673 RAIVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAH------RLstiqnADIIAVMAQG 734
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSAR 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
527-746 |
8.24e-31 |
|
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: 121.69 E-value: 8.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPV 606
Cdd:COG1120 9 VGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 L-FACSIMDNIKYG---------DNTKEipMERVIAAA-KQAQLHDFVmslpekyETNVgsqgSQLSRGEKQRIAIARAI 675
Cdd:COG1120 86 ApFGLTVRELVALGryphlglfgRPSAE--DREAVEEAlERTGLEHLA-------DRPV----DELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 676 VRDPKILLLDEATSALDtesektV--QVAL-----DKARE-GRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELM 746
Cdd:COG1120 153 AQEPPLLLLDEPTSHLD------LahQLEVlellrRLARErGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
1-99 |
2.44e-30 |
|
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: 126.74 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:TIGR02204 477 LSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQG 556
|
90
....*....|....*....
gi 767920345 81 THEELLERKGVYFTLVTLQ 99
Cdd:TIGR02204 557 THAELIAKGGLYARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-96 |
6.00e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 126.38 E-value: 6.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEvlSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMG 695
|
90
....*....|....*.
gi 767920345 81 THEELLERKGVYFTLV 96
Cdd:TIGR00958 696 THKQLMEDQGCYKHLV 711
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
520-748 |
6.82e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.84 E-value: 6.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 599
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEP--VLFACSIMDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIAR 673
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHeemkERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 674 AIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
536-745 |
6.99e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 121.72 E-value: 6.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLF-ACSIMD 614
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMVFQSYALYpHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 615 NIKYG-----DNTKEIpMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATS 689
Cdd:COG3839 95 NIAFPlklrkVPKAEI-DRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 690 ALD------TESE-KTVQvaldkAREGRTCIVIAHRLS---TIqnADIIAVMAQGVVIEKGTHEEL 745
Cdd:COG3839 163 NLDaklrveMRAEiKRLH-----RRLGTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGTPEEL 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
534-744 |
9.26e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 121.59 E-value: 9.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSI 612
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFPhMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIKYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 688
Cdd:PRK09452 104 FENVAFGLRMQKTPaaeiTPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 689 SALDTESEKTVQVALdKA--RE-GRTCIVIAH-RLSTIQNADIIAVMAQGVVIEKGTHEE 744
Cdd:PRK09452 173 SALDYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
528-748 |
9.94e-30 |
|
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: 120.16 E-value: 9.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDP---DQGKVMIDGHD----SKKVNVQFLRSNIG 599
Cdd:COG0444 10 YFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDllklSEKELRKIRGREIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPvlFAC---------SIMDNIKY-GDNTKEIPMERVIAAAKQAQLHDfvmslPEKYetnVGSQGSQLSRGEKQRI 669
Cdd:COG0444 90 MIFQDP--MTSlnpvmtvgdQIAEPLRIhGGLSKAEARERAIELLERVGLPD-----PERR---LDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 670 AIARAIVRDPKILLLDEATSALDTesekTVQVA-LD-----KAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTH 742
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDV----TIQAQiLNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPV 235
|
....*.
gi 767920345 743 EELMAQ 748
Cdd:COG0444 236 EELFEN 241
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1-99 |
2.00e-29 |
|
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: 124.68 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQhgHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:TIGR03797 589 LSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK--VTRIVIAHRLSTIRNADRIYVLDAGRVVQQG 666
|
90
....*....|....*....
gi 767920345 81 THEELLERKGVYFTLVTLQ 99
Cdd:TIGR03797 667 TYDELMAREGLFAQLARRQ 685
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
524-736 |
7.01e-29 |
|
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: 114.55 E-value: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 524 DCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVnvqflRSNIGIVSQ 603
Cdd:cd03235 4 DLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 604 EPVL---FACSIMDNIKYGDNTKEIPMERVIAAAKQA--QLHDFV-MSlpEKYETNVGsqgsQLSRGEKQRIAIARAIVR 677
Cdd:cd03235 76 RRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAKvdEALERVgLS--ELADRQIG----ELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 678 DPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVV 736
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
533-745 |
1.41e-28 |
|
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: 114.74 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 533 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CS 611
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 612 IMDNIKYGDNTKEIPmERVIAAAKQAQLHDFVM-----SLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:cd03296 91 VFDNVAFGLRVKPRS-ERPPEAEIRAKVHELLKlvqldWLADRYP-------AQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 687 ATSALDTESEKTVQVALDKARE--GRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEEL 745
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
520-745 |
1.85e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 117.17 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQL---LERfydPDQGKVMIDGHDSKkVNVQFLRS 596
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLF-TNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 597 NIGIVSQEPVLFA-CSIMDNIKYGdntkeIPMERVIAAAKQAQlhdfVMSLPEKyetnVGSQG------SQLSRGEKQRI 669
Cdd:COG1118 76 RVGFVFQHYALFPhMTVAENIAFG-----LRVRPPSKAEIRAR----VEELLEL----VQLEGladrypSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 670 AIARAIVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAH------RLstiqnADIIAVMAQGVVIEKGT 741
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRlhDELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
|
....
gi 767920345 742 HEEL 745
Cdd:COG1118 218 PDEV 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1-99 |
2.63e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 120.45 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
90
....*....|....*....
gi 767920345 81 THEELLERKGVYFTLVTLQ 99
Cdd:PRK13657 552 SFDELVARGGRFAALLRAQ 570
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
537-740 |
1.50e-27 |
|
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: 110.81 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkVN-VQFLRSNIGIVSQEPVLFA-CSIMD 614
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD---VTdLPPKDRDIAMVFQNYALYPhMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 615 NIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 690
Cdd:cd03301 92 NIAFGLKLRKVPKdeidERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767920345 691 LDTESEKTVQVALDK--AREGRTCIVIAH-RLSTIQNADIIAVMAQGVVIEKG 740
Cdd:cd03301 161 LDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
537-747 |
2.07e-27 |
|
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: 111.37 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQfLRSNIGIVS--QEPVLFA-CSIM 613
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPeLTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 614 DNI--------KYGDNTKEIPMERVIAAAKQAQLHDFVmSLPEKYETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLLD 685
Cdd:cd03219 94 ENVmvaaqartGSGLLLARARREEREARERAEELLERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920345 686 EATSAL-DTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 747
Cdd:cd03219 169 EPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
527-740 |
2.12e-27 |
|
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: 109.45 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQepv 606
Cdd:cd03214 7 VGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 lfacsimdnikygdntkeipmerviaAAKQAQLHDFVmslpekyETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:cd03214 81 --------------------------ALELLGLAHLA-------DRPF----NELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 687 ATSALDTESektvQVALDK------AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKG 740
Cdd:cd03214 124 PTSHLDIAH----QIELLEllrrlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
532-748 |
2.27e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 113.52 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 532 RPDSQV--LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN---VQFLRSNIGIVSQEPv 606
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 lFAcSIMDNIKYGD--------NTKEIPMERviaAAKQAQLHDFVMSLPEKYetnvGSQGSQLSRGEKQRIAIARAIVRD 678
Cdd:PRK11308 102 -YG-SLNPRKKVGQileeplliNTSLSAAER---REKALAMMAKVGLRPEHY----DRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 679 PKILLLDEATSALDTESEKTV-QVALDKAREGRTCIV-IAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVlNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
527-747 |
2.29e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.49 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEP- 605
Cdd:PRK13642 12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 606 -VLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKyetnvgsQGSQLSRGEKQRIAIARAIVRDPKILLL 684
Cdd:PRK13642 92 nQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTR-------EPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 685 DEATSALDTESEKTVQVALDKAREGR--TCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMA 747
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
212-449 |
2.58e-27 |
|
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: 112.73 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 212 PLYAFLFSQILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDd 291
Cdd:cd18780 16 PYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 292 lRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRD 371
Cdd:cd18780 95 -VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 372 KQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFcfaFAQCIMFIANSA---SYRYGGYL 448
Cdd:cd18780 174 QDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGG---FNGFMGAAAQLAivlVLWYGGRL 250
|
.
gi 767920345 449 I 449
Cdd:cd18780 251 V 251
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
528-745 |
4.81e-27 |
|
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: 110.35 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---SKKVNVQFLRSNIGIVSQE 604
Cdd:cd03256 9 TYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRRQIGMIFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 605 PVLFA-CSIMDNIKYGdNTKEIPMERVIA-----AAKQAQLH--DFVmSLPEKYETNVgsqgSQLSRGEKQRIAIARAIV 676
Cdd:cd03256 87 FNLIErLSVLENVLSG-RLGRRSTWRSLFglfpkEEKQRALAalERV-GLLDKAYQRA----DQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 677 RDPKILLLDEATSALDTESEKTV-QVALDKARE-GRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEEL 745
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVmDLLKRINREeGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
528-745 |
7.48e-27 |
|
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: 109.13 E-value: 7.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPSRPdSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIGIVSQEPVL 607
Cdd:cd03263 9 TYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 608 F-ACSIMDNIKY-----GDNTKEIPMErviaaakQAQLHDfVMSLPEKYETNVGsqgsQLSRGEKQRIAIARAIVRDPKI 681
Cdd:cd03263 87 FdELTVREHLRFyarlkGLPKSEIKEE-------VELLLR-VLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 682 LLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 745
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
527-761 |
1.08e-26 |
|
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: 117.35 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYpSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvnvqflrsNIGIVSQEPV 606
Cdd:TIGR00957 644 FTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAW 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 LFACSIMDNIKYGDNTKEIPMERVIAAAkqAQLHDFVMsLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:TIGR00957 710 IQNDSLRENILFGKALNEKYYQQVLEAC--ALLPDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 687 ATSALDTESEKTV---QVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTGSP 761
Cdd:TIGR00957 787 PLSAVDAHVGKHIfehVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAP 864
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1-762 |
1.37e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 117.19 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNE-SEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVER 79
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFS 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 80 GTHEELLeRKGVYFTLVTlQSQGNQALNEEDiKDATEDDMLArtfSRGSYQDSLRASIRQRSKSQLSYLVHEPPlavVDH 159
Cdd:PTZ00243 863 GSSADFM-RTSLYATLAA-ELKENKDSKEGD-ADAEVAEVDA---APGGAVDHEPPVAKQEGNAEGGDGAALDA---AAG 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 160 KSTYEEDRKDKDIPVQEEVE--------PAPVRRILKFSAPE--------WPYMLvgSVGAAVNGTVTPLYAFLFSQILG 223
Cdd:PTZ00243 934 RLMTREEKASGSVPWSTYVAylrfcgglHAAGFVLATFAVTElvtvssgvWLSMW--STRSFKLSAATYLYVYLGIVLLG 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 224 TFSIPDKEEqrsqingVCLLFVAMGCVSLFTQFLQGYAFAKsgelltkrlrkfgframlgqdIAWFDdlRNSPGALTTRL 303
Cdd:PTZ00243 1012 TFSVPLRFF-------LSYEAMRRGSRNMHRDLLRSVSRGT---------------------MSFFD--TTPLGRILNRF 1061
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 304 ATDAsqvqGAAGSQIGMIVNSFTNVTVAM---IIAFSFSWKLSLVIL--CFFPFLAL-----SGATQTRMLTGFASRDkq 373
Cdd:PTZ00243 1062 SRDI----DILDNTLPMSYLYLLQCLFSIcssILVTSASQPFVLVALvpCGYLYYRLmqfynSANREIRRIKSVAKSP-- 1135
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 374 alemVGQITNEALSNIRTVAGIGKERRFI-EALEtELEKPFKTAIQK--------------ANIYGFCFAFAQCIMFIAN 438
Cdd:PTZ00243 1136 ----VFTLLEEALQGSATITAYGKAHLVMqEALR-RLDVVYSCSYLEnvanrwlgvrveflSNIVVTVIALIGVIGTMLR 1210
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 439 SASYRYGgyLIS---------NEGLhfSYVFRVISAVVLSATALGRAFSYTPSYAKAKISA--ARFFQLLDRQ------- 500
Cdd:PTZ00243 1211 ATSQEIG--LVSlsltmamqtTATL--NWLVRQVATVEADMNSVERLLYYTDEVPHEDMPEldEEVDALERRTgmaadvt 1286
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 501 -----PPISVYNTAGEkwdNFQ-GKIDFVDCKFTY----PsrpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLER 570
Cdd:PTZ00243 1287 gtvviEPASPTSAAPH---PVQaGSLVFEGVQMRYreglP-----LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMR 1358
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 571 FYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKY 650
Cdd:PTZ00243 1359 MVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGI 1435
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 651 ETNVGSQGSQLSRGEKQRIAIARAIV-RDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIA 729
Cdd:PTZ00243 1436 DSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKII 1515
|
810 820 830
....*....|....*....|....*....|....
gi 767920345 730 VMAQGVVIEKGTHEEL-MAQKGAYYKLVTTGSPI 762
Cdd:PTZ00243 1516 VMDHGAVAEMGSPRELvMNRQSIFHSMVEALGRS 1549
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
538-748 |
1.51e-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: 114.78 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFyDPDQGKVMIDGHD----SKKVNvQFLRSNIGIVSQEPvlFAC--- 610
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDldglSRRAL-RPLRRRMQVVFQDP--FGSlsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 --SIMDNIKYGDNTKEIPM------ERVIAAAKQAQLHDFVMslpEKYETnvgsqgsQLSRGEKQRIAIARAIVRDPKIL 682
Cdd:COG4172 378 rmTVGQIIAEGLRVHGPGLsaaerrARVAEALEEVGLDPAAR---HRYPH-------EFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 683 LLDEATSALDteseKTVQ---VALDK---AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:COG4172 448 VLDEPTSALD----VSVQaqiLDLLRdlqREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
531-748 |
1.71e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 110.98 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQV--LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD----SKKVNVQfLRSNIGIVSQE 604
Cdd:COG4608 25 GRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitglSGRELRP-LRRRMQMVFQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 605 PvlFAC-----SIMDNIK-----YGDNTKEIPMERViaaakqAQLHDFVMSLPEKYETNVGsqgsQLSRGEKQRIAIARA 674
Cdd:COG4608 104 P--YASlnprmTVGDIIAeplriHGLASKAERRERV------AELLELVGLRPEHADRYPH----EFSGGQRQRIGIARA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 675 IVRDPKILLLDEATSALDteseKTVQ---VAL--D-KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 747
Cdd:COG4608 172 LALNPKLIVCDEPVSALD----VSIQaqvLNLleDlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYA 247
|
.
gi 767920345 748 Q 748
Cdd:COG4608 248 R 248
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
527-748 |
2.63e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 108.25 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVnvqflRSNIGIVSQEPV 606
Cdd:COG1121 14 VSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 L---FACSIMDNIKYGdNTKEIPM---------ERVIAAAKQAQLHDFVmslpekyetnvGSQGSQLSRGEKQRIAIARA 674
Cdd:COG1121 86 VdwdFPITVRDVVLMG-RYGRRGLfrrpsradrEAVDEALERVGLEDLA-----------DRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 675 IVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEkGTHEELMAQ 748
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLLNRGLVAH-GPPEEVLTP 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
533-737 |
3.56e-26 |
|
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: 105.20 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 533 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvnvqflrsnigivsqEPVLFAcSI 612
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFA-SP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIKYGdntkeipmervIAaakqaqlhdFVMslpekyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSAL- 691
Cdd:cd03216 70 RDARRAG-----------IA---------MVY---------------QLSVGERQMVEIARALARNARLLILDEPTAALt 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767920345 692 DTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVI 737
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
231-455 |
3.66e-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: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 231 EEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQV 310
Cdd:cd18572 29 DGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 311 qgaaGSQIGMIVNSFTN----VTVAMIIAFSFSWKLSLVILCFFPFLALS----GATQTRMltgfASRDKQALEMVGQIT 382
Cdd:cd18572 107 ----SDPLSTNLNVFLRnlvqLVGGLAFMFSLSWRLTLLAFITVPVIALItkvyGRYYRKL----SKEIQDALAEANQVA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 383 NEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLH 455
Cdd:cd18572 179 EEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMS 251
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
524-734 |
5.20e-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: 106.19 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 524 DCKFTYpsRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNVQFLRSNIGIVSQ 603
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 604 EP--VLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKI 681
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 682 LLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQG 734
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVgELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANG 202
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
520-757 |
5.21e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.28 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 599
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEP--VLFACSIMDNIKYGD-----NTKEIpMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIA 672
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPvnmglDKDEV-ERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 673 RAIVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKG-----THEEL 745
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDI 230
|
250
....*....|..
gi 767920345 746 MAQKGAYYKLVT 757
Cdd:PRK13647 231 VEQAGLRLPLVA 242
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-104 |
5.81e-26 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 113.27 E-value: 5.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQG 556
|
90 100
....*....|....*....|....
gi 767920345 81 THEELLERKGVYFTLVTLQSQGNQ 104
Cdd:PRK10790 557 THQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
534-746 |
8.01e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.17 E-value: 8.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD--PD---QGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 606
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 LFACSIMDNIKYG-----DNTKEIPMERVIAAAKQAQLHDFVMSlpEKYETNVGsqgsqLSRGEKQRIAIARAIVRDPKI 681
Cdd:PRK14239 97 PFPMSIYENVVYGlrlkgIKDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 682 LLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRL---STIqnADIIAVMAQGVVIEKG-THEELM 746
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNdTKQMFM 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
536-740 |
8.09e-26 |
|
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: 105.91 E-value: 8.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIGIVSQEPVLFA-CSIMD 614
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDrLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 615 NIKY--------GDNTKEipmeRVIAAAKQAQLHDFVmslpekyETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:cd03266 98 NLEYfaglyglkGDELTA----RLEELADRLGMEELL-------DRRVGG----FSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 687 ATSALDTESEKTVQVALDKAREGRTCIVIA-HRLSTIQN-ADIIAVMAQGVVIEKG 740
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
520-749 |
8.99e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.47 E-value: 8.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFL--RSN 597
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 598 IGIVSQEP--VLFACSIMDNIKYGDNTKEIPME----RVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAI 671
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLGLSKEevekRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 672 ARAIVRDPKILLLDEATSALDTE-SEKTVQVALDKAREGRTCIVIAHRLSTIQ-NADIIAVMAQGVVIEKGTHEELMAQK 749
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
534-746 |
9.60e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 106.72 E-value: 9.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLFA-C 610
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvnDPKVDERLIRQEAGMVFQQFYLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 SIMDNIKYGdntkeiPMeRVIAAAKqAQLHDFVMSLPEK--YETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEAT 688
Cdd:PRK09493 93 TALENVMFG------PL-RVRGASK-EEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 689 SALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELM 746
Cdd:PRK09493 165 SALDPELRHEVlKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
538-748 |
1.21e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.73 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGHDSKKVNVQFLRS---NIGIVSQEPVLFAC- 610
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMIFQHFNLLSSr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 SIMDNIKygdntkeIPMErvIAAAKQAQLHDFVMSLPE---------KYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKI 681
Cdd:PRK11153 98 TVFDNVA-------LPLE--LAGTPKAEIKARVTELLElvglsdkadRYP-------AQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 682 LLLDEATSALDTEsekTVQVALDKARE-----GRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:PRK11153 162 LLCDEATSALDPA---TTRSILELLKDinrelGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGTVSEVFSH 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
531-730 |
1.34e-25 |
|
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: 104.87 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFlRSNIGIVSQEPVLF-A 609
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNIK-----YGDntkEIPMERVIAAAKQAQLHDFvMSLPekyetnvgsqGSQLSRGEKQRIAIARAIVRDPKILLL 684
Cdd:COG4133 90 LTVRENLRfwaalYGL---RADREAIDEALEAVGLAGL-ADLP----------VRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767920345 685 DEATSALDTESEKTVQVALDKAREGRTCIVIA-HRLSTIQNADIIAV 730
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
547-740 |
1.52e-25 |
|
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: 105.07 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 547 PGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDG---HDS-KKVNVQFLRSNIGIVSQEPVLFA-CSIMDNIKYGDN 621
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSrKKINLPPQQRKIGLVFQQYALFPhLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 622 TKEiPMERVIAAAKQAQLHDfVMSLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQV 701
Cdd:cd03297 102 RKR-NREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767920345 702 ALDK--AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 740
Cdd:cd03297 173 ELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
542-748 |
3.23e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.84 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 542 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnvqFLRSNIG-----IVSQEPVLFA-CSIMDN 615
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-------LTALPPAerpvsMLFQENNLFPhLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 616 I--------KYGDNTKEipmeRVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEA 687
Cdd:COG3840 92 IglglrpglKLTAEQRA----QVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 688 TSALD----TESEKTV-QVAldkAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:COG3840 157 FSALDpalrQEMLDLVdELC---RERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
194-749 |
6.53e-25 |
|
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: 111.54 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 194 WPYMLVGSV--GAAVNGTVTPLyafLFSQILGTFSiPDKEEQRSQIN----GVCLLFVAMgcvslfTQFLQGYAFAKSGE 267
Cdd:TIGR01271 80 WRFVFYGILlyFGEATKAVQPL---LLGRIIASYD-PFNAPEREIAYylalGLCLLFIVR------TLLLHPAIFGLHHL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 268 LLTKRLRKFG--FRAMLGQDIAWFDDLrnSPGALTTRLATDASQVQGaagsqiGMIVNSFTNVT-VAMIIAFSFSWKL-- 342
Cdd:TIGR01271 150 GMQMRIALFSliYKKTLKLSSRVLDKI--STGQLVSLLSNNLNKFDE------GLALAHFVWIApLQVILLMGLIWELle 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 343 --SLVILCFFPFLALSGATQTRMLTGFasRDKQAlEMVGQ---ITNEALSNIRTVAGIGKErrfiEALETELEKPFKTAI 417
Cdd:TIGR01271 222 vnGFCGLGFLILLALFQACLGQKMMPY--RDKRA-GKISErlaITSEIIENIQSVKAYCWE----EAMEKIIKNIRQDEL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 418 QKANIYGFCFAFaqcimfiaNSASYRYGGYLIS---------NEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKI 488
Cdd:TIGR01271 295 KLTRKIAYLRYF--------YSSAFFFSGFFVVflsvvpyalIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 489 SAARFFQ-LLDRQPPISV-YN-TAGE--------KWDNFQGKIdFVDCK----------------FTYPSRPDSQVLNGL 541
Cdd:TIGR01271 367 GAITKIQdFLCKEEYKTLeYNlTTTEvemvnvtaSWDEGIGEL-FEKIKqnnkarkqpngddglfFSNFSLYVTPVLKNI 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 542 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvnvqflrsnIGIVSQEPVLFACSIMDNIKYGDN 621
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGLS 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 622 TKEIPMERVIAAAkqaQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV-Q 700
Cdd:TIGR01271 513 YDEYRYTSVIKAC---QLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfE 589
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 767920345 701 VALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQK 749
Cdd:TIGR01271 590 SCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
536-740 |
9.18e-25 |
|
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: 102.68 E-value: 9.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdSKKVNVQFLRSNIGIVSQEPVLF-ACSIMD 614
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG--KSYQKNIEALRRIGALIEAPGFYpNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 615 NIKYGDNTKEIPMERViaaakqAQLHDFV-MSLPEKYETnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDT 693
Cdd:cd03268 92 NLRLLARLLGIRKKRI------DEVLDVVgLKDSAKKKV------KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767920345 694 ESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 740
Cdd:cd03268 160 DGIKELrELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
521-748 |
9.82e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 106.34 E-value: 9.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 521 DFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGI 600
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 601 VSQEPVLFA-CSIMDNIKYGDNTKEIPMERVIAAAKQA-QLHDFVmSLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRD 678
Cdd:PRK11432 83 VFQSYALFPhMSLGENVGYGLKMLGVPKEERKQRVKEAlELVDLA-GFEDRYV-------DQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 679 PKILLLDEATSALDTESEKTVQvalDKARE-----GRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMR---EKIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
534-744 |
1.30e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.36 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEP--VLFA 609
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNIKYGD-----NTKEIpMERVIAAAKQAQLhdfvmslpeKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLL 684
Cdd:PRK13637 99 ETIEKDIAFGPinlglSEEEI-ENRVKRAMNIVGL---------DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 685 DEATSALDTESEKTV--QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEE 744
Cdd:PRK13637 169 DEPTAGLDPKGRDEIlnKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
216-451 |
1.40e-24 |
|
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: 104.52 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 216 FLFSQILGTFS--IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlR 293
Cdd:cd18573 17 FAIGKLIDVASkeSGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD--K 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 294 NSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQ 373
Cdd:cd18573 95 NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 374 ALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQcimFIANSASYR---YGGYLIS 450
Cdd:cd18573 175 ALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTG---FSGNLSLLSvlyYGGSLVA 251
|
.
gi 767920345 451 N 451
Cdd:cd18573 252 S 252
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
520-745 |
1.82e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.68 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 599
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPV-LFACSIMD-NIKYGDNTKEIPMERVIAAAKQAqLHDFVMSLPEKYETNvgsqgsQLSRGEKQRIAIARAIVR 677
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRRVSEA-LKQVDMLERADYEPN------ALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 678 DPKILLLDEATSALDTESEKTVQVALDKAREGR--TCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
535-743 |
2.26e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 102.79 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 535 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---SKKVN---VQFLRSNIGIVSQE---- 604
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSdkaIRELRRNVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 605 PVLfacSIMDN-----IKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDP 679
Cdd:PRK11124 95 PHL---TVQQNlieapCRVLGLSKDQALARAEKLLERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 680 KILLLDEATSALDTE-SEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHE 743
Cdd:PRK11124 161 QVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
532-723 |
3.39e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.59 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 532 RPDSQVL-NGLSVSISPGQTLAFVGSSGCGKST--------------SIQLlerfydPDQGKVMidghdskkvnvqFLrs 596
Cdd:COG4178 372 TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTllraiaglwpygsgRIAR------PAGARVL------------FL-- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 597 nigivSQEPVLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEkyetnVGSQGSQLSRGEKQRIAIARAIV 676
Cdd:COG4178 432 -----PQRPYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAERLDE-----EADWDQVLSLGEQQRLAFARLLL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767920345 677 RDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQ 723
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAA 548
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-98 |
4.09e-24 |
|
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: 107.54 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
90
....*....|....*...
gi 767920345 81 THEELLERKGVYFTLVTL 98
Cdd:COG4987 552 THEELLAQNGRYRQLYQR 569
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
536-747 |
4.29e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.14 E-value: 4.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKV-----MIDGHDS---KKVNVQFLRSNIGIVSQE 604
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ---PEAGTIrvgdiTIDTARSlsqQKGLIRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 605 PVLFAC-SIMDNIKYGDN-TKEIPMERVIAAAKQaqlhdfvmsLPEKyetnVGSQGSQ------LSRGEKQRIAIARAIV 676
Cdd:PRK11264 94 FNLFPHrTVLENIIEGPViVKGEPKEEATARARE---------LLAK----VGLAGKEtsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 677 RDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 747
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
519-749 |
4.46e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.94 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 519 KIDFVDCKFTY-PSRP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDG----HDSKKVNVQ 592
Cdd:PRK13646 2 TIRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 593 FLRSNIGIVSQ--EPVLFACSIMDNIKYGDNTKEIPMERVIAAAkqaqlHDFVMSLpeKYETNVGSQGS-QLSRGEKQRI 669
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-----HRLLMDL--GFSRDVMSQSPfQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 670 AIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAR--EGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELM 746
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELF 234
|
...
gi 767920345 747 AQK 749
Cdd:PRK13646 235 KDK 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
527-740 |
7.48e-24 |
|
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: 100.35 E-value: 7.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYPSRpdsQVLNGLSVSISPGQTlAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIGIVSQEPV 606
Cdd:cd03264 8 KRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 LFA-CSIMDNIKYGDNTKEIP----MERVIAAAKQAQLHDFvmslpekYETNVGSqgsqLSRGEKQRIAIARAIVRDPKI 681
Cdd:cd03264 83 VYPnFTVREFLDYIAWLKGIPskevKARVDEVLELVNLGDR-------AKKKIGS----LSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 682 LLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 740
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
517-745 |
7.98e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.14 E-value: 7.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 517 QGKIDFVDCKFTYPsrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD--PD---QGKVMIDGHDSKKVNV 591
Cdd:PRK14247 1 MNKIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 592 QFLRSNIGIVSQEP-VLFACSIMDNIKYG-------DNTKEIpMERVIAAAKQAQLHDFVmslpekyETNVGSQGSQLSR 663
Cdd:PRK14247 78 IELRRRVQMVFQIPnPIPNLSIFENVALGlklnrlvKSKKEL-QERVRWALEKAQLWDEV-------KDRLDAPAGKLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 664 GEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAH------RLStiqnaDIIAVMAQGVVI 737
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIV 224
|
....*...
gi 767920345 738 EKGTHEEL 745
Cdd:PRK14247 225 EWGPTREV 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
542-746 |
9.74e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 104.34 E-value: 9.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 542 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS----NIGIVSQEPVLFA-CSIMDNI 616
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 617 KYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 692
Cdd:PRK10070 128 AFGMELAGINaeerREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 693 TESEKTVQVALDK--AREGRTCIVIAHRL-STIQNADIIAVMAQGVVIEKGTHEELM 746
Cdd:PRK10070 197 PLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
536-745 |
1.45e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.10 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQF------LRSNIGIVSQEPVLFA 609
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP-----VRFrsprdaQAAGIAIIHQELNLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 C-SIMDNIKYGDNTKE---IPMERVIAAAKQAqLHDFVMSLPEkyETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLLD 685
Cdd:COG1129 93 NlSVAENIFLGREPRRgglIDWRAMRRRAREL-LARLGLDIDP--DTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 686 EATSAL-DTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 745
Cdd:COG1129 166 EPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
535-749 |
1.47e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.46 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 535 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH--DSKKVNVQFLRSNIGIVSQEP--VLFAC 610
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQDPdnQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 SIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKyetnvgsQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 690
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 691 LDTES-EKTVQVALDKARE-GRTCIVIAHRLSTIQ-NADIIAVMAQGVVIEKGTHEELMAQK 749
Cdd:PRK13636 172 LDPMGvSEIMKLLVEMQKElGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-74 |
1.48e-23 |
|
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: 99.85 E-value: 1.48e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHG 74
Cdd:cd03248 151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
534-745 |
1.76e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.51 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERF---YDPD---QGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL 607
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 608 FA-CSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDfvMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:PRK14246 102 FPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRK--VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 687 ATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
534-743 |
2.71e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIM 613
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 614 DNIKYgdnTKEIPMERVIAAAKQAQLHDFvmSLPEK-YETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 692
Cdd:PRK10247 99 DNLIF---PWQIRNQQPDPAIFLDDLERF--ALPDTiLTKNI----AELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767920345 693 TESEKTVQVALDK-AREGRTCIV-IAHRLSTIQNAD-IIAVMAQGVVIEKGTHE 743
Cdd:PRK10247 170 ESNKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADkVITLQPHAGEMQEARYE 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
538-719 |
3.14e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.86 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD-----PDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLFAC 610
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 SIMDNIKYGD--NTKEIPM-ERVIAAAKQAQLHDFVmslPEKYETNvgsqGSQLSRGEKQRIAIARAIVRDPKILLLDEA 687
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMdELVERSLRQAALWDEV---KDKLKQS----GLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|..
gi 767920345 688 TSALDTESEKTVQVALDKAREGRTCIVIAHRL 719
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
520-745 |
3.26e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 100.26 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGKVMIDGHDSKKVNVQFLRS 596
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 597 NIGIVSQEP--VLFACSIMDNIKYGDNTKEIP---MERVIA-AAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIA 670
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPrpeMIKIVRdVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 671 IARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
534-745 |
3.72e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.22 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQ-VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNvQFLRSnIGIVSQEPVLFA-CS 611
Cdd:PRK11607 30 DGQhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRP-INMMFQSYALFPhMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 612 IMDNIKYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEA 687
Cdd:PRK11607 108 VEQNIAFGLKQDKLPkaeiASRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 688 TSALDTESEKTVQVALDK--AREGRTCIVIAH-RLSTIQNADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
534-740 |
5.78e-23 |
|
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: 5.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvNVQFL-RSNIGIVSQEPVLF-ACS 611
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-----PLDIAaRNRIGYLPEERGLYpKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 612 IMDNIKYGDNTKEIPMErviAAAKQAQ--LHDFvmSLPEKYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATS 689
Cdd:cd03269 87 VIDQLVYLAQLKGLKKE---EARRRIDewLERL--ELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767920345 690 ALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 740
Cdd:cd03269 158 GLDPVNVELLkDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
541-741 |
7.65e-23 |
|
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: 97.18 E-value: 7.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 541 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSIMDNIKYG 619
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 620 DNT----KEIPMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALDT-- 693
Cdd:cd03298 95 LSPglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPal 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767920345 694 ESEKTVQVALDKAREGRTCIVIAHrlstiQNADIIAVMAQGVVIEKGT 741
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLMVTH-----QPEDAKRLAQRVVFLDNGR 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
535-745 |
1.20e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.16 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 535 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSIM 613
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRhMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 614 DNIKYGdnTKEIPM-ERVIAAA---KQAQLHDFVM--SLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEA 687
Cdd:PRK10851 93 DNIAFG--LTVLPRrERPNAAAikaKVTQLLEMVQlaHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 688 TSALDTESEKTVQVALDKARE--GRTCIVIAH-RLSTIQNADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
520-740 |
1.35e-22 |
|
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: 96.08 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPDS---QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL--ERFYDPDQGKVMIDGHDSKKVNvqfL 594
Cdd:cd03213 4 LSFRNLTVTVKSSPSKsgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRS---F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 595 RSNIGIVSQEPVLFAC-SIMDNIKYgdntkeipmerviaaakQAQLhdfvmslpekyetnvgsqgSQLSRGEKQRIAIAR 673
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMF-----------------AAKL-------------------RGLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 674 AIVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLST--IQNADIIAVMAQGVVIEKG 740
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
527-722 |
1.38e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.19 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYPSRpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD-----QGKVMIDGHD--SKKVNVQFLRSNIG 599
Cdd:PRK14258 15 FYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNiyERRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPVLFACSIMDNIKYGDNT----KEIPMERVIAAA-KQAQLHDFVmslpekyETNVGSQGSQLSRGEKQRIAIARA 674
Cdd:PRK14258 92 MVHPKPNLFPMSVYDNVAYGVKIvgwrPKLEIDDIVESAlKDADLWDEI-------KHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767920345 675 IVRDPKILLLDEATSALDTESEKTVQ--VALDKAREGRTCIVIAHRLSTI 722
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVEslIQSLRLRSELTMVIVSHNLHQV 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
534-745 |
1.96e-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: 96.28 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD----SKKVnvqflRSNIGIVSQEPVLfa 609
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvvrePREV-----RRRIGIVFQDLSV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 csimDNIKYGDNTKEI-----PMERVIAAAKQAQLHDFvMSLPEKYETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLL 684
Cdd:cd03265 85 ----DDELTGWENLYIharlyGVPGAERRERIDELLDF-VGLLEAADRLVKT----YSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920345 685 DEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEEL 745
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-98 |
2.44e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 103.19 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRAADTIIGFEH----G 74
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtG 1438
|
90 100
....*....|....*....|....*.
gi 767920345 75 TAVE-RGTHEELLE-RKGVYFTLVTL 98
Cdd:PTZ00265 1439 SFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
534-747 |
4.06e-22 |
|
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: 95.58 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFA-CS 611
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPHERARAGIGYVPEGRRIFPeLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 612 IMDNIKYGdntkeipMERVIAAAKQAQLhDFVMSL-PEKYEtNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 690
Cdd:cd03224 92 VEENLLLG-------AYARRRAKRKARL-ERVYELfPRLKE-RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 691 LdteSEKTVQV---ALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 747
Cdd:cd03224 163 L---APKIVEEifeAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
525-745 |
7.33e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.23 E-value: 7.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 525 CKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMI---------------DGHDSKKV 589
Cdd:PRK13631 29 CVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnheliTNPYSKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 590 -NVQFLRSNIGIVSQEP--VLFACSIMDNIKYGDNTKEIPMERviaAAKQAQLHDFVMSLPEKYetnVGSQGSQLSRGEK 666
Cdd:PRK13631 109 kNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYLNKMGLDDSY---LERSPFGLSGGQK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 667 QRIAIARAIVRDPKILLLDEATSALDTESEK-TVQVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEE 744
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYE 262
|
.
gi 767920345 745 L 745
Cdd:PRK13631 263 I 263
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
531-748 |
1.01e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 95.67 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFL---------------- 594
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRckhirmifqdpntsln 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 595 -RSNIGIVSQEPVLFacsimdnikygdNTKEIPMER---VIAAAKQAQLhdfvmsLPEkyETNVGSQgsQLSRGEKQRIA 670
Cdd:COG4167 102 pRLNIGQILEEPLRL------------NTDLTAEEReerIFATLRLVGL------LPE--HANFYPH--MLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 671 IARAIVRDPKILLLDEATSALDTeSEKT--VQVALD-KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELM 746
Cdd:COG4167 160 LARALILQPKIIIADEALAALDM-SVRSqiINLMLElQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVF 238
|
..
gi 767920345 747 AQ 748
Cdd:COG4167 239 AN 240
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-86 |
1.33e-21 |
|
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: 94.18 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
....*....
gi 767920345 78 ERGTHEELL 86
Cdd:cd03258 221 EEGTVEEVF 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
536-747 |
1.92e-21 |
|
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: 94.34 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD--SKKVnvqFLRSNIGIVS--QEPVLFA-C 610
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitGLPP---HRIARLGIARtfQNPRLFPeL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 SIMDNI------KYGDNTKEIPMERVIAAAKQAQLHDFVMS------LPEKYETNVGSqgsqLSRGEKQRIAIARAIVRD 678
Cdd:COG0411 95 TVLENVlvaahaRLGRGLLAALLRLPRARREEREARERAEEllervgLADRADEPAGN----LSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 679 PKILLLDEATSAL-DTESEKTVQVALD-KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 747
Cdd:COG0411 171 PKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
536-738 |
2.15e-21 |
|
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: 94.49 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN----------VQFL----------R 595
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqrrafrrdVQLVfqdspsavnpR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 596 SNIGIVSQEPvlfacsiMDNIKYGDNTKEipMERVIAAAKQAQLHDFVMS-LPEkyetnvgsqgsQLSRGEKQRIAIARA 674
Cdd:TIGR02769 105 MTVRQIIGEP-------LRHLTSLDESEQ--KARIAELLDMVGLRSEDADkLPR-----------QLSGGQLQRINIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 675 IVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIE 738
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-76 |
2.70e-21 |
|
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: 91.51 E-value: 2.70e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTVRAADTIIGFEHGTA 76
Cdd:cd03246 98 SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-81 |
2.86e-21 |
|
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: 92.94 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 81
Cdd:cd03244 141 SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
534-745 |
3.02e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 93.75 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQ-----GKVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 606
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNiySPDVDPIEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 LFA-CSIMDNIKYG-------DNTKEIPmERVIAAAKQAQLHDFVMSLPEKYETNvgsqgsqLSRGEKQRIAIARAIVRD 678
Cdd:PRK14267 96 PFPhLTIYDNVAIGvklnglvKSKKELD-ERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 679 PKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHrlSTIQNA---DIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-118 |
3.58e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 98.25 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRG 531
|
90 100 110
....*....|....*....|....*....|....*...
gi 767920345 81 THEELLERKGVYFTLVTLQsQGNQALNEEDIKDATEDD 118
Cdd:PRK10789 532 NHDQLAQQSGWYRDMYRYQ-QLEAALDDAPEIREEAVD 568
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
197-417 |
4.51e-21 |
|
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: 94.41 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 197 MLVGSVGAAVNGTVTPLYAFLFSQILGTFSIpdkEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 276
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFV---EKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 277 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALs 356
Cdd:cd18552 78 LFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 357 gatqtrmLTGFASR-----DKQALEMVGQITN---EALSNIRTVAGIGKERRFIEALETELEKPFKTAI 417
Cdd:cd18552 155 -------PIRRIGKrlrkiSRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSM 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
520-746 |
5.04e-21 |
|
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: 93.23 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGK-VMIDGHDSKKVNVQFLRSNI 598
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 599 GIVSQEpvlfacsIMDNIKYGDNTKEI--------------PMERVIAAAKQAqLHDFVMSlpEKYETNVGSqgsqLSRG 664
Cdd:COG1119 81 GLVSPA-------LQLRFPRDETVLDVvlsgffdsiglyrePTDEQRERAREL-LELLGLA--HLADRPFGT----LSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 665 EKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIV-IAHRLStiqnaDIIA------VMAQGVV 736
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPgithvlLLKDGRV 221
|
250
....*....|
gi 767920345 737 IEKGTHEELM 746
Cdd:COG1119 222 VAAGPKEEVL 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-88 |
6.86e-21 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 92.36 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKIQH----GHTIISVAHRLSTVR-AADTIIGFEHGTA 76
Cdd:COG1126 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLDVMRDlakeGMTMVVVTHEMGFAReVADRVVFMDGGRI 214
|
90
....*....|..
gi 767920345 77 VERGTHEELLER 88
Cdd:COG1126 215 VEEGPPEEFFEN 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
536-748 |
9.27e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 92.72 E-value: 9.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-------------SKKVNVQFLRSNIGIVS 602
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 603 QEPVLFacSIMDNIkygDNTKEIPMErVIAAAKQAQLHDFVmslpeKYETNVG----SQG---SQLSRGEKQRIAIARAI 675
Cdd:PRK10619 99 QHFNLW--SHMTVL---ENVMEAPIQ-VLGLSKQEARERAV-----KYLAKVGiderAQGkypVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 676 VRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
521-748 |
9.54e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 93.23 E-value: 9.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 521 DFVDCK---FTYPSRPDSQ---VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKV-NVQF 593
Cdd:PRK13633 3 EMIKCKnvsYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 594 LRSNIGIVSQEP--VLFACSIMDNIKYGDNTKEIPME----RVIAAAKQAQLHDFvmslpEKYETNVgsqgsqLSRGEKQ 667
Cdd:PRK13633 83 IRNKAGMVFQNPdnQIVATIVEEDVAFGPENLGIPPEeireRVDESLKKVGMYEY-----RRHAPHL------LSGGQKQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 668 RIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
...
gi 767920345 746 MAQ 748
Cdd:PRK13633 232 FKE 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
552-748 |
1.35e-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: 94.01 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 552 AFVGSSGCGKSTSIQL---LERfydPDQGKVMIDGH---DSKKVnvQFL---RSNIGIVSQEPVLFA-CSIMDNIKYGdn 621
Cdd:COG4148 29 ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqDSARG--IFLpphRRRIGYVFQEARLFPhLSVRGNLLYG-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 622 tkeipMERVIAAAKQAQLHDfVMSL----------PEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 691
Cdd:COG4148 102 -----RKRAPRAERRISFDE-VVELlgighlldrrPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 692 DTESEKTVQVALDK-AREGRTCIV-IAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:COG4148 165 DLARKAEILPYLERlRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-88 |
1.55e-20 |
|
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: 95.74 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
90
....*....|.
gi 767920345 78 ERGTHEELLER 88
Cdd:COG1123 485 EDGPTEEVFAN 495
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
536-763 |
1.87e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.48 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNvqflRSNIGIVSQEPVLFA-CSIMD 614
Cdd:COG4152 15 TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYPkMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 615 NIKYgdntkeipmerviaaakQAQLHDfvMS----------------LPEKYETNVGSqgsqLSRGEKQRIAIARAIVRD 678
Cdd:COG4152 91 QLVY-----------------LARLKG--LSkaeakrradewlerlgLGDRANKKVEE----LSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 679 PKILLLDEATSALDTES-EKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQKGAYYKLV 756
Cdd:COG4152 148 PELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRL 227
|
....*..
gi 767920345 757 TTGSPIS 763
Cdd:COG4152 228 EADGDAG 234
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-97 |
1.94e-20 |
|
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: 96.35 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHgHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:TIGR01193 612 ISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQG 690
|
90
....*....|....*..
gi 767920345 81 THEELLERKGVYFTLVT 97
Cdd:TIGR01193 691 SHDELLDRNGFYASLIH 707
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
520-749 |
2.01e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.20 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTY-PSRP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH----DSKKVNVQF 593
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 594 LRSNIGIVSQ--EPVLFACSIMDNIKYGDN----TKEIPMERVIAAAKQAQLHDFVMSlpekyetnvgSQGSQLSRGEKQ 667
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKnfgfSEDEAKEKALKWLKKVGLSEDLIS----------KSPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 668 RIAIARAIVRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
....
gi 767920345 746 MAQK 749
Cdd:PRK13641 233 FSDK 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
528-748 |
2.42e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.79 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEP-- 605
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 606 VLFACSIMDNIKYGDNT----KEIPMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKI 681
Cdd:PRK13652 90 QIFSPTVEQDIAFGPINlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 682 LLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
537-738 |
2.53e-20 |
|
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: 90.57 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQL---LERfydPDQGKVMIDGHDSKKVN----VQFLRSNIGIVSQE----P 605
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfqllP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 606 VLFAcsiMDNIkygdntkEIPMErvIAAAKQAQlhdfvmSLPEKYETNVGSQG------SQLSRGEKQRIAIARAIVRDP 679
Cdd:COG4181 104 TLTA---LENV-------MLPLE--LAGRRDAR------ARARALLERVGLGHrldhypAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 680 KILLLDEATSALDTESEKTVQVAL-DKARE-GRTCIVIAHRLSTIQNADIIAVMAQGVVIE 738
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
536-722 |
2.81e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.32 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDS---KKVNVQFLRSNIGIVSQEP-VLFACS 611
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHhLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 612 IMDN-----IKYGDNTKEIpMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:PRK10908 96 VYDNvaiplIIAGASGDDI-RRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 767920345 687 ATSALDTE-SEKTVQVALDKAREGRTCIVIAHRLSTI 722
Cdd:PRK10908 164 PTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-75 |
3.22e-20 |
|
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: 88.07 E-value: 3.22e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGT 75
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
531-694 |
3.51e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.46 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGKVMIDGHDSKKVNVQflRSNIGIVSQEPVL 607
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 608 FA-CSIMDNIKYG---DNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILL 683
Cdd:COG4136 88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|.
gi 767920345 684 LDEATSALDTE 694
Cdd:COG4136 157 LDEPFSKLDAA 167
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
234-454 |
3.53e-20 |
|
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: 91.39 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 234 RSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDLRNspGALTTRLATDASQVQGA 313
Cdd:cd18576 32 TASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRV--GELTSRLSNDVTQIQDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 314 AGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVA 393
Cdd:cd18576 110 LTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVK 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 394 GIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGL 454
Cdd:cd18576 190 AFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGEL 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
532-738 |
4.22e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 90.90 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 532 RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN----------VQFL------- 594
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 595 ---RSNIGIVSQEPVLFACSImdnikygdnTKEIPMERVIAAAKQAQLHDFVMS-LPEkyetnvgsqgsQLSRGEKQRIA 670
Cdd:PRK10419 102 vnpRKTVREIIREPLRHLLSL---------DKAERLARASEMLRAVDLDDSVLDkRPP-----------QLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 671 IARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIE 738
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
527-747 |
4.41e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN-VQFLRSNIGIVSQEP 605
Cdd:PRK13644 9 YSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 606 --VLFACSIMDNIKYG-DNTKEIPME---RVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDP 679
Cdd:PRK13644 87 etQFVGRTVEEDLAFGpENLCLPPIEirkRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 680 KILLLDEATSALDTESEKTVQVALDKA-REGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMA 747
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
297-756 |
5.28e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 95.81 E-value: 5.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 297 GALTTRLATDASQVQGAAGSQIGMIVNSFTnVTVAMIIAFS----FSWKLSLVILCFFPFLALSGATQTRMLT-GFASRD 371
Cdd:PLN03232 398 GKVTNMITTDANALQQIAEQLHGLWSAPFR-IIVSMVLLYQqlgvASLFGSLILFLLIPLQTLIVRKMRKLTKeGLQWTD 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 372 KQalemVGqITNEALSNIRTVAGIGKERRF---IEALETELEKPFKTAiqkaniyGFCFAFAQcimFIANSASY-----R 443
Cdd:PLN03232 477 KR----VG-IINEILASMDTVKCYAWEKSFesrIQGIRNEELSWFRKA-------QLLSAFNS---FILNSIPVvvtlvS 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 444 YGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQL-------LDRQPPISVYNTAgekwdnf 516
Cdd:PLN03232 542 FGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELllseeriLAQNPPLQPGAPA------- 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 517 qgkIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQ-LLERFYDPDQGKVMIdghdskkvnvqflR 595
Cdd:PLN03232 615 ---ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-------------R 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 596 SNIGIVSQEPVLFACSIMDNIKYGDNTKEIPMERVIAAAkqAQLHDFVMsLPEKYETNVGSQGSQLSRGEKQRIAIARAI 675
Cdd:PLN03232 679 GSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVT--ALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAV 755
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 676 VRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYK 754
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKK 835
|
..
gi 767920345 755 LV 756
Cdd:PLN03232 836 LM 837
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
515-747 |
5.37e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.22 E-value: 5.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 515 NFQGKIDFVDCKFTYPSRP--DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH----DSKK 588
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 589 VN-VQFLRSNIGIVSQEP--VLFACSIMDNIKYG-----DNTKEipmerviAAAKQAQLHDFVmSLPEKYetnVGSQGSQ 660
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpvnlgENKQE-------AYKKVPELLKLV-QLPEDY---VKRSPFE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 661 LSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK---TVQVALDKaREGRTCIVIAHRLSTI-QNADIIAVMAQGVV 736
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKV 229
|
250
....*....|.
gi 767920345 737 IEKGTHEELMA 747
Cdd:PRK13645 230 ISIGSPFEIFS 240
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
536-740 |
5.42e-20 |
|
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: 89.64 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGKVMIDGHDSKKVNVQFlrsNIGIVSQEPVLFAC-S 611
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQK---CVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 612 IMDNIKYgdnTKEIPMeRVIAAAKQAQLHDFVMSLPEKYETNVGSQG-SQLSRGEKQRIAIARAIVRDPKILLLDEATSA 690
Cdd:cd03234 98 VRETLTY---TAILRL-PRKSSDAIRKKRVEDVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767920345 691 LDTESE-KTVQVALDKAREGRTCIVIAH--RLSTIQNADIIAVMAQGVVIEKG 740
Cdd:cd03234 174 LDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
532-745 |
5.83e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.73 E-value: 5.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 532 RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLErFYDPD----QGKVMIDGHdskKVNVQFLRSNIGIVSQEPVL 607
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGM---PIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 608 F-------ACSIMDNIKYGDN-TKEIPMERViaaakQAQLHDfvMSLPEKYETNVGSQGSQ--LSRGEKQRIAIARAIVR 677
Cdd:TIGR00955 111 IptltvreHLMFQAHLRMPRRvTKKEKRERV-----DEVLQA--LGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 678 DPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLST--IQNADIIAVMAQGVVIEKGTHEEL 745
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVvQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
534-749 |
7.80e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.69 E-value: 7.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---------SKKVNV--QFLRSNIGIVS 602
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlARRLALlpQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 603 QEPVLFACSIMDNI--KYGDNTKEipmeRVIAAAKQAQLHDFVmslpEKYETNvgsqgsqLSRGEKQRIAIARAIVRDPK 680
Cdd:PRK11231 94 RELVAYGRSPWLSLwgRLSAEDNA----RVNQAMEQTRINHLA----DRRLTD-------LSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 681 ILLLDEATSALDTESektvQVALDK-----AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELMAQK 749
Cdd:PRK11231 159 VVLLDEPTTYLDINH----QVELMRlmrelNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
536-748 |
7.90e-20 |
|
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: 93.60 E-value: 7.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTS----IQLLERFYDPDQGKVMIDGHDSKKVNVQFLR----SNIGIVSQEP-- 605
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPmt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 606 --------------VLFacsimdnIKYGDNTKEIpMERVIAAAKQAQLHDfvmslPEKyetNVGSQGSQLSRGEKQRIAI 671
Cdd:COG4172 104 slnplhtigkqiaeVLR-------LHRGLSGAAA-RARALELLERVGIPD-----PER---RLDAYPHQLSGGQRQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 672 ARAIVRDPKILLLDEATSALDTesekTVQVA-LD-----KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEE 744
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDV----TVQAQiLDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAE 243
|
....
gi 767920345 745 LMAQ 748
Cdd:COG4172 244 LFAA 247
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
520-741 |
9.87e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.19 E-value: 9.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPS-RP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDG----HDSKKVNVQF 593
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 594 LRSNIGIVSQ--EPVLFACSIMDNIKYGDNTKEIPMERVIAAAKQaQLHDFVMSlPEKYETNvgsqGSQLSRGEKQRIAI 671
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALARE-KLALVGIS-ESLFEKN----PFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 672 ARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE-GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGT 741
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
537-749 |
1.40e-19 |
|
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: 89.53 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDqGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI 616
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 617 K-YGDNTKEipmeRVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 695
Cdd:cd03289 98 DpYGKWSDE----EIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767920345 696 EKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQK 749
Cdd:cd03289 174 YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
531-746 |
1.79e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 88.68 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL-FA 609
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNIKYGdntkEIPMERVIAAAKQaqlhdfvmsLPEKYETNVGSQG------SQLSRGEKQRIAIARAIVR------ 677
Cdd:PRK13548 91 FTVEEVVAMG----RAPHGLSRAEDDA---------LVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 678 DPKILLLDEATSALD-TESEKTVQVALDKARE-GRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELM 746
Cdd:PRK13548 158 PPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
534-747 |
1.80e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.30 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH--DSKKVNVQFLRSNIGIVSQEP--VLFA 609
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNIKYGDNTKEIPMERViaaakqAQLHDFVMSLpekyetnVGSQGSQ------LSRGEKQRIAIARAIVRDPKILL 683
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEI------TRRVDEALTL-------VDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 684 LDEATSALDTESeKTVQVALDK--AREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELMA 747
Cdd:PRK13638 160 LDEPTAGLDPAG-RTQMIAIIRriVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-75 |
2.36e-19 |
|
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: 86.09 E-value: 2.36e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGT 75
Cdd:cd03229 102 SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
536-717 |
2.66e-19 |
|
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: 87.49 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDgHDSKKVNV------QFL---RSNIGIVSQ--- 603
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLaqasprEILalrRRTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 604 ------------EPVLfacsimdnikygdntkEIPMERVIAAAKQAQLHDFvMSLPEK----YETNvgsqgsqLSRGEKQ 667
Cdd:COG4778 104 viprvsaldvvaEPLL----------------ERGVDREEARARARELLAR-LNLPERlwdlPPAT-------FSGGEQQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767920345 668 RIAIARAIVRDPKILLLDEATSALDTES-EKTVQVALDKAREGRTCIVIAH 717
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANrAVVVELIEEAKARGTAIIGIFH 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-88 |
2.72e-19 |
|
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: 87.94 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVaHLCDRVAVMQNGRIV 218
|
90
....*....|.
gi 767920345 78 ERGTHEELLER 88
Cdd:COG1124 219 EELTVADLLAG 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
527-749 |
4.68e-19 |
|
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: 87.99 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvnvqflrsnIGIVSQEPV 606
Cdd:cd03291 42 FSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 LFACSIMDNIKYGDNTKEIPMERVIaaaKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:cd03291 109 IMPGTIKENIIFGVSYDEYRYKSVV---KACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920345 687 ATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQK 749
Cdd:cd03291 186 PFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
536-747 |
4.79e-19 |
|
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: 86.83 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVqFLRSNIGI--VSQEPVLF-ACSI 612
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIK-----YGDNTKEIpMERViaaakQAQLHDFvmslpeKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 687
Cdd:cd03218 93 EENILavleiRGLSKKER-EEKL-----EELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 688 TSALDTESEKTVQVALDKAREGRTCIVIA-HRLS-TIQNADIIAVMAQGVVIEKGTHEELMA 747
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-101 |
5.11e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 91.44 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 81
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGD 566
|
90 100
....*....|....*....|
gi 767920345 82 HEELLERKGVYFTLVTLQSQ 101
Cdd:PRK11174 567 YAELSQAGGLFATLLAHRQE 586
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
198-492 |
5.52e-19 |
|
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: 87.87 E-value: 5.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 198 LVGSVGAAVNGTVTPLYAflfSQILGTFSipDKEEQRSQINGVCLLFVamgcVSLFTQFLQGYAFAKSGELLTKRLRKFG 277
Cdd:cd18551 5 LLLSLLGTAASLAQPLLV---KNLIDALS--AGGSSGGLLALLVALFL----LQAVLSALSSYLLGRTGERVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 278 FRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSG 357
Cdd:cd18551 76 WRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 358 ATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIA 437
Cdd:cd18551 154 LPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLA 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 438 NSASYRYGGYLISNEGLHFS-------YVFRVISAVvlsaTALGRAFSytpSYAKAKISAAR 492
Cdd:cd18551 234 LLVVLGVGGARVASGALTVGtlvafllYLFQLITPL----SQLSSFFT---QLQKALGALER 288
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-87 |
6.45e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 86.68 E-value: 6.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTII-----GFEH 73
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLllnrgLVAH 219
|
90
....*....|....
gi 767920345 74 GTAVERGTHEELLE 87
Cdd:COG1121 220 GPPEEVLTPENLSR 233
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
230-492 |
7.07e-19 |
|
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: 87.87 E-value: 7.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 230 KEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQ 309
Cdd:cd18542 31 GGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 310 VQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGatqTRMLTGFASRDKQALEMVGQITN---EAL 386
Cdd:cd18542 109 IRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFS---YVFFKKVRPAFEEIREQEGELNTvlqENL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 387 SNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHF-------SYV 459
Cdd:cd18542 186 TGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLgelvafiSYL 265
|
250 260 270
....*....|....*....|....*....|...
gi 767920345 460 FRVISAVvlsaTALGRAFSytpSYAKAKISAAR 492
Cdd:cd18542 266 WMLIWPV----RQLGRLIN---DMSRASASAER 291
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-80 |
7.70e-19 |
|
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: 86.02 E-value: 7.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeeLGLTLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
...
gi 767920345 78 ERG 80
Cdd:cd03257 226 EEG 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1-74 |
8.37e-19 |
|
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: 85.62 E-value: 8.37e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRAADTIIGFEHG 74
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
528-717 |
8.89e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.84 E-value: 8.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPSRPDSQ-VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQFLRSNIGIVSQEPV 606
Cdd:COG4525 12 RYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADRGVVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 LFA-CSIMDNIKYGdntkeIPMERVIAAAKQAQLHDFVmslpekyeTNVGSQG------SQLSRGEKQRIAIARAIVRDP 679
Cdd:COG4525 87 LLPwLNVLDNVAFG-----LRLRGVPKAERRARAEELL--------ALVGLADfarrriWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767920345 680 KILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAH 717
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
529-717 |
9.04e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.68 E-value: 9.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 529 YPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkVNVQFLRSNIGIVSQ-EPVL 607
Cdd:PRK11248 11 YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPGAERGVVFQnEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 608 FACSIMDNIKYGDNTKEIPMERVIAAAKQAQlhdfvmslpekyeTNVGSQGS------QLSRGEKQRIAIARAIVRDPKI 681
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQML-------------KKVGLEGAekryiwQLSGGQRQRVGIARALAANPQL 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 767920345 682 LLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAH 717
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-85 |
9.09e-19 |
|
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: 86.08 E-value: 9.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVER 79
Cdd:cd03260 142 LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEF 221
|
....*.
gi 767920345 80 GTHEEL 85
Cdd:cd03260 222 GPTEQI 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-89 |
1.23e-18 |
|
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: 85.46 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRA-ADTIIGFEHGTAVER 79
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAElADRVIVLDDGRIVAD 215
|
90
....*....|
gi 767920345 80 GTHEELLERK 89
Cdd:COG1122 216 GTPREVFSDY 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
520-747 |
1.80e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 86.61 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTY-PSRP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH----DSKKVNVQF 593
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 594 LRSNIGIVSQ--EPVLFACSIMDNIKYGDNTKEIPMERviAAAKQAQLHDFVmSLPEKYETNvgsqgS--QLSRGEKQRI 669
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEED--AKQKAREMIELV-GLPEELLAR-----SpfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 670 AIARAIVRDPKILLLDEATSALDTESEKTVQ---VALDKaREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
..
gi 767920345 746 MA 747
Cdd:PRK13634 234 FA 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-78 |
3.01e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 84.32 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGTAVE 78
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1-74 |
3.27e-18 |
|
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: 83.73 E-value: 3.27e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKI----QHGHTIISVAHRLSTVR-AADTIIGFEHG 74
Cdd:cd03262 136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLDVMkdlaEEGMTMVVVTHEMGFAReVADRVIFMDDG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
542-692 |
3.86e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.25 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 542 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSIMDNIKYG- 619
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 620 ------DNTKEIPMERViaaAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 692
Cdd:PRK10771 97 npglklNAAQREKLHAI---ARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
533-734 |
4.06e-18 |
|
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: 83.92 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 533 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV----MIDGHDSKKVNVQFLRSNIGIVSQEPVLF 608
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 609 ACSIMDNIKYGDNTKEipmERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEAT 688
Cdd:cd03290 92 NATVEENITFGSPFNK---QRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767920345 689 SALDTE-SEKTVQVALDK--AREGRTCIVIAHRLSTIQNADIIAVMAQG 734
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1-80 |
4.33e-18 |
|
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: 83.79 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:cd03245 141 LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
531-761 |
4.53e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL-FA 609
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNIKYG-----------DNTKEIPMERVIAAAKQAQLHDFVMSlpekyetnvgsqgsQLSRGEKQRIAIARAIVRD 678
Cdd:PRK09536 92 FDVRQVVEMGrtphrsrfdtwTETDRAAVERAMERTGVAQFADRPVT--------------SLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 679 PKILLLDEATSALDTESE-KTVQVALDKAREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKG------THEELMAQKG 750
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGppadvlTADTLRAAFD 237
|
250
....*....|....
gi 767920345 751 AYYKLVT---TGSP 761
Cdd:PRK09536 238 ARTAVGTdpaTGAP 251
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
536-753 |
7.58e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.45 E-value: 7.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPDQGKVMIDGHDSKKVNVQFL---RSNIGIVSQEPV------ 606
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNsslnpr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 LFACSIMDN---IKYGDNTKEIPMERVIAAAKQAQLHdfvmslPE---KYEtnvgsqgSQLSRGEKQRIAIARAIVRDPK 680
Cdd:PRK15134 379 LNVLQIIEEglrVHQPTLSAAQREQQVIAVMEEVGLD------PEtrhRYP-------AEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 681 ILLLDEATSALDteseKTVQ---VALDKAREGR---TCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQKGAYY 753
Cdd:PRK15134 446 LIILDEPTSSLD----KTVQaqiLALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
520-749 |
7.70e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.65 E-value: 7.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIG 599
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPVL-FACSIMDNI-----KYGDNTKEIpmERVIAAakqaqLHDFVmSLPEKYETNVgsqgSQLSRGEKQRIAIAR 673
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLlvfgrYFGMSTREI--EAVIPS-----LLEFA-RLESKADARV----SDLSGGMKRRLTLAR 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 674 AIVRDPKILLLDEATSALDTESEKTVQVALDK--AReGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQK 749
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
513-719 |
8.39e-18 |
|
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: 88.43 E-value: 8.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 513 WDNfQGKIDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDqGKVMIDGHDSKKVNVQ 592
Cdd:TIGR01271 1212 WPS-GGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 593 FLRSNIGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIA 672
Cdd:TIGR01271 1289 TWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLA 1365
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767920345 673 RAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRL 719
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
537-745 |
1.26e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN-VQFLRSNIGIVSQEPVLFA-CSIMD 614
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPnLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 615 NIKYGDNTKEIPMERVIAAAKQAQLHdfvmslpekyeTNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALdTE 694
Cdd:PRK15439 106 NILFGLPKRQASMQKMKQLLAALGCQ-----------LDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL-TP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 695 SE-----KTVQVALDKareGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK15439 174 AEterlfSRIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
531-718 |
1.31e-17 |
|
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: 80.66 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVL-NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvnvqflrSNIGIVSQEPVLFA 609
Cdd:cd03223 9 ATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLLFLPQRPYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNIKYgdntkeiPMERViaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATS 689
Cdd:cd03223 78 GTLREQLIY-------PWDDV------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180
....*....|....*....|....*....
gi 767920345 690 ALDTESEKTVQVALDKarEGRTCIVIAHR 718
Cdd:cd03223 121 ALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
539-762 |
1.40e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.76 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 539 NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN-VQFL--RSNIGIVSQEPVlfaCSIMDN 615
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPL---ASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 616 IKYGDNTKEiPMERVIAAAKQAQLHDFVMSLPEKyetnVGSQGSQLSR-------GEKQRIAIARAIVRDPKILLLDEAT 688
Cdd:PRK15079 115 MTIGEIIAE-PLRTYHPKLSRQEVKDRVKAMMLK----VGLLPNLINRyphefsgGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 689 SALDTESEKTVqVALDKA--RE-GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ-KGAYYKLVTTGSPI 762
Cdd:PRK15079 190 SALDVSIQAQV-VNLLQQlqREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNpLHPYTKALMSAVPI 267
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-57 |
1.42e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 81.79 E-value: 1.42e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 57
Cdd:COG4619 132 SGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSH 189
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2-86 |
1.43e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 84.74 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInrELGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
....*...
gi 767920345 79 RGTHEELL 86
Cdd:COG1135 222 QGPVLDVF 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-75 |
1.76e-17 |
|
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: 81.74 E-value: 1.76e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRA-ADTIIGFEHGT 75
Cdd:cd03225 136 SGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
519-761 |
1.85e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 84.51 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 519 KIDFVDCKFTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERFYDpdqGKVMIDGhdsKKVN-VQFL 594
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTllrMVAGLERITS---GEIWIGG---RVVNeLEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 595 RSNIGIVSQEPVLFA-CSIMDNIKYG-DNTK----EIpMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQR 668
Cdd:PRK11650 75 DRDIAMVFQNYALYPhMSVRENMAYGlKIRGmpkaEI-EERVAEAARILELEPLLDRKP-----------RELSGGQRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 669 IAIARAIVRDPKILLLDEATSALDTESEktVQVALD----KAREGRTCIVIAH-RLSTIQNADIIAVMAQGVVIEKGTHE 743
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAKLR--VQMRLEiqrlHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
250 260
....*....|....*....|....
gi 767920345 744 ELmaqkgaYYKLVTT------GSP 761
Cdd:PRK11650 221 EV------YEKPASTfvasfiGSP 238
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1-69 |
2.22e-17 |
|
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: 81.43 E-value: 2.22e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTII 69
Cdd:cd03235 133 LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVL 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-88 |
2.26e-17 |
|
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: 86.11 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:COG1123 144 SGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVaEIADRVVVMDDGRIVE 223
|
90
....*....|
gi 767920345 79 RGTHEELLER 88
Cdd:COG1123 224 DGPPEEILAA 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
538-748 |
3.40e-17 |
|
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: 85.24 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV-------MIDGHDSKKVNVQFLRSNIGIVSQEPVLFA- 609
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYPh 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNIkygdnTKEIPMERVIAAAKQAQLHDFVMS-LPEKYETNVGSQ-GSQLSRGEKQRIAIARAIVRDPKILLLDEA 687
Cdd:TIGR03269 380 RTVLDNL-----TEAIGLELPDELARMKAVITLKMVgFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920345 688 TSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-88 |
3.59e-17 |
|
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: 85.51 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQreHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVE 506
|
90
....*....|
gi 767920345 79 RGTHEELLER 88
Cdd:COG4172 507 QGPTEQVFDA 516
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
534-743 |
3.94e-17 |
|
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: 80.26 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERF--YDPDQGKVMIDGHDSKKVNVQfLRSNIGI--VSQEPVlfa 609
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 csimdnikygdntkEIPMERVIaaakqaqlhDFVMSLpekyetNVGsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATS 689
Cdd:cd03217 88 --------------EIPGVKNA---------DFLRYV------NEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 690 ALDTESEKTVQVALDKAR-EGRTCIVIAH--RLSTIQNADIIAVMAQGVVIEKGTHE 743
Cdd:cd03217 134 GLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
520-761 |
5.11e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.09 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTY-PSRP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV----MIDGHDSKKVNVQF 593
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 594 LRSNIGIVSQEP--VLFACSIMDNIKYGDNTKEIPMERVIA-AAKQAQLHDFVMSLPEKyetnvgsQGSQLSRGEKQRIA 670
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKiAAEKLEMVGLADEFWEK-------SPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 671 IARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE-GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMaQ 748
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVF-Q 233
|
250
....*....|...
gi 767920345 749 KGAYYKLVTTGSP 761
Cdd:PRK13643 234 EVDFLKAHELGVP 246
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
232-437 |
5.24e-17 |
|
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: 82.15 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 232 EQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQ 311
Cdd:cd18575 30 GNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 312 GAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPF----LALSGATQTRMltgfaSRDKQ-ALEMVGQITNEAL 386
Cdd:cd18575 108 TVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLvvlpIILFGRRVRRL-----SRASQdRLADLSAFAEETL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767920345 387 SNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIA 437
Cdd:cd18575 183 SAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGA 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1-69 |
6.03e-17 |
|
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: 84.65 E-value: 6.03e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTII 69
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIV 527
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
535-720 |
6.06e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 535 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQF---LRSN-IGIVSQ-EPVLFA 609
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNIKygdntkeipMERVIAAAKQAQLHD--FVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 687
Cdd:PRK11629 102 FTALENVA---------MPLLIGKKKPAEINSraLEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 767920345 688 TSALDTESEKTVQVALDK--AREGRTCIVIAHRLS 720
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-95 |
6.38e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.88 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 81
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
90
....*....|....
gi 767920345 82 HEELLERKGVYFTL 95
Cdd:PRK11160 557 HQELLAQQGRYYQL 570
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
538-743 |
6.38e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNV----QFLRSNIGIVSQEPVLF-ACSI 612
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIrsprDAIALGIGMVHQHFMLVpNLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIKYGDNTKEIPMERVIAAAKQaqlhdfVMSLPEKY------ETNVGsqgsQLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:COG3845 98 AENIVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVE----DLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 687 ATSALdTESE-KTVQVALDK-AREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIekGTHE 743
Cdd:COG3845 168 PTAVL-TPQEaDELFEILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKVV--GTVD 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-88 |
6.46e-17 |
|
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: 84.80 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFG 548
|
....*...
gi 767920345 81 THEELLER 88
Cdd:COG4618 549 PRDEVLAR 556
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
537-747 |
7.89e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 85.60 E-value: 7.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDghdskkvnvqflRSnIGIVSQEPVLFACSIMDNI 616
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 617 KYGDNTKEipmERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE-S 695
Cdd:PTZ00243 742 LFFDEEDA---ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767920345 696 EKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMA 747
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
527-717 |
8.04e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 8.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvnvqfLRsnIGIVSQEPV 606
Cdd:COG0488 6 KSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 LFA-CSIMDNIKYGDN---TKEIPMERVIAA--------AKQAQLHDFVMSL-------------------PEKYETNVG 655
Cdd:COG0488 72 LDDdLTVLDTVLDGDAelrALEAELEELEAKlaepdedlERLAELQEEFEALggweaearaeeilsglgfpEEDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 656 SqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES----EKTVqvaldKAREGrTCIVIAH 717
Cdd:COG0488 152 E----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSH 207
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
220-451 |
8.58e-17 |
|
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: 81.69 E-value: 8.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 220 QILGTF--SIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPG 297
Cdd:cd18541 20 RIIGRAidALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQ--KNRTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 298 ALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTgfaSRDKQALEM 377
Cdd:cd18541 98 DLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIH---KRFRKVQEA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 378 VGQITN---EALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISN 451
Cdd:cd18541 175 FSDLSDrvqESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIR 251
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
534-743 |
9.64e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.50 E-value: 9.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL---ERfYDPDQGKVMIDGHD---------SKK------------- 588
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDilelspderARAgiflafqypveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 589 -VNV-QFLRSNIGIVSQEPVlfacSIMDNIKygdntkeipmeRVIAAAKQaqlhdfvMSLPEKY---ETNVGsqgsqLSR 663
Cdd:COG0396 91 gVSVsNFLRTALNARRGEEL----SAREFLK-----------LLKEKMKE-------LGLDEDFldrYVNEG-----FSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 664 GEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAR-EGRTCIVIAH--RLSTIQNADIIAVMAQGVVIEKG 740
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
...
gi 767920345 741 THE 743
Cdd:COG0396 224 GKE 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
541-740 |
1.15e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.14 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 541 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH------DSKkvnVQFLRSNIGIVSQEPVlfaCSIMD 614
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlsPGK---LQALRRDIQFIFQDPY---ASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 615 NIKYGDNTKEiPMeRV-------IAAAKQAQLHDFVMSLPE---KYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLL 684
Cdd:PRK10261 417 RQTVGDSIME-PL-RVhgllpgkAAAARVAWLLERVGLLPEhawRYP-------HEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 685 DEATSALDTE-SEKTVQVALDKARE-GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 740
Cdd:PRK10261 488 DEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
536-719 |
1.21e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.29 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMI---DGHDSKKV---------------------NV 591
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTkekekvleklviqktrfkkikKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 592 QFLRSNIGIVSQ--EPVLFACSIMDNIKYGDNTKEIPMERviaAAKQAQLHDFVMSLPEKYetnvgSQGS--QLSRGEKQ 667
Cdd:PRK13651 101 KEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEE---AKKRAAKYIELVGLDESY-----LQRSpfELSGGQKR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767920345 668 RIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKA-REGRTCIVIAHRL 719
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDL 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-88 |
1.23e-16 |
|
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: 80.07 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:cd03299 130 LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLI 209
|
90
....*....|.
gi 767920345 78 ERGTHEELLER 88
Cdd:cd03299 210 QVGKPEEVFKK 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
537-747 |
1.66e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.53 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDP-----DQGKVMIDGHDSKKV-NVQFLRSNIGIVSQEPVLFAC 610
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 SIMDNIKYGDNTKEIPMERVIAAAKQAQLHDfvMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 690
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 691 LDTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 747
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
541-741 |
1.73e-16 |
|
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: 84.68 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 541 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKkVNVQFLRSNIGIVSQEPVLFA-CSIMDNIKYG 619
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHhLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 620 DNTKEIPMErviaaakQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV 699
Cdd:TIGR01257 1028 AQLKGRSWE-------EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767920345 700 QVALDKAREGRTCIVIAHRLStiqNADI----IAVMAQGVVIEKGT 741
Cdd:TIGR01257 1101 WDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
541-747 |
1.79e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.22 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 541 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPvlfACSIMDNIKYGD 620
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 621 --------NTKEIPMER---VIAAAKQAQLhdfvmsLPEkyetNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATS 689
Cdd:PRK15112 109 ildfplrlNTDLEPEQRekqIIETLRQVGL------LPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 690 ALD-TESEKTVQVALD-KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 747
Cdd:PRK15112 179 SLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-89 |
2.18e-16 |
|
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: 79.78 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGTAVER 79
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnkEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
90
....*....|
gi 767920345 80 GTHEELLERK 89
Cdd:TIGR04520 218 GTPREIFSQV 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
534-747 |
2.88e-16 |
|
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: 78.87 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQFLRSN------IGIVSQEPVL 607
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-----ITGLPPHriarlgIGYVPEGRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 608 FA-CSIMDNIkygdntkEIPMERVIAAAKQAQLHDFVMSL-PEKYEtNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLD 685
Cdd:COG0410 90 FPsLTVEENL-------LLGAYARRDRAEVRADLERVYELfPRLKE-RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 686 EATSALdteSEKTVQVALDK----AREGRTCIVI---AHRLSTIqnADIIAVMAQGVVIEKGTHEELMA 747
Cdd:COG0410 162 EPSLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
552-744 |
2.89e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.07 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 552 AFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH---DS-KKVNVQFLRSNIGIVSQEPVLFA-CSIMDNIKYGdntkeip 626
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARLFPhYKVRGNLRYG------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 627 mervIAAAKQAQLHDFVM-----SLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQV 701
Cdd:PRK11144 101 ----MAKSMVAQFDKIVAllgiePLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767920345 702 ALDK-AREGRTCIV-IAHRLSTI-QNADIIAVMAQGVVIEKGTHEE 744
Cdd:PRK11144 170 YLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
527-755 |
2.90e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.63 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPdqgkvMIDGHdskkvnvQFLRSNIGIVSQEPV 606
Cdd:PLN03130 622 FSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP-----RSDAS-------VVIRGTVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 LFACSIMDNIKYGDNTKEIPMERVIAAAkqAQLHDFVMsLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:PLN03130 690 IFNATVRDNILFGSPFDPERYERAIDVT--ALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 687 ATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 755
Cdd:PLN03130 767 PLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
537-717 |
3.69e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.28 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQ---FLRS-NIGIVSQE----PVLF 608
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAkHVGFVFQSfmliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 609 AcsiMDNIKY-----GDNTKEiPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILL 683
Cdd:PRK10584 105 A---LENVELpallrGESSRQ-SRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 767920345 684 LDEATSALDTES-EKTVQVALDKARE-GRTCIVIAH 717
Cdd:PRK10584 170 ADEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTH 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-69 |
4.49e-16 |
|
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: 77.90 E-value: 4.49e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS-TVRAADTII 69
Cdd:cd03293 132 LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVV 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
545-745 |
5.87e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.46 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 545 ISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVN-VQFLRSNIGIVSQEPVLFA-CSIMDNIKYG--- 619
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNdVPPAERGVGMVFQSYALYPhLSVAENMSFGlkl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 620 --DNTKEIPmERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK 697
Cdd:PRK11000 103 agAKKEEIN-QRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767920345 698 TVQVALDK--AREGRTCIVIAH-RLSTIQNADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK11000 171 QMRIEISRlhKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1-85 |
6.51e-16 |
|
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: 77.99 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
....*...
gi 767920345 78 ERGTHEEL 85
Cdd:cd03256 225 FDGPPAEL 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
537-760 |
6.56e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.81 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvNVQFL-------------RSNIgivsq 603
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALlelgagfhpeltgRENI----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 604 epvLFACSIMdnikyGDNTKEIP--MERVIAAAkqaQLHDFvMSLPekyetnVGSqgsqLSRGEKQRIAIARAIVRDPKI 681
Cdd:COG1134 110 ---YLNGRLL-----GLSRKEIDekFDEIVEFA---ELGDF-IDQP------VKT----YSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 682 LLLDEATSALDTE-SEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAqkgAYYKLVTTG 759
Cdd:COG1134 168 LLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA---AYEALLAGR 244
|
.
gi 767920345 760 S 760
Cdd:COG1134 245 E 245
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1-81 |
6.60e-16 |
|
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: 77.07 E-value: 6.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
.
gi 767920345 81 T 81
Cdd:cd03369 206 H 206
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
227-454 |
7.40e-16 |
|
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: 78.97 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 227 IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATD 306
Cdd:cd18544 30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTND 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 307 ASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGAT-QTRMLTGF-ASRDKQAlEMVGQItNE 384
Cdd:cd18544 108 TEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLfRKKSRKAYrEVREKLS-RLNAFL-QE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 385 ALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGL 454
Cdd:cd18544 186 SISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAV 255
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2-81 |
8.06e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 79.46 E-value: 8.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
...
gi 767920345 79 RGT 81
Cdd:PRK11153 222 QGT 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
536-748 |
1.04e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.90 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKS-TSIQLLERFYDPD----QGKVMIDGHDSKKVNVQFLR----SNIGIVSQEP- 605
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 606 ---------------VLfacSIMDNIKYGDNTKEI--PMERV-IAAAKQaQLHDFvmslPEkyetnvgsqgsQLSRGEKQ 667
Cdd:PRK15134 103 vslnplhtlekqlyeVL---SLHRGMRREAARGEIlnCLDRVgIRQAAK-RLTDY----PH-----------QLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 668 RIAIARAIVRDPKILLLDEATSALDTesekTVQVA-LDKARE-----GRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKG 740
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDV----SVQAQiLQLLRElqqelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQN 239
|
....*...
gi 767920345 741 THEELMAQ 748
Cdd:PRK15134 240 RAATLFSA 247
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
538-755 |
1.57e-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: 76.74 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVnvqflrsnigivsQEP-----VLFacsi 612
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG---KQI-------------TEPgpdrmVVF---- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 mdnikygDNTKEIPMERV---IAAAKQAQLHDfvMSLPEKYETN------VGSQGS------QLSRGEKQRIAIARAIVR 677
Cdd:TIGR01184 61 -------QNYSLLPWLTVrenIALAVDRVLPD--LSKSERRAIVeehialVGLTEAadkrpgQLSGGMKQRVAIARALSI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 678 DPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRL-STIQNADIIAVMAQG----------VVIEKGTHEE 744
Cdd:TIGR01184 132 RPKVLLLDEPFGALDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGpaanigqileVPFPRPRDRL 211
|
250
....*....|.
gi 767920345 745 LMAQKGAYYKL 755
Cdd:TIGR01184 212 EVVEDPSYYDL 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-58 |
1.92e-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: 74.50 E-value: 1.92e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSkiQHGHTIISVAHR 58
Cdd:cd03223 93 SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK--ELGITVISVGHR 147
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-74 |
1.96e-15 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 76.63 E-value: 1.96e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHG 74
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRyADRIIGLRDG 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
528-760 |
2.25e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.15 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN----VQFLRSNIGIVS 602
Cdd:PRK10535 13 SYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLRREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 603 QEPVLFA-CSIMDNIkygdntkEIP-----MERviaAAKQAQLHDFVMSLpeKYETNVGSQGSQLSRGEKQRIAIARAIV 676
Cdd:PRK10535 93 QRYHLLShLTAAQNV-------EVPavyagLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 677 RDPKILLLDEATSALDTESEKTVQVALDKARE-GRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 755
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPV 240
|
....*
gi 767920345 756 VTTGS 760
Cdd:PRK10535 241 VNTAS 245
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
216-492 |
2.28e-15 |
|
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: 77.44 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 216 FLFSQILGTFSIPD----------KEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQD 285
Cdd:cd18548 7 FKLLEVLLELLLPTlmadiidegiANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 286 IAWFDDLrnSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLT 365
Cdd:cd18548 87 FAEIDKF--GTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 366 GFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYG 445
Cdd:cd18548 165 PLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFG 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767920345 446 GYLISNEGLHF-------SYVFRVISAVVLSATALGrafsytpSYAKAKISAAR 492
Cdd:cd18548 245 GHLINAGSLQVgdlvafiNYLMQILMSLMMLSMVFV-------MLPRASASAKR 291
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-58 |
3.08e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.47 E-value: 3.08e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHR 58
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1-80 |
3.23e-15 |
|
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: 74.39 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD--NESEAMvqEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHGT 75
Cdd:cd03214 98 LSGGERQRVLLARALAQEPPILLLDEPTSHLDiaHQIELL--ELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGR 175
|
....*
gi 767920345 76 AVERG 80
Cdd:cd03214 176 IVAQG 180
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-88 |
3.39e-15 |
|
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: 77.40 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQreLGLAILFITHDLGVVAEiADRVAVMYAGRIV 230
|
90
....*....|.
gi 767920345 78 ERGTHEELLER 88
Cdd:COG0444 231 EEGPVEELFEN 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1-88 |
3.81e-15 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 75.49 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:COG1131 132 LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVA 211
|
90
....*....|
gi 767920345 79 RGTHEELLER 88
Cdd:COG1131 212 DGTPDELKAR 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
536-734 |
3.81e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSN-IGIVSQE-PVLFACSIM 613
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 614 DNIKYGDN-TKEIPMERVIAAAK---QAQLHDFVMSLPEKYETNVGsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATS 689
Cdd:PRK09700 99 ENLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767920345 690 AL-DTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQG 734
Cdd:PRK09700 175 SLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-86 |
4.32e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.56 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKI----QHGHTIISVAHRLSTVR-AADTIIGFEHGT 75
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPE---LVGEVLNTIrqlaQEKRTMVIVTHEMSFARdVADRAIFMDQGR 221
|
90
....*....|.
gi 767920345 76 AVERGTHEELL 86
Cdd:PRK11264 222 IVEQGPAKALF 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
537-722 |
4.59e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.89 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQFL----RSN-IGIVSQEPVLFAC- 610
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD-----VTKLpeykRAKyIGRVFQDPMMGTAp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 --SIMDN------------IKYGDNTKEIPMERviaaakqAQLHDFVMSLPEKYETNVGSqgsqLSRGEKQRIAIARAIV 676
Cdd:COG1101 96 smTIEENlalayrrgkrrgLRRGLTKKRRELFR-------ELLATLGLGLENRLDTKVGL----LSGGQRQALSLLMATL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767920345 677 RDPKILLLDEATSALDTeseKTVQVALDKAREgrtcIVIAHRLSTI 722
Cdd:COG1101 165 TKPKLLLLDEHTAALDP---KTAALVLELTEK----IVEENNLTTL 203
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
537-741 |
4.67e-15 |
|
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: 75.45 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRsNIGIV--SQEPVLFACSIMD 614
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 615 NIKYGDNTKEIPMERviAAAKQAQLHDfVMSLPEKYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 694
Cdd:cd03267 115 SFYLLAAIYDLPPAR--FKKRLDELSE-LLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767920345 695 SEKTVQVALDKAREGRTCIVIahrLSTIQNADIIAVMAQGVVIEKGT 741
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVL---LTSHYMKDIEALARRVLVIDKGR 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-90 |
5.20e-15 |
|
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: 75.28 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNES-EAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:COG4555 133 LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMArRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVA 212
|
90
....*....|..
gi 767920345 79 RGTHEELLERKG 90
Cdd:COG4555 213 QGSLDELREEIG 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
535-745 |
5.26e-15 |
|
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: 74.87 E-value: 5.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 535 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFA-CSI 612
Cdd:TIGR03410 13 SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDiTKLPPHERARAGIAYVPQGREIFPrLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIKYG-----DNTKEIPmerviaaakqaqlhDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 687
Cdd:TIGR03410 93 EENLLTGlaalpRRSRKIP--------------DEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 688 TSALDTESEKTVQVALDK--AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEEL 745
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-89 |
5.64e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 75.80 E-value: 5.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRAADTIIGFEHGTAVE 78
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIA 222
|
90
....*....|.
gi 767920345 79 RGTHEELLERK 89
Cdd:PRK13632 223 QGKPKEILNNK 233
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
231-686 |
8.15e-15 |
|
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: 77.92 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 231 EEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDLRNSpgALTTRLATDASQV 310
Cdd:COG4615 41 NATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAA--RLLAALTEDVRTI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 311 QGAAgSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFfpfLALSGATQTRMLtgfaSRDKQALEMVGQITNEALSNIR 390
Cdd:COG4615 119 SQAF-VRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVL---LGLGVAGYRLLV----RRARRHLRRAREAEDRLFKHFR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 391 TVAGIGKE------RRfiEALeteLEKPFKTAIQKA--------NIYGFCFAFAQCIMFIansasyryggyLIsneGL-- 454
Cdd:COG4615 191 ALLEGFKElklnrrRR--RAF---FDEDLQPTAERYrdlriradTIFALANNWGNLLFFA-----------LI---GLil 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 455 ----HFSYVF-RVISAVVL----SATALGRAFSYTPSYAKAKISAARFFQL---LDRQPPISVYNTAGEKWDNFQgKIDF 522
Cdd:COG4615 252 fllpALGWADpAVLSGFVLvllfLRGPLSQLVGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQ-TLEL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 523 VDCKFTYPSRPDSQ--VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGI 600
Cdd:COG4615 331 RGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 601 VSQEPVLFacsimDNIkYGDNTKEIPmERVIAAAKQAQLHDFVmslpeKYETNVGSQgSQLSRGEKQRIAIARAIVRDPK 680
Cdd:COG4615 411 VFSDFHLF-----DRL-LGLDGEADP-ARARELLERLELDHKV-----SVEDGRFST-TDLSQGQRKRLALLVALLEDRP 477
|
....*.
gi 767920345 681 ILLLDE 686
Cdd:COG4615 478 ILVFDE 483
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-80 |
8.15e-15 |
|
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: 74.09 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLS-TVRAADTIIGFEHGTAV 77
Cdd:cd03259 131 LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIV 210
|
...
gi 767920345 78 ERG 80
Cdd:cd03259 211 QVG 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
538-734 |
8.20e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.66 E-value: 8.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPD---QGKVMIDGHDSKKVNVQFL-RSNIGIVSQEPVLFA-CSI 612
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKeLSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIKYGDNTKE---IPMERVIAAAKQ--AQLhdfvmslpeKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 687
Cdd:PRK13549 100 LENIFLGNEITPggiMDYDAMYLRAQKllAQL---------KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767920345 688 TSALdTESEKTVQVAL--DKAREGRTCIVIAHRLSTIQN-ADIIAVMAQG 734
Cdd:PRK13549 171 TASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-83 |
8.63e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 74.66 E-value: 8.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVR-AADTIIGFEHGTAVE 78
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARkVASQVVYMEKGRIIE 221
|
....*
gi 767920345 79 RGTHE 83
Cdd:COG4161 222 QGDAS 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-88 |
9.23e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.44 E-value: 9.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEamvQEVLSKI-----QHGHTIISVAHRLSTVRAADTIIGFEHGT 75
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR---REVLETVrqlkeQKGITVLSITHDLDEAAQADRVIVMNKGE 217
|
90
....*....|...
gi 767920345 76 AVERGTHEELLER 88
Cdd:PRK13635 218 ILEEGTPEEIFKS 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-88 |
1.01e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 76.29 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNES-EAMVQEvLSKIQH--GHTIISVAHRLS---TVraADTIIGFEHG 74
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLrEEMREE-LRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDG 212
|
90
....*....|....
gi 767920345 75 TAVERGTHEELLER 88
Cdd:COG3842 213 RIEQVGTPEEIYER 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-87 |
1.05e-14 |
|
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: 74.25 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIA 222
|
....*....
gi 767920345 79 RGTHEELLE 87
Cdd:COG1127 223 EGTPEELLA 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-77 |
1.16e-14 |
|
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: 72.08 E-value: 1.16e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-87 |
1.17e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEA----MVQEVlsKIQHGHTIISVAHRLSTVRAADTIIGFEHGTA 76
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQnlldLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
90
....*....|.
gi 767920345 77 VERGTHEELLE 87
Cdd:PRK13648 221 YKEGTPTEIFD 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-86 |
1.52e-14 |
|
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: 74.31 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD--NESEAMvqEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHGT 75
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDlaHQLEVL--ELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGR 215
|
90
....*....|.
gi 767920345 76 AVERGTHEELL 86
Cdd:COG1120 216 IVAQGPPEEVL 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-85 |
1.57e-14 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 73.87 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:TIGR02315 146 LSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInkEDGITVIINLHQVDLAKKyADRIVGLKAGEIV 225
|
....*...
gi 767920345 78 ERGTHEEL 85
Cdd:TIGR02315 226 FDGAPSEL 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-75 |
1.94e-14 |
|
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: 72.89 E-value: 1.94e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQE--VLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGT 75
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
534-692 |
2.14e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.94 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMidghdSKKVNVQFLRSNIGIVSQEPVLFAC-SI 612
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQDARLLPWkKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 613 MDNIKYGDNTKEIPmerviaAAKQA----QLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 688
Cdd:PRK11247 99 IDNVGLGLKGQWRD------AALQAlaavGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
....
gi 767920345 689 SALD 692
Cdd:PRK11247 162 GALD 165
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-88 |
2.74e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.20 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKIQ----HGHTIISVAHRLSTVR-AADTIIGFEHGT 75
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE---LRHEVLKVMQdlaeEGMTMVIVTHEIGFAEkVASRLIFIDKGR 213
|
90
....*....|...
gi 767920345 76 AVERGTHEELLER 88
Cdd:PRK09493 214 IAEDGDPQVLIKN 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
531-737 |
2.98e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNVQFLRSN----IGIVSQE-- 604
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQEln 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 605 --PVLfacSIMDNIKYGDNTKE----IPMERVIAAAKQ--AQLhdfvmSLPEKYETNVGsqgsQLSRGEKQRIAIARAIV 676
Cdd:PRK10762 90 liPQL---TIAENIFLGREFVNrfgrIDWKKMYAEADKllARL-----NLRFSSDKLVG----ELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 677 RDPKILLLDEATSAL-DTESEKTVQVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVI 737
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDGQFI 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-87 |
3.02e-14 |
|
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: 73.45 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLS-TVRAADTIIGFEHGTAV 77
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQaeLQKTIVFITHDLDeALRLGDRIAIMKDGRLV 240
|
90
....*....|
gi 767920345 78 ERGTHEELLE 87
Cdd:cd03294 241 QVGTPEEILT 250
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
533-748 |
3.41e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 533 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkVNVQF------LRSNIGIVSQE-- 604
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG-----QEMRFasttaaLAAGVAIIYQElh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 605 --PVLfacSIMDNIKYGD--NTKEIPMERVIAAAKQAQLH----DFVMSLPEKYetnvgsqgsqLSRGEKQRIAIARAIV 676
Cdd:PRK11288 90 lvPEM---TVAENLYLGQlpHKGGIVNRRLLNYEAREQLEhlgvDIDPDTPLKY----------LSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920345 677 RDPKILLLDEATSALDT-ESEKTVQVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEkgTHEElMAQ 748
Cdd:PRK11288 157 RNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDD-MAQ 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1-88 |
3.44e-14 |
|
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: 72.65 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQ 210
|
90
....*....|.
gi 767920345 78 ERGTHEELLER 88
Cdd:cd03300 211 QIGTPEEIYEE 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
528-686 |
3.60e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.75 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPSRpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSiqllerFY------DPDQGKVMIDGHDSKKVNVqFLRSNIGI- 600
Cdd:COG1137 12 SYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 601 -VSQEPVLFA-CSIMDNIK----YGDNTKEIPMERViaaakQAQLHDFvmSLpekyeTNV-GSQGSQLSRGEKQRIAIAR 673
Cdd:COG1137 82 yLPQEASIFRkLTVEDNILavleLRKLSKKEREERL-----EELLEEF--GI-----THLrKSKAYSLSGGERRRVEIAR 149
|
170
....*....|...
gi 767920345 674 AIVRDPKILLLDE 686
Cdd:COG1137 150 ALATNPKFILLDE 162
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1-87 |
3.81e-14 |
|
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: 72.47 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALdneSEAMVQEVLSKIQH----GHTIISVAHRLSTVRA-ADTIIGFEHGT 75
Cdd:cd03224 133 LSGGEQQMLAIARALMSRPKLLLLDEPSEGL---APKIVEEIFEAIRElrdeGVTILLVEQNARFALEiADRAYVLERGR 209
|
90
....*....|..
gi 767920345 76 AVERGTHEELLE 87
Cdd:cd03224 210 VVLEGTAAELLA 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-80 |
5.13e-14 |
|
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: 70.80 E-value: 5.13e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:cd03247 100 SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
520-747 |
5.36e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPsrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhDSKKVNVQFLRSNIG 599
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQepvlfacsiMDNIKYGDNTKEipMERVIA---AAKQAQLHDFVMSLPE--KYETNVGSQGSQLSRGEKQRIAIARA 674
Cdd:PRK13537 84 VVPQ---------FDNLDPDFTVRE--NLLVFGryfGLSAAAARALVPPLLEfaKLENKADAKVGELSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 675 IVRDPKILLLDEATSALDTESEKTVQVALDK--AReGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 747
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-109 |
5.71e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 72.56 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVR-AADTIIGFEHGTAV 77
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQekLGISYIYVSQHLGIVKhISDKVLVMHQGEVV 229
|
90 100 110
....*....|....*....|....*....|..
gi 767920345 78 ERGTHEELLERKGVYFTLVTLQSQGNQALNEE 109
Cdd:COG4167 230 EYGKTAEVFANPQHEVTKRLIESHFGEALTAD 261
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
237-417 |
5.94e-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: 73.32 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 237 INGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGS 316
Cdd:cd18564 53 LLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLVS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 317 QIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGfASRDKQALEmvGQIT---NEALSNIRTVA 393
Cdd:cd18564 131 GVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKE-ASREQRRRE--GALAsvaQESLSAIRVVQ 207
|
170 180
....*....|....*....|....
gi 767920345 394 GIGKERRFIEALETELEKPFKTAI 417
Cdd:cd18564 208 AFGREEHEERRFARENRKSLRAGL 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-57 |
7.47e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.04 E-value: 7.47e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 57
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTH 197
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
536-740 |
8.01e-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: 71.41 E-value: 8.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSkkvnvQFLRSNIGIvsqEPVLfacSIMDN 615
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLLGLGGGF---NPEL---TGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 616 IK-----YGDNTKEIP--MERVIAAakqAQLHDFvMSLPEKyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEAT 688
Cdd:cd03220 105 IYlngrlLGLSRKEIDekIDEIIEF---SELGDF-IDLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767920345 689 SALDTE-SEKTVQVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKG 740
Cdd:cd03220 171 AVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
541-745 |
1.04e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.85 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 541 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD-PdqGKVM-----IDGHD----SKKVNVQFLRSNIGIVSQEPV--LF 608
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMaekleFNGQDlqriSEKERRNLVGAEVAMIFQDPMtsLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 609 AC-----SIMDNIKY--GDNTKEiPMERVIAAAKQAQLHDFVMSLpEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKI 681
Cdd:PRK11022 104 PCytvgfQIMEAIKVhqGGNKKT-RRQRAIDLLNQVGIPDPASRL-DVYP-------HQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 682 LLLDEATSALD-TESEKTVQVALD-KAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK11022 175 LIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
517-747 |
1.07e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.11 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 517 QGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFL-- 594
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 595 -RSNIGIVSQEPVLFA-CSIMDNIKYgdntkeiPMeRVIAAAKQAQLHDFVMSlpeKYETnVGSQG------SQLSRGEK 666
Cdd:PRK11831 82 vRKRMSMLFQSGALFTdMNVFDNVAY-------PL-REHTQLPAPLLHSTVMM---KLEA-VGLRGaaklmpSELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 667 QRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHE 743
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQ 229
|
....
gi 767920345 744 ELMA 747
Cdd:PRK11831 230 ALQA 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-74 |
1.12e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.63 E-value: 1.12e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHG 74
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEG 210
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
197-454 |
1.44e-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: 72.13 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 197 MLVGSVGAAVNGTVTPlyaFLFSQILGTfSIPDKEEQRsqINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 276
Cdd:cd18550 4 VLLLILLSALLGLLPP---LLLREIIDD-ALPQGDLGL--LVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 277 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS 356
Cdd:cd18550 78 LYAHLQRMSLAFFT--RTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 357 GATQTRMLTGFASRDKQALEMVGQITNEALSnirtVAGI------GKERRFIEALETELEKPFKTAIqKANIYG--FcFA 428
Cdd:cd18550 156 TRRVGRRRRKLTREQQEKLAELNSIMQETLS----VSGAllvklfGREDDEAARFARRSRELRDLGV-RQALAGrwF-FA 229
|
250 260
....*....|....*....|....*.
gi 767920345 429 FAQCIMFIANSASYRYGGYLISNEGL 454
Cdd:cd18550 230 ALGLFTAIGPALVYWVGGLLVIGGGL 255
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-80 |
1.49e-13 |
|
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: 70.40 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ---HGHTIIsVAHRLSTV-RAADTIIGFEHGTA 76
Cdd:cd03297 132 LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKknlNIPVIF-VTHDLSEAeYLADRIVVMEDGRL 210
|
....
gi 767920345 77 VERG 80
Cdd:cd03297 211 QYIG 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1-69 |
1.64e-13 |
|
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: 69.35 E-value: 1.64e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTII 69
Cdd:cd03230 96 LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAeRLCDRVA 166
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1-86 |
1.79e-13 |
|
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: 70.79 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRL-STVRAADTIIGFEHGTAV 77
Cdd:cd03295 136 LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIV 215
|
....*....
gi 767920345 78 ERGTHEELL 86
Cdd:cd03295 216 QVGTPDEIL 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-85 |
1.98e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.96 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVER 79
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEY 228
|
....*.
gi 767920345 80 GTHEEL 85
Cdd:PRK14239 229 NDTKQM 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-85 |
2.19e-13 |
|
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: 70.22 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:cd03261 138 SGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAiADRIAVLYDGKIVA 217
|
....*..
gi 767920345 79 RGTHEEL 85
Cdd:cd03261 218 EGTPEEL 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
534-747 |
2.20e-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: 73.30 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERF--YDPDQGKVM-----------ID------------GHDSKK 588
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyVErpskvgepcpvcGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 589 VNVQF----------LRSNIGIVSQEPvlFAC----SIMDNIKYGDNTKEIPMERVIAAA----KQAQLHDFVMSLpeky 650
Cdd:TIGR03269 92 EEVDFwnlsdklrrrIRKRIAIMLQRT--FALygddTVLDNVLEALEEIGYEGKEAVGRAvdliEMVQLSHRITHI---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 651 etnvgsqGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKA--REGRTCIVIAHRLSTIQN-ADI 727
Cdd:TIGR03269 166 -------ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDK 238
|
250 260
....*....|....*....|
gi 767920345 728 IAVMAQGVVIEKGTHEELMA 747
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVA 258
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-88 |
2.35e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.17 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD----NESEAMVQEVLSkiQHGHTIISVAHRLSTV-RAADTIIGFEHGT 75
Cdd:COG3840 130 LSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCR--ERGLTVLMVTHDPEDAaRIADRVLLVADGR 207
|
90
....*....|...
gi 767920345 76 AVERGTHEELLER 88
Cdd:COG3840 208 IAADGPTAALLDG 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-83 |
2.62e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVR-AADTIIGFEHGTAVE 78
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARkTASRVVYMENGHIVE 221
|
....*
gi 767920345 79 RGTHE 83
Cdd:PRK11124 222 QGDAS 226
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
245-452 |
2.95e-13 |
|
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: 71.19 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 245 VAMGCVS-LFTqflqgYAFAKsgelLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVN 323
Cdd:cd18784 51 VAAGIRGgLFT-----LAMAR----LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTVSLNLNIFLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 324 SFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIE 403
Cdd:cd18784 120 SLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEAN 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767920345 404 ALETELEKPFKTAIQKANIYG---FCFAFAQCIMFIansASYRYGGYLISNE 452
Cdd:cd18784 200 RYSEKLKDTYKLKIKEALAYGgyvWSNELTELALTV---STLYYGGHLVITG 248
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-88 |
3.58e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 71.72 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALD----NESEAMVQEVLSKIqhGHTIISVAH-RLSTVRAADTIIGFEHGTA 76
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL--GGTTVFVTHdQEEALELADRVVVMNQGRI 212
|
90
....*....|..
gi 767920345 77 VERGTHEELLER 88
Cdd:COG1118 213 EQVGTPDEVYDR 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
534-742 |
4.13e-13 |
|
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: 72.55 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPD---QGKVMIDGHDSKKVNVQFL-RSNIGIVSQEPVLFA 609
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 -CSIMDNIKYGdNTKEIPMERVIAAAKQAQLHDFV--MSLPEkyeTNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:TIGR02633 92 eLSVAENIFLG-NEITLPGGRMAYNAMYLRAKNLLreLQLDA---DNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 687 ATSALdTESEKTVQVAL--DKAREGRTCIVIAHRLSTIQnadiiAVMAQGVVIEKGTH 742
Cdd:TIGR02633 168 PSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVK-----AVCDTICVIRDGQH 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
536-749 |
4.27e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.54 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNV-QFLRSNIGIVSQEPVLFA-CSIM 613
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRrLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 614 DNIkygdntkeIPMERVIAAAKQAQLHDFVMSLPEKYETN--VGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 691
Cdd:PRK10895 97 DNL--------MAVLQIRDDLSAEQREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 692 DTESEKTVQVALDKARE-GRTCIVIAHRL-STIQNADIIAVMAQGVVIEKGTHEELMAQK 749
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-85 |
5.44e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.89 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVR-AADTIIGFEHGTAVE 78
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKhISDRVLVMYLGHAVE 242
|
....*..
gi 767920345 79 RGTHEEL 85
Cdd:PRK15079 243 LGTYDEV 249
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
235-438 |
9.47e-13 |
|
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: 69.74 E-value: 9.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 235 SQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAA 314
Cdd:cd18547 42 SGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 315 GSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSgatqTRMLTGFASR--DKQAlEMVGQIT---NEALSNI 389
Cdd:cd18547 120 SQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLV----TKFIAKRSQKyfRKQQ-KALGELNgyiEEMISGQ 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767920345 390 RTVAGIGKERRFIEALETELEKPFKTAIqKANIYGfcFAFAQCIMFIAN 438
Cdd:cd18547 195 KVVKAFNREEEAIEEFDEINEELYKASF-KAQFYS--GLLMPIMNFINN 240
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
542-740 |
1.06e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.80 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 542 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQ---------FLRSNIGIVSQEP---VLFA 609
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYalseaerrrLLRTEWGFVHQHPrdgLRMQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNI----------KYGD--NTKEIPMERV-IAAAKqaqLHDfvmsLPekyetnvgsqgSQLSRGEKQRIAIARAIV 676
Cdd:PRK11701 106 VSAGGNIgerlmavgarHYGDirATAGDWLERVeIDAAR---IDD----LP-----------TTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 677 RDPKILLLDEATSALDTesekTVQVA-LDKARE-----GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 740
Cdd:PRK11701 168 THPRLVFMDEPTGGLDV----SVQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-96 |
1.14e-12 |
|
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: 68.78 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 81
Cdd:cd03288 158 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDT 237
|
90
....*....|....*.
gi 767920345 82 HEELLERK-GVYFTLV 96
Cdd:cd03288 238 PENLLAQEdGVFASLV 253
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-88 |
1.20e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.61 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVR-AADTIIGFEHGTAVE 78
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHDLSVVEhIADEVMVMYLGRCVE 235
|
90
....*....|
gi 767920345 79 RGTHEELLER 88
Cdd:PRK11308 236 KGTKEQIFNN 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-87 |
1.38e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTI--ISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVE 506
|
....*....
gi 767920345 79 RGTHEELLE 87
Cdd:PRK15134 507 QGDCERVFA 515
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
520-717 |
1.64e-12 |
|
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: 65.55 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDghdsKKVNVQFLrsnig 599
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 ivsqepvlfacsimdnikygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgSQLSRGEKQRIAIARAIVRDP 679
Cdd:cd03221 69 -----------------------------------------------------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190
....*....|....*....|....*....|....*...
gi 767920345 680 KILLLDEATSALDTESEKTVQVALdKAREGrTCIVIAH 717
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-88 |
1.66e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.60 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGTAVE 78
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrdDYQMTVISITHDLDEVALSDRVLVMKNGQVES 220
|
90
....*....|
gi 767920345 79 RGTHEELLER 88
Cdd:PRK13650 221 TSTPRELFSR 230
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-88 |
1.77e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 69.38 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVR-AADTIIGFEHGTAVE 78
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQdeLGLTYLFISHDLSVVRhISDRVAVMYLGKIVE 238
|
90
....*....|
gi 767920345 79 RGTHEELLER 88
Cdd:COG4608 239 IAPRDELYAR 248
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
2-88 |
3.39e-12 |
|
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: 68.59 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEamvQEVLSKIQ--HGHT---IISVAHRLSTV-RAADTIIGFEHGT 75
Cdd:COG4148 135 SGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK---AEILPYLErlRDELdipILYVSHSLDEVaRLADHVVLLEQGR 211
|
90
....*....|...
gi 767920345 76 AVERGTHEELLER 88
Cdd:COG4148 212 VVASGPLAEVLSR 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
538-757 |
4.27e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.80 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRsNIGIV----SQepVLFACSIM 613
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ--LWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 614 DNIK-----YgdntkEIPMERviAAAKQAQLHDfVMSLPEKYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 688
Cdd:COG4586 115 DSFRllkaiY-----RIPDAE--YKKRLDELVE-LLDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 689 SALDTESEKTVQVALDK--AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELmAQKGAYYKLVT 757
Cdd:COG4586 183 IGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEEL-KERFGPYKTIV 253
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
534-740 |
4.81e-12 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 66.52 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL--ERFYDPDQGKVMIDGHDSKKVNVQfLRSNIGIV--SQEPV--- 606
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEPD-ERARAGLFlaFQYPEeip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 -----LFACSIMDNIKYGDNTKEIPMERVIAAAKQA-QLHDFVMSLPEKYeTNVGsqgsqLSRGEKQRIAIARAIVRDPK 680
Cdd:TIGR01978 91 gvsnlEFLRSALNARRSARGEEPLDLLDFEKLLKEKlALLDMDEEFLNRS-VNEG-----FSGGEKKRNEILQMALLEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 681 ILLLDEATSALDTESEKTVQVALDKAR-EGRTCIVIAH--RLSTIQNADIIAVMAQGVVIEKG 740
Cdd:TIGR01978 165 LAILDEIDSGLDIDALKIVAEGINRLRePDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
538-743 |
5.10e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVnvqfLRSN-IGIVSQE-------PVLFA 609
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNlVAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNiKYGD-----NTKEIPMERVIAAAKQAQLHDFVMSlpekyetnvgsQGSQLSRGEKQRIAIARAIVRDPKILLL 684
Cdd:PRK15056 99 DVVMMG-RYGHmgwlrRAKKRDRQIVTAALARVDMVEFRHR-----------QIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 685 DEATSALDTESEKTVQVALDKAR-EGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHE 743
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
537-740 |
5.49e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFY--DPDQGKVMIDghdskkvNVQFlrsnigivSQEpvlfaCSIMD 614
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP-------DNQF--------GRE-----ASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 615 NIKYGDNTKEipmerVIAAAKQAQLHDFVMSLpEKYetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 694
Cdd:COG2401 105 AIGRKGDFKD-----AVELLNAVGLSDAVLWL-RRF--------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767920345 695 SEKTVQVALDKA--REGRTCIVIAHRlstiqnADIIAVMAQGVVIEKG 740
Cdd:COG2401 171 TAKRVARNLQKLarRAGITLVVATHH------YDVIDDLQPDLLIFVG 212
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
536-734 |
6.86e-12 |
|
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: 64.96 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL-ERFYDPD-QGKVMIDGhdsKKVNVQFLRSnIGIVSQEPVLFACSim 613
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILING---RPLDKNFQRS-TGYVEQQDVHSPNL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 614 dnikygdnTKEIPMErvIAAAKQAqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSALDT 693
Cdd:cd03232 95 --------TVREALR--FSALLRG-----------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767920345 694 ESEKTVQVALDK-AREGRTCIVIAHRLS--TIQNADIIAVMAQG 734
Cdd:cd03232 142 QAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-88 |
7.14e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 66.75 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRAADTIIGFEHGTAVE 78
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLA 223
|
90
....*....|
gi 767920345 79 RGTHEELLER 88
Cdd:PRK13640 224 QGSPVEIFSK 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-68 |
7.73e-12 |
|
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: 65.19 E-value: 7.73e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSK-IQHGHTIISVAHRLSTVRAADTI 68
Cdd:COG4133 132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-75 |
7.94e-12 |
|
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: 65.53 E-value: 7.94e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGT 75
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIeEAKARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
532-716 |
8.37e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.28 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 532 RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGivSQEPVLFACS 611
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 612 IMDNIKYGDNTKEIPMERVIAAAKQAQLHDfVMSLPEKYetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSAL 691
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*
gi 767920345 692 DTESEKTVQvALDKAREGRTCIVIA 716
Cdd:PRK13539 159 DAAAVALFA-ELIRAHLAQGGIVIA 182
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
547-729 |
1.02e-11 |
|
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: 63.55 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 547 PGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV-MIDGHDSKKVNVQFLRsnigivsqepvlfacsimdnikygdntkei 625
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 626 pmerviaaakqaqlhdfvmslpekyETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALD- 704
Cdd:smart00382 51 -------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEEl 105
|
170 180 190
....*....|....*....|....*....|.
gi 767920345 705 ------KAREGRTCIVIAHRLSTIQNADIIA 729
Cdd:smart00382 106 rlllllKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
520-748 |
1.08e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIdGHdskkvNVQflrsnIG 599
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPVLFAC--SIMDNIK-YGDNTKEIpmerviaaakqaqlhdFVMSL-------PEKYETNVGSqgsqLSRGEKQRI 669
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRdGAPGGTEQ----------------EVRGYlgrflfsGDDAFKPVGV----LSGGEKARL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 670 AIARAIVRDPKILLLDEATSALDTESEKTVQVALDkAREGrTCIVIAH-R--LSTIQNaDIIAVMAQGVVIEKGTHEELM 746
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRVAT-RILEFEDGGVREYPGGYDDYL 518
|
..
gi 767920345 747 AQ 748
Cdd:COG0488 519 EK 520
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-57 |
1.20e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 67.02 E-value: 1.20e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNES-EAMVQEvLSKIQH--GHTIISVAH 57
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLrVEMRAE-IKRLHRrlGTTTIYVTH 192
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
533-746 |
1.56e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 533 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH-----DSKKvnvqFLRSNIGIVSQEPVL 607
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswSSKA----FARKVAYLPQQLPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 608 FACSIMDNI------------KYGDNTKEipmeRVIAAAKQAQLHDFVMSLpekyetnVGSqgsqLSRGEKQRIAIARAI 675
Cdd:PRK10575 98 EGMTVRELVaigrypwhgalgRFGAADRE----KVEEAISLVGLKPLAHRL-------VDS----LSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 676 VRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAhRLSTIQNA----DIIAVMAQGVVIEKGTHEELM 746
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-86 |
1.59e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKIQH----GHTIISVAHRLSTVRAADTIIGFEH-GT 75
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQQlaeeGKTMVVVTHEMGFARHVSSHVIFLHqGK 229
|
90
....*....|.
gi 767920345 76 AVERGTHEELL 86
Cdd:PRK10619 230 IEEEGAPEQLF 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2-78 |
1.63e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 64.69 E-value: 1.63e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADT-IIGFEHGTAVE 78
Cdd:COG2884 139 SGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-84 |
1.63e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.84 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEamvQEVLSKIQHGH-----TIISVAHRLSTV-RAADTIIGFEHG 74
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR---DEILNKIKELHkeynmTIILVSHSMEDVaKLADRIIVMNKG 221
|
90
....*....|
gi 767920345 75 TAVERGTHEE 84
Cdd:PRK13637 222 KCELQGTPRE 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-57 |
1.92e-11 |
|
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: 64.20 E-value: 1.92e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNE-SEAMVQEvLSKIQ--HGHTIISVAH 57
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKlRVQMRAE-LKRLQqrLGTTTIYVTH 189
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
541-746 |
2.09e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 541 LSVSISPGQTLAFVGSSGCGKSTsiqLLERFYD--PDQGKVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFAcsiMDNIK 617
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPlEAWSAAELARHRAYLSQQQTPPFA---MPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 618 Y-----GDNTKEipmerviaAAKQAQLHDFV--MSLPEKYETNVGsqgsQLSRGEKQRIAIARAIVR-------DPKILL 683
Cdd:PRK03695 89 YltlhqPDKTRT--------EAVASALNEVAeaLGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 684 LDEATSALDTesekTVQVALDK-----AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELM 746
Cdd:PRK03695 157 LDEPMNSLDV----AQQAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
532-745 |
2.28e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 532 RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV-------------MIDGHDSKKVNVQFLR-SN 597
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 598 IGIVSQEPV-----LFAC--SIMDNIKYGDNTKEipmERVIAAAKQaqLHDFVmSLPEKyETNVGSQGSQLSRGEKQRIA 670
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQGASR---EEAMVEAKR--MLDQV-RIPEA-QTILSRYPHQLSGGMRQRVM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 671 IARAIVRDPKILLLDEATSALD-TESEKTVQ-VALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDvTIQAQILQlIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1-69 |
2.54e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.41 E-value: 2.54e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRAADTII 69
Cdd:NF040873 120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCV 189
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-88 |
2.65e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 64.67 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLS-TVRAADTIIGFEHGTAVER 79
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEF 234
|
....*....
gi 767920345 80 GTHEELLER 88
Cdd:COG1117 235 GPTEQIFTN 243
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-80 |
3.27e-11 |
|
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: 63.54 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:cd03266 137 FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVeRLCDRVVVLHRGRVVY 216
|
..
gi 767920345 79 RG 80
Cdd:cd03266 217 EG 218
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
247-406 |
3.44e-11 |
|
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: 64.67 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 247 MGCVSLFTQF---LQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVN 323
Cdd:cd18590 42 MCLFSLGSSLsagLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEK--TKTGDLTSRLSTDTTLMSRSVALNANVLLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 324 SFTNVTVAMIIAFSFSWKLSLVILCFFPFLALsgaTQTRMLTGFASRDKQALEMV---GQITNEALSNIRTVAGIGKE-- 398
Cdd:cd18590 120 SLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAI---AQKVYNTYHQKLSQAVQDSIakaGELAREAVSSIRTVRSFKAEee 196
|
170
....*....|
gi 767920345 399 --RRFIEALE 406
Cdd:cd18590 197 eaCRYSEALE 206
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
240-454 |
3.64e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 64.84 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 240 VCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQG--AAGSQ 317
Cdd:cd18563 45 LVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDflSDGLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 318 iGMIVNSFTNVTVAmIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGK 397
Cdd:cd18563 123 -DFLTNILMIIGIG-VVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQ 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 398 ERRFIEALETELEKPFKTAIQKANIYGFCFAFaqcIMFIANSASY---RYGGYLISNEGL 454
Cdd:cd18563 201 EKREIKRFDEANQELLDANIRAEKLWATFFPL---LTFLTSLGTLivwYFGGRQVLSGTM 257
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
237-454 |
3.77e-11 |
|
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: 64.80 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 237 INGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGS 316
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 317 QIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGAT-QTRMLTGF-ASRDKQAlEMVGQItNEALSNIRTVAG 394
Cdd:cd18545 117 GLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLlRRRARKAWqRVRKKIS-NLNAYL-HESISGIRVIQS 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 395 IGKE----RRFIEaLETELEKPFKTAIQKANIYG----FCFAFAQCIMFIansasyrYGGYLISNEGL 454
Cdd:cd18545 195 FAREdeneEIFDE-LNRENRKANMRAVRLNALFWplveLISALGTALVYW-------YGGKLVLGGAI 254
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
537-747 |
3.98e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.44 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLE-RFYDPD-QGKVMIDGhdsKKVNVQFLRsNIGIVSQEPVLFA----- 609
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILK-RTGFVTQDDILYPhltvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 -----CSIMDNIK-YGDNTKEIPMERVIAAAKQAQLHDFVMSlpekyetNVGSQGsqLSRGEKQRIAIARAIVRDPKILL 683
Cdd:PLN03211 159 etlvfCSLLRLPKsLTKQEKILVAESVISELGLTKCENTIIG-------NSFIRG--ISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 684 LDEATSALD-TESEKTVQVALDKAREGRTCIVIAHRLST--IQNADIIAVMAQGVVIEKGTHEELMA 747
Cdd:PLN03211 230 LDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-89 |
4.19e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.42 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIV 225
|
90
....*....|..
gi 767920345 78 ERGTHEELLERK 89
Cdd:PRK13646 226 SQTSPKELFKDK 237
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-88 |
4.72e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.35 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAH----RLSTvraADTIIGFEHG 74
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdqeeALTM---SDRIVVMRDG 221
|
90
....*....|....
gi 767920345 75 TAVERGTHEELLER 88
Cdd:PRK09452 222 RIEQDGTPREIYEE 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1-89 |
4.90e-11 |
|
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: 65.13 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIqHGHT---IISVAHRLSTV-RAADTIIGFEHGTA 76
Cdd:TIGR02142 132 LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERL-HAEFgipILYVSHSLQEVlRLADRVVVLEDGRV 210
|
90
....*....|...
gi 767920345 77 VERGTHEELLERK 89
Cdd:TIGR02142 211 AAAGPIAEVWASP 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
542-751 |
6.81e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 542 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH--DSKKVNVqflRSNIGIVSQepvlfACSImdnikYG 619
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIAT---RRRVGYMSQ-----AFSL-----YG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 620 DNT----------------KEIPmERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILL 683
Cdd:NF033858 353 ELTvrqnlelharlfhlpaAEIA-ARVAEMLERFDLADVADALPD-----------SLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 684 LDEATSALDTesektvqVA--------LDKAREGRTCIVIA-HRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGA 751
Cdd:NF033858 421 LDEPTSGVDP-------VArdmfwrllIELSREDGVTIFIStHFMNEAERCDRISLMHAGRVLASDTPAALVAARGA 490
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1-80 |
6.93e-11 |
|
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: 62.51 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:cd03298 129 LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
...
gi 767920345 78 ERG 80
Cdd:cd03298 209 AQG 211
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
198-475 |
8.56e-11 |
|
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: 63.66 E-value: 8.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 198 LVGSVGAAVNGTVTPLYAFLFSQILgtfsI--PDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRK 275
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRA----IdgPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 276 FGFRAMLGQDIAWFDDLRnsPGALTTRLATDASQVQGAAGSQIGMIVNSFTnVTVAMIIAFSFSWKLSLVILCFFPFLAL 355
Cdd:cd18543 77 DLFAHLQRLDGAFHDRWQ--SGQLLSRATSDLSLVQRFLAFGPFLLGNLLT-LVVGLVVMLVLSPPLALVALASLPPLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 356 SGATQTRMLTGfASRDKQalEMVGQIT---NEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQC 432
Cdd:cd18543 154 VARRFRRRYFP-ASRRAQ--DQAGDLAtvvEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 433 IMFIANSASYRYGGYLISNEGL-------HFSYV------FRVISAVVLSA----TALGR 475
Cdd:cd18543 231 LPELGLAAVLALGGWLVANGSLtlgtlvaFSAYLtmlvwpVRMLGWLLAMAqrarAAAER 290
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
536-745 |
1.02e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.11 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQ---GKVMIDGHDSKKV-----NVQFLRSNIGIVSQEPVL 607
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREgrlarDIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 608 F-ACSIMDNIKYGdNTKEIPMERV-IAAAKQAQLHDFVMSLpekyeTNVG------SQGSQLSRGEKQRIAIARAIVRDP 679
Cdd:PRK09984 98 VnRLSVLENVLIG-ALGSTPFWRTcFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 680 KILLLDEATSALDTESEKTVQVALD--KAREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-91 |
1.14e-10 |
|
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: 62.31 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALdneSEAMVQEVLSKIQH----GHTIISVAHRLSTVRA-ADTIIGFEHGT 75
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPSLGL---APLIVEEIFEIIRRlnreGVTILLVEQNARFALEiADRAYVLERGR 213
|
90
....*....|....*.
gi 767920345 76 AVERGTHEELLERKGV 91
Cdd:COG0410 214 IVLEGTAAELLADPEV 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
537-746 |
1.18e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.70 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQepvlfacsimDNI 616
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ----------NAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 617 KYGDntkeIPMERVIAAAKQAQLHDFVMSLPEKYE-----------TNVGSQG-SQLSRGEKQRIAIARAIVRDPKILLL 684
Cdd:PRK10253 92 TPGD----ITVQELVARGRYPHQPLFTRWRKEDEEavtkamqatgiTHLADQSvDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 685 DEATSALDTESE-KTVQVALDKARE-GRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELM 746
Cdd:PRK10253 168 DEPTTWLDISHQiDLLELLSELNREkGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-87 |
1.19e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.55 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHR-LSTVRAADTIIGFEHGTAVER 79
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEV 229
|
....*...
gi 767920345 80 GTHEELLE 87
Cdd:PRK14267 230 GPTRKVFE 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1-75 |
1.33e-10 |
|
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: 60.15 E-value: 1.33e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQhgHTIISVAH-R--LSTVraADTIIGFEHGT 75
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
534-743 |
1.58e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.35 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERF--YDPDQGKVMIDGHDSKKVNVQfLRSNIGI--VSQEPVLFA 609
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 -CSIMDNIKYGDNTKEipmerviaaaKQAQLHD-----FVMSLPEKYETnVGSQGSQLSR--------GEKQRIAIARAI 675
Cdd:CHL00131 98 gVSNADFLRLAYNSKR----------KFQGLPEldpleFLEIINEKLKL-VGMDPSFLSRnvnegfsgGEKKRNEILQMA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 676 VRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIV-IAH--RLSTIQNADIIAVMAQGVVIEKGTHE 743
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
534-719 |
1.60e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.05 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMidgHDSKkvnvqfLRsnIGIVSQ----EPVL-F 608
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGK------LR--IGYVPQklylDTTLpL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 609 ACSIMDNIKYGDNTKEI--PMERVIAAakqaQLHDFVMSlpekyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:PRK09544 85 TVNRFLRLRPGTKKEDIlpALKRVQAG----HLIDAPMQ--------------KLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 767920345 687 ATSALDTESektvQVAL----DKAREGRTCIV--IAHRL 719
Cdd:PRK09544 147 PTQGVDVNG----QVALydliDQLRRELDCAVlmVSHDL 181
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-86 |
1.88e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.51 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRL-STVRAADTIIGFEHGTAV 77
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVV 244
|
....*....
gi 767920345 78 ERGTHEELL 86
Cdd:PRK10070 245 QVGTPDEIL 253
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1-29 |
1.91e-10 |
|
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: 59.58 E-value: 1.91e-10
10 20
....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATS 29
Cdd:pfam00005 122 LSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-86 |
2.40e-10 |
|
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: 61.64 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLStvraaDTIIGFEH----- 73
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVE-----EIPPGITHvlllk 217
|
90
....*....|....
gi 767920345 74 -GTAVERGTHEELL 86
Cdd:COG1119 218 dGRVVAAGPKEEVL 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
531-734 |
2.64e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNV----QFLRSNIGIVSQE-P 605
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFksskEALENGISMVHQElN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 606 VLFACSIMDNIKYGdntkEIPMERVIaaAKQAQLHDFVMSLPEKYETNVG--SQGSQLSRGEKQRIAIARAIVRDPKILL 683
Cdd:PRK10982 84 LVLQRSVMDNMWLG----RYPTKGMF--VDQDKMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 684 LDEATSALdteSEKTVQ---VALDKAREgRTC--IVIAHRLSTI-QNADIIAVMAQG 734
Cdd:PRK10982 158 MDEPTSSL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDG 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-86 |
2.84e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.93 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADTIIGFEHGTAVER 79
Cdd:PRK13644 137 LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
....*..
gi 767920345 80 GTHEELL 86
Cdd:PRK13644 217 GEPENVL 223
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
533-743 |
3.11e-10 |
|
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: 61.23 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 533 PDSQVLNGLSVsISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV------------------------MIDGHDSKK 588
Cdd:cd03236 12 PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildefrgselqnyftkLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 589 VNVQFlrsnigiVSQEPVLFACSIMDNIKYGD--NTKEIPMERviaaakqaqlhdfvMSLPEKYETNVgsqgSQLSRGEK 666
Cdd:cd03236 91 VKPQY-------VDLIPKAVKGKVGELLKKKDerGKLDELVDQ--------------LELRHVLDRNI----DQLSGGEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 667 QRIAIARAIVRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVM-----AQGVV-IE 738
Cdd:cd03236 146 QRVAIAAALARDADFYFFDEPSSYLDIKQRLNAaRLIRELAEDDNYVLVVEHDLAVLDYlSDYIHCLygepgAYGVVtLP 225
|
....*
gi 767920345 739 KGTHE 743
Cdd:cd03236 226 KSVRE 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-92 |
3.15e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.18 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEA-MVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILK 256
|
90
....*....|....
gi 767920345 79 RGTHEELLERKGVY 92
Cdd:PRK13631 257 TGTPYEIFTDQHII 270
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1-84 |
3.24e-10 |
|
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: 60.91 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSAL-DNESEAMVqEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:cd03219 144 LSYGQQRRLEIARALATDPKLLLLDEPAAGLnPEETEELA-ELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
....*..
gi 767920345 78 ERGTHEE 84
Cdd:cd03219 223 AEGTPDE 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
538-738 |
3.55e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPD---QGKVMIDG--------HDSKKVNvqflrsnIGIVSQE-- 604
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfkdiRDSEALG-------IVIIHQEla 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 605 --PVLfacSIMDNIKYGDntkEIPMERVI----AAAKQAQLHDFVmSLPEKYETNVGSQGSqlsrGEKQRIAIARAIVRD 678
Cdd:NF040905 89 liPYL---SIAENIFLGN---ERAKRGVIdwneTNRRARELLAKV-GLDESPDTLVTDIGV----GKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 679 PKILLLDEATSAL-DTESEKTVQVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIE 738
Cdd:NF040905 158 VKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-85 |
4.30e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.57 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVF 225
|
....*...
gi 767920345 78 ERGTHEEL 85
Cdd:PRK13634 226 LQGTPREI 233
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
234-441 |
5.02e-10 |
|
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: 61.35 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 234 RSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQG- 312
Cdd:cd18546 35 LGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSEl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 313 AAGSQIGMIVNSFTNVTVAmIIAFSFSWKLSLVILCFFPFLALsgAT-QTRMLTGFASRdkQALEMVGQIT---NEALSN 388
Cdd:cd18546 113 LQTGLVQLVVSLLTLVGIA-VVLLVLDPRLALVALAALPPLAL--ATrWFRRRSSRAYR--RARERIAAVNadlQETLAG 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767920345 389 IRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFaqcIMFIANSAS 441
Cdd:cd18546 188 IRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPG---VELLGNLAT 237
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
202-408 |
5.07e-10 |
|
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: 61.43 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 202 VGAAVNGTV--TPLYAFLFSQILGTfsipdkEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFR 279
Cdd:cd18565 22 IGVAIDAVFngEASFLPLVPASLGP------ADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 280 AMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLAL-SGA 358
Cdd:cd18565 96 HVQRLDMAFFED--RQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAgTYW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767920345 359 TQTRMLTGFASRDKQALEMVGQITNeALSNIRTVAGIGKERRFIEALETE 408
Cdd:cd18565 174 FQRRIEPRYRAVREAVGDLNARLEN-NLSGIAVIKAFTAEDFERERVADA 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
539-745 |
5.13e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.77 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 539 NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-----SKKV----------NVQFLRS-----NI 598
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpGHQIarmgvvrtfqHVRLFREmtvieNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 599 gIVSQ----EPVLFAcSIMDNIKYGDNTKEiPMERVIAAAKQAQLHDFVmslpekyetnvGSQGSQLSRGEKQRIAIARA 674
Cdd:PRK11300 102 -LVAQhqqlKTGLFS-GLLKTPAFRRAESE-ALDRAATWLERVGLLEHA-----------NRQAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920345 675 IVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 745
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1-57 |
6.61e-10 |
|
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: 60.17 E-value: 6.61e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 57
Cdd:TIGR01184 115 LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIweEHRVTVLMVTH 173
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-86 |
6.98e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVER 79
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEW 233
|
....*..
gi 767920345 80 GTHEELL 86
Cdd:PRK14246 234 GSSNEIF 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-88 |
9.31e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.93 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAH-RLSTVRAADTIIGFEHGTAVER 79
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEW 226
|
....*....
gi 767920345 80 GTHEELLER 88
Cdd:PRK14247 227 GPTREVFTN 235
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-89 |
9.62e-10 |
|
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: 59.46 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:TIGR03410 133 SGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVA 212
|
90
....*....|.
gi 767920345 79 RGTHEELLERK 89
Cdd:TIGR03410 213 SGAGDELDEDK 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-118 |
1.17e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.12 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD--NeSEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:COG4152 130 LSKGNQQKVQLIAALLHDPELLILDEPFSGLDpvN-VELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKV 208
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767920345 78 ERGTHEELLERKGVYFTLVTLQSQGNQALNEEDIKDATEDD 118
Cdd:COG4152 209 LSGSVDEIRRQFGRNTLRLEADGDAGWLRALPGVTVVEEDG 249
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-86 |
1.22e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.11 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLS-TVRAADTIIGFEHGTAVER 79
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEE 243
|
....*..
gi 767920345 80 GTHEELL 86
Cdd:PRK14271 244 GPTEQLF 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-68 |
1.23e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.19 E-value: 1.23e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALdNESEAmvqEVLSKI-----QHGHTIISVAHRLSTVRA-ADTI 68
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASL-TEREV---ERLFRIirrlkAQGVAIIYISHRLDEVFEiADRV 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-78 |
1.35e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 59.70 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVeRFCQRVMVMDNGQIV 231
|
.
gi 767920345 78 E 78
Cdd:PRK10419 232 E 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
531-696 |
1.40e-09 |
|
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: 58.66 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFAC 610
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 SIMDNIKY--GDNTKeipmERVIAAAKQAQLHDFvmslpEKYETNvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEAT 688
Cdd:cd03231 89 SVLENLRFwhADHSD----EQVEEALARVGLNGF-----EDRPVA------QLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
....*...
gi 767920345 689 SALDTESE 696
Cdd:cd03231 154 TALDKAGV 161
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-89 |
1.41e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.84 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNES-EAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIK 225
|
90
....*....|.
gi 767920345 79 RGTHEELLERK 89
Cdd:PRK13641 226 HASPKEIFSDK 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-85 |
1.41e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.72 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEamvQEVLSKIQ-----HGHTIISVAHRLSTVRAADTIIGFEHGT 75
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR---REVVNTIKelnkkYGITIILITHYMEEAVEADRIIVMDSGK 221
|
90
....*....|
gi 767920345 76 AVERGTHEEL 85
Cdd:PRK13633 222 VVMEGTPKEI 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-88 |
1.43e-09 |
|
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: 61.24 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQreLGMALLLITHDLGVVRRfADRVAVMRQGEIV 236
|
90
....*....|.
gi 767920345 78 ERGTHEELLER 88
Cdd:COG4172 237 EQGPTAELFAA 247
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2-57 |
1.43e-09 |
|
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: 58.42 E-value: 1.43e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAH 57
Cdd:cd03226 128 SGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITH 184
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
199-452 |
1.59e-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: 59.87 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 199 VGSVGAAVNGTVTPLyafLFSQILGTFSIPDKEEQRSQINGV-------CLLFVAMgcvSLFTqFLQGYAFAKSGELLTK 271
Cdd:cd18574 3 LSALAAALVNIQIPL---LLGDLVNVISRSLKETNGDFIEDLkkpalklLGLYLLQ---SLLT-FAYISLLSVVGERVAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 272 RLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFP 351
Cdd:cd18574 76 RLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 352 FLALSGATQTRMLTGFAsrdKQALEMVGQITN---EALSNIRTVAGIGKERRFIEALETELEKPFKTAIQkaniYGFCFA 428
Cdd:cd18574 154 VVVLVGTLYGSFLRKLS---RRAQAQVAKATGvadEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEK----LGLGIG 226
|
250 260
....*....|....*....|....*...
gi 767920345 429 FAQCIMFIA-NS---ASYRYGGYLISNE 452
Cdd:cd18574 227 IFQGLSNLAlNGivlGVLYYGGSLVSRG 254
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-69 |
1.77e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.28 E-value: 1.77e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADTII 69
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVI 214
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
531-742 |
1.87e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKST-SIQLLERF-YDPDQGKVMIDGHDSKKVNVQfLRSNIGI--VSQEPV 606
Cdd:PRK09580 10 SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 --------LFACSIMDNI-KYGDNTkeiPMERViaaakqaQLHDFV------MSLPEKYET---NVGSQGsqlsrGEKQR 668
Cdd:PRK09580 89 eipgvsnqFFLQTALNAVrSYRGQE---PLDRF-------DFQDLMeekialLKMPEDLLTrsvNVGFSG-----GEKKR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 669 IAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREG-RTCIVIAH--RLSTIQNADIIAVMAQGVVIEKGTH 742
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-88 |
1.90e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.12 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD-NESEAMvQEVLSKIQHGHTIIS--VAHRLSTVRA-ADTIIGFEHGTA 76
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDaNLRRSM-REKIRELQQQFNITSlyVTHDQSEAFAvSDTVIVMNKGKI 215
|
90
....*....|..
gi 767920345 77 VERGTHEELLER 88
Cdd:PRK11432 216 MQIGSPQELYRQ 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
527-694 |
2.13e-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: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYPSRpdSQVLNGLSVSISPG-----QTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnvqflrsnigiV 601
Cdd:cd03237 1 YTYPTM--KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 602 SQEPVLFacsimdNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSlPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKI 681
Cdd:cd03237 64 SYKPQYI------KADYEGTVRDLLSSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170
....*....|...
gi 767920345 682 LLLDEATSALDTE 694
Cdd:cd03237 137 YLLDEPSAYLDVE 149
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-83 |
2.35e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.19 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVaiarALIRN----PKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFE-H 73
Cdd:PRK10247 138 LSGGEKQRI----SLIRNlqfmPKVLLLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQpH 213
|
90
....*....|
gi 767920345 74 GTAVERGTHE 83
Cdd:PRK10247 214 AGEMQEARYE 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-74 |
2.68e-09 |
|
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: 57.80 E-value: 2.68e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHG 74
Cdd:cd03292 137 LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVdTTRHRVIALERG 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
531-748 |
2.89e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.35 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQV--LNGLSVSISPGQTLAFVGSSGCGKS-TSIQLLERFYDPDQ--GKVMIDGHD-----SKKVNVqfLRS-NIG 599
Cdd:PRK09473 23 STPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREilnlpEKELNK--LRAeQIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 600 IVSQEPVlfaCSIMDNIKYGDNTKEIPMerviaaakqaqLHDFvMSLPEKYETNV---------------GSQGSQLSRG 664
Cdd:PRK09473 101 MIFQDPM---TSLNPYMRVGEQLMEVLM-----------LHKG-MSKAEAFEESVrmldavkmpearkrmKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 665 EKQRIAIARAIVRDPKILLLDEATSALDTesekTVQVAL-----DKAREGRTCIV-IAHRLSTIQN-ADIIAVMAQGVVI 737
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDV----TVQAQImtllnELKREFNTAIImITHDLGVVAGiCDKVLVMYAGRTM 241
|
250
....*....|.
gi 767920345 738 EKGTHEELMAQ 748
Cdd:PRK09473 242 EYGNARDVFYQ 252
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
533-720 |
3.11e-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: 60.53 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 533 PDSQVL-NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvnvqflRSNIGIVSQEPVLFACS 611
Cdd:TIGR00954 462 PNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 612 IMDNIKYGDNTKEIPMERV-----IAAAKQAQLHDFVmslpekyETNVGSQGSQ-----LSRGEKQRIAIARAIVRDPKI 681
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLsdkdlEQILDNVQLTHIL-------EREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQF 603
|
170 180 190
....*....|....*....|....*....|....*....
gi 767920345 682 LLLDEATSALDTESEKTVQVALDKAreGRTCIVIAHRLS 720
Cdd:TIGR00954 604 AILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
534-748 |
3.42e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---------SKKVNVQFLRSNIGIVSQe 604
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHitrlsfeqlQKLVSDEWQRNNTDMLSP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 605 pvlfacsimDNIKYGDNTKEIPMERVIAAAKQAQLH-----DFVMSLPEKYetnvgsqgsqLSRGEKQRIAIARAIVRDP 679
Cdd:PRK10938 94 ---------GEDDTGRTTAEIIQDEVKDPARCEQLAqqfgiTALLDRRFKY----------LSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 680 KILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 748
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-80 |
3.45e-09 |
|
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: 57.59 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 80
Cdd:cd03264 132 SGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-81 |
3.96e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.25 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG 231
|
.
gi 767920345 81 T 81
Cdd:PRK14243 232 G 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
536-691 |
4.72e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.58 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFA-CSIM 613
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKIMREAVAIVPEGRRVFSrMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 614 DNIKYGD--NTKEIPMERViaaakqAQLHDFvmsLPEKYETNVGSQGSqLSRGEKQRIAIARAIVRDPKILLLDEATSAL 691
Cdd:PRK11614 99 ENLAMGGffAERDQFQERI------KWVYEL---FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
531-746 |
5.28e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLE-RFYDPD-------QGKVMIDGHDSKKVNVQFLRSNIGIVS 602
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 603 Q--EPVlFACSIMDNIKYGdntkEIPMERVIAAAKQA--QLHDFVMSLPEKyETNVGSQGSQLSRGEKQRIAIARAI--- 675
Cdd:PRK13547 90 QaaQPA-FAFSAREIVLLG----RYPHARRAGALTHRdgEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 676 ------VRDPKILLLDEATSALD-TESEKTVQVALDKAREGRT-CIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELM 746
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-85 |
5.31e-09 |
|
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: 56.99 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIA 212
|
....*..
gi 767920345 79 RGTHEEL 85
Cdd:cd03265 213 EGTPEEL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-59 |
5.60e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 57.28 E-value: 5.60e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD----NESEAMVQEVLSKIQhgHTIISVAHRL 59
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQ--LTLLMVSHSL 190
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-86 |
6.98e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 4 GQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTI--ISVAHRLSTVR-AADTIIGFEHGTAVERG 80
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKhISDQVLVMHQGEVVERG 232
|
....*.
gi 767920345 81 THEELL 86
Cdd:PRK15112 233 STADVL 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-57 |
7.41e-09 |
|
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: 57.06 E-value: 7.41e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 57
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnrERGTTLVLVTH 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-74 |
8.82e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.33 E-value: 8.82e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLS-TVRAADTIIGFEHG 74
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQG 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1-75 |
9.43e-09 |
|
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: 56.57 E-value: 9.43e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD-NESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGT 75
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
518-694 |
9.93e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 518 GKIDFVDCKFTYpSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVmidgHDSKKVNVQFLRSN 597
Cdd:PRK11147 316 GKIVFEMENVNY-QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 598 IGIVSQEPvlfacSIMDNIkyGDNTKEIPM---ERVIAaakqAQLHDFVMSlPEKYETNVgsqgSQLSRGEKQRIAIARA 674
Cdd:PRK11147 391 RAELDPEK-----TVMDNL--AEGKQEVMVngrPRHVL----GYLQDFLFH-PKRAMTPV----KALSGGERNRLLLARL 454
|
170 180
....*....|....*....|
gi 767920345 675 IVRDPKILLLDEATSALDTE 694
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVE 474
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
531-695 |
1.20e-08 |
|
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: 55.83 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFAC 610
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 SIMDNIKYgdntkeipmerviaaakQAQLHDFVMSLPEKYETNVGSQG------SQLSRGEKQRIAIARAIVRDPKILLL 684
Cdd:TIGR01189 89 SALENLHF-----------------WAAIHGGAQRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170
....*....|.
gi 767920345 685 DEATSALDTES 695
Cdd:TIGR01189 152 DEPTTALDKAG 162
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-84 |
1.60e-08 |
|
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: 56.20 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLD-----MATSaldnESEAMVqEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFE 72
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDepaagLNPE----ETEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLD 227
|
90
....*....|..
gi 767920345 73 HGTAVERGTHEE 84
Cdd:COG0411 228 FGRVIAEGTPAE 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-86 |
1.68e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 56.64 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAHRLSTVRAADTIIGFEHGTAVE 78
Cdd:PRK13642 141 LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIK 220
|
....*...
gi 767920345 79 RGTHEELL 86
Cdd:PRK13642 221 EAAPSELF 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
520-726 |
1.72e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 520 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKK------VNVQF 593
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlctyqKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 594 LRSNIGIvsqEPVLfacSIMDNIKYGDNTKEIPME--RVIAAAKQAQLHDFVMSLpekyetnvgsqgsqLSRGEKQRIAI 671
Cdd:PRK13540 79 VGHRSGI---NPYL---TLRENCLYDIHFSPGAVGitELCRLFSLEHLIDYPCGL--------------LSSGQKRQVAL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 672 ARAIVRDPKILLLDEATSALDTESEKTVQVALDKAR-EGRTCIVIAHRLSTIQNAD 726
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-86 |
1.86e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.79 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCV 236
|
....*....
gi 767920345 78 ERGTHEELL 86
Cdd:PRK15134 237 EQNRAATLF 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-111 |
1.90e-08 |
|
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: 57.50 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSK--IQHGHTIISVAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIeDLSDKAIWLENGEIK 248
|
90 100 110
....*....|....*....|....*....|....
gi 767920345 78 ERGTHEELLErkgVYFTLVTLQSQGNQALNEEDI 111
Cdd:TIGR03269 249 EEGTPDEVVA---VFMEGVSEVEKECEVEVGEPI 279
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
534-751 |
2.06e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIdghdSKKvnvqflrSNIGIVSQEPVL-FAC-- 610
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW----SEN-------ANIGYYAQDHAYdFENdl 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 SIMDNI----KYGDNtkeipmERVIAAAkqaqLHDFVMSlpekyETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:PRK15064 400 TLFDWMsqwrQEGDD------EQAVRGT----LGRLLFS-----QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 687 ATSALDTESEKTVQVALDKArEGrTCIVIAH------RLSTiqnaDIIAVMAQGVVIEKGTHEELMAQKGA 751
Cdd:PRK15064 465 PTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-87 |
2.35e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.77 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNE-SEAMVQEVLSKIQH-GHTIISVAH-RLSTVRAADTIIGFEHGTAV 77
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFV 229
|
90
....*....|
gi 767920345 78 ERGTHEELLE 87
Cdd:PRK11607 230 QIGEPEEIYE 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-93 |
3.01e-08 |
|
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: 55.04 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLS-TVRAADTIIGFEHGTAV 77
Cdd:cd03296 137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIE 216
|
90
....*....|....*.
gi 767920345 78 ERGTHEELLERKGVYF 93
Cdd:cd03296 217 QVGTPDEVYDHPASPF 232
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
531-694 |
3.30e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 531 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNvqflRSN-IGIVSQEPVLFA 609
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 -CSIMDNIKY-----GDNTKEIPMERVIaaakqaqlhdfVMSLPEKYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILL 683
Cdd:PRK13543 96 dLSTLENLHFlcglhGRRAKQMPGSALA-----------IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWL 160
|
170
....*....|.
gi 767920345 684 LDEATSALDTE 694
Cdd:PRK13543 161 LDEPYANLDLE 171
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-48 |
3.79e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.09 E-value: 3.79e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH 48
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQ 176
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
471-755 |
3.81e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 471 TALGRAFSYTPSYAKAKISAARF--FQLLDRQPPISVYNtAGEKWDnfqgKIDFVDCKFTYPSRPDSqvLNGLSVSISPG 548
Cdd:PRK10522 277 TPLLSAVGALPTLLSAQVAFNKLnkLALAPYKAEFPRPQ-AFPDWQ----TLELRNVTFAYQDNGFS--VGPINLTIKRG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 549 QTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSImdnikyGDNTKEIPME 628
Cdd:PRK10522 350 ELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL------GPEGKPANPA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 629 RVIAAAKQAQLHDFVmSLPEKYETNVgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV-QVALDKAR 707
Cdd:PRK10522 424 LVEKWLERLKMAHKL-ELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQ 497
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767920345 708 E-GRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 755
Cdd:PRK10522 498 EmGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAVART 546
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-89 |
3.96e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.99 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLrSLLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIA 252
|
90
....*....|.
gi 767920345 79 RGTHEELLERK 89
Cdd:PRK13536 253 EGRPHALIDEH 263
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1-87 |
4.48e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.59 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLST--VRAADTIIGFEHGTAV 77
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVA 246
|
90
....*....|
gi 767920345 78 ERGTHEELLE 87
Cdd:TIGR00955 247 YLGSPDQAVP 256
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-86 |
5.78e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIR------NPKILLLDMATSALDneseamvqevlskIQHGHTIISVAHRLS--------------- 60
Cdd:PRK13548 136 SGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD-------------LAHQHHVLRLARQLAherglavivvlhdln 202
|
90 100
....*....|....*....|....*..
gi 767920345 61 -TVRAADTIIGFEHGTAVERGTHEELL 86
Cdd:PRK13548 203 lAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1-75 |
8.84e-08 |
|
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: 52.71 E-value: 8.84e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 1 MSGGQKQRVAIARALIRNPK--ILLLDMATSALDNESEAMVQEVLSK-IQHGHTIISVAHRLSTVRAADTIIGFEHGT 75
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-85 |
8.96e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVaEAAHKIIVMYAGQVV 233
|
....*...
gi 767920345 78 ERGTHEEL 85
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-32 |
9.28e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 54.70 E-value: 9.28e-08
10 20 30
....*....|....*....|....*....|..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD 32
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-85 |
9.57e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 54.32 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTKRTIFFKDGKIIK 245
|
....*...
gi 767920345 79 RG-THEEL 85
Cdd:PRK13651 246 DGdTYDIL 253
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
528-695 |
1.08e-07 |
|
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: 55.33 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTsiqLLerfydpdqgKVM--IDghdsKKVNVQFLRS---NIGIVS 602
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKST---LL---------RIMagVD----KDFNGEARPQpgiKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 603 QEP-----------VLFACS----IMD-----NIKYGDNTKEipMERViaAAKQAQLHDFV------------------M 644
Cdd:TIGR03719 75 QEPqldptktvrenVEEGVAeikdALDrfneiSAKYAEPDAD--FDKL--AAEQAELQEIIdaadawdldsqleiamdaL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767920345 645 SLPEKyETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 695
Cdd:TIGR03719 151 RCPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-74 |
1.46e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.27 E-value: 1.46e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHrlSTVRA---ADTIIGFEHG 74
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTH--DQVEAmtlADKIVVLDAG 210
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
534-728 |
1.47e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.57 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIdgHDSKKVNVQ-----FLRSNIGIVSQEPVLf 608
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAkpyctYIGHNLGLKLEMTVF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 609 acsimDNIKYgdnTKEI--PMERVIAAAKQAQLHDFvmsLPEKYETnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:PRK13541 89 -----ENLKF---WSEIynSAETLYAAIHYFKLHDL---LDEKCYS--------LSSGMQKIVAIARLIACQSDLWLLDE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767920345 687 ATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQNADII 728
Cdd:PRK13541 150 VETNLSKENRDLLnNLIVMKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
538-729 |
1.72e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQ-----TLAFVGSSGCGKSTSIQLLERFYDPDQGKVmidghdSKKVNV----QFLRSNI-GIVSQepvl 607
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------DPELKIsykpQYIKPDYdGTVED---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 608 FACSIMDNikYGDN--TKEIpmerviaaAKQAQLHDFvmslpekYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLD 685
Cdd:PRK13409 420 LLRSITDD--LGSSyyKSEI--------IKPLQLERL-------LDKNV----KDLSGGELQRVAIAACLSRDADLYLLD 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767920345 686 EATSALDTESEKTVQVALDKAREGR--TCIVIAHRLSTIqnaDIIA 729
Cdd:PRK13409 479 EPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYIS 521
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-91 |
1.73e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 53.31 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:PRK13636 142 LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRVI 221
|
90
....*....|....
gi 767920345 78 ERGTHEELLERKGV 91
Cdd:PRK13636 222 LQGNPKEVFAEKEM 235
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-87 |
1.82e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD----NESEAMVQEvLSKiQHGHTIISVAHRLS-TVRAADTIIGFEHGT 75
Cdd:PRK10575 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHR-LSQ-ERGLTVIAVLHDINmAARYCDYLVALRGGE 225
|
90
....*....|..
gi 767920345 76 AVERGTHEELLE 87
Cdd:PRK10575 226 MIAQGTPAELMR 237
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-59 |
1.93e-07 |
|
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: 54.29 E-value: 1.93e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRL 59
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-46 |
2.12e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.94 E-value: 2.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI 46
Cdd:COG4525 136 SGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
272-406 |
2.23e-07 |
|
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: 53.24 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 272 RLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFP 351
Cdd:cd18589 70 RLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLP 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 352 FLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKE----RRFIEALE 406
Cdd:cd18589 148 LLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEegeaQRYRQRLQ 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-60 |
2.69e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.13 E-value: 2.69e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS 60
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-57 |
2.76e-07 |
|
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: 52.12 E-value: 2.76e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAH 57
Cdd:cd03263 134 LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1-108 |
2.99e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 52.70 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVI 230
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767920345 78 ERG------THEELL-----ERKGVYFTLVTLQSQGNQALNE 108
Cdd:PRK13645 231 SIGspfeifSNQELLtkieiDPPKLYQLMYKLKNKGIDLLNK 272
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-32 |
3.11e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.34 E-value: 3.11e-07
10 20 30
....*....|....*....|....*....|..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD 32
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-89 |
3.23e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.89 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLrSLLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIA 218
|
90
....*....|.
gi 767920345 79 RGTHEELLERK 89
Cdd:PRK13537 219 EGAPHALIESE 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
530-747 |
3.23e-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: 53.68 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 530 PSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPDQ--GKVMIDGHDSKKVN-VQFLRSNIGIVSQE-- 604
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGKPVDIRNpAQAIRAGIAMVPEDrk 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 605 -----PVLfacSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSqLSRGEKQRIAIARAIVRDP 679
Cdd:TIGR02633 347 rhgivPIL---GVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 680 KILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQG-----VVIEKGTHEELMA 747
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGklkgdFVNHALTQEQVLA 497
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2-53 |
3.69e-07 |
|
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: 51.89 E-value: 3.69e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTII 53
Cdd:cd03234 145 SGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIV 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-86 |
4.48e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHGTAV 77
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIV 223
|
....*....
gi 767920345 78 ERGTHEELL 86
Cdd:PRK10253 224 AQGAPKEIV 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-88 |
4.62e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.01 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVaRLADDVAVMSHGRIV 220
|
90
....*....|.
gi 767920345 78 ERGTHEELLER 88
Cdd:PRK10418 221 EQGDVETLFNA 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-86 |
5.66e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 51.55 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMA 218
|
....*...
gi 767920345 79 RGTHEELL 86
Cdd:PRK11231 219 QGTPEEVM 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-68 |
5.75e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 5.75e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 3 GGQKQRVAIARALIRNPKILLLDMATSALdNESEAmvqEVLSKI-----QHGHTIISVAHRLSTVRA-ADTI 68
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASL-TESET---AVLLDIirdlkAHGIACIYISHKLNEVKAiSDTI 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-74 |
7.03e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.58 E-value: 7.03e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLS--KIQHGHTIISVAHRLSTVRAADTIIGFEHG 74
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
533-747 |
8.36e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.24 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 533 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTS----IQLLERFYDPDQGKVMIDGhdsKKVNVQFLRsniGIVsqepvlf 608
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDG---KPVAPCALR---GRK------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 609 ACSIMDNIK--------YGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPK 680
Cdd:PRK10418 81 IATIMQNPRsafnplhtMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 681 ILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 747
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
540-717 |
8.40e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.19 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 540 GLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNI------GIVS----QEPVLFA 609
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpGIKTeltaLENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNikYGDntkeipmERVIAAAKQAQLHDFvMSLPekyetnvgsqGSQLSRGEKQRIAIARAIVRDPKILLLDEATS 689
Cdd:PRK13538 99 QRLHGP--GDD-------EALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*....
gi 767920345 690 ALDTESEKTVQVALDK-AREGRTCIVIAH 717
Cdd:PRK13538 159 AIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-68 |
8.46e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 8.46e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSAL-DNESE-------AMVQEvlskiqhGHTIISVAHRLSTVRA-ADTI 68
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADelfeilrRLAAE-------GKSIIFITHKLREVMAiADRV 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-85 |
8.53e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 51.23 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVyADKVYVMSDGKIIK 217
|
....*..
gi 767920345 79 RGTHEEL 85
Cdd:PRK13639 218 EGTPKEV 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-116 |
9.76e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 50.89 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVE 78
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLA 218
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767920345 79 RG-----THEELLERKGVYFTLVT-----LQSQGNQALnEEDIKDATE 116
Cdd:PRK13647 219 EGdksllTDEDIVEQAGLRLPLVAqifedLPELGQSKL-PLTVKEAVQ 265
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
659-736 |
9.78e-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: 52.09 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 659 SQLSRGEKQRIAIARAIVRDPKILLLDEATSALD-TESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVM----- 731
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAILDYlADYVHILygepg 290
|
....*
gi 767920345 732 AQGVV 736
Cdd:COG1245 291 VYGVV 295
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-101 |
1.02e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.16 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISvAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNHVIIS-SHDIDLIyEISDAVYVLRQGQIL 215
|
90 100 110
....*....|....*....|....*....|.
gi 767920345 78 ERG------THEELLERKGVYFT-LVTLQSQ 101
Cdd:PRK13638 216 THGapgevfACTEAMEQAGLTQPwLVKLHTQ 246
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-89 |
1.20e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.90 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVL 225
|
90
....*....|....*..
gi 767920345 79 RGT------HEELLERK 89
Cdd:PRK13649 226 SGKpkdifqDVDFLEEK 242
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-85 |
1.21e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.26 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTME 242
|
....*..
gi 767920345 79 RGTHEEL 85
Cdd:PRK09473 243 YGNARDV 249
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-80 |
1.28e-06 |
|
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: 49.97 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRAVL 208
|
..
gi 767920345 79 RG 80
Cdd:cd03269 209 YG 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-57 |
1.40e-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: 51.47 E-value: 1.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLskIQHGHTIISVAH 57
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL--QEYPGTVVAVTH 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-87 |
1.57e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.50 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVR-AADTIIGFEHGTAVE 78
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIIS 224
|
....*....
gi 767920345 79 RGTHEELLE 87
Cdd:PRK13643 225 CGTPSDVFQ 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-88 |
1.79e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.19 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpeTYGMTVIFSTHQLDLVpEMADYIYVMDKGRIV 217
|
90
....*....|.
gi 767920345 78 ERGTHEELLER 88
Cdd:PRK13652 218 AYGTVEEIFLQ 228
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
528-695 |
2.48e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 528 TYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTsiqLLerfydpdqgKVM--IDghdsKKVNVQFLRS---NIGIVS 602
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKST---LL---------RIMagVD----KEFEGEARPApgiKVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 603 QEPVLfacsimdnikygDNTK---EIPMERV------------IAA-------------AKQAQLHDFV----------- 643
Cdd:PRK11819 77 QEPQL------------DPEKtvrENVEEGVaevkaaldrfneIYAayaepdadfdalaAEQGELQEIIdaadawdldsq 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 644 -------MSLPEKyETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 695
Cdd:PRK11819 145 leiamdaLRCPPW-DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
538-728 |
2.67e-06 |
|
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: 49.54 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQ------LLERFY----DPDQGKvMIDGHD--SKKVNV------QFLRSN-- 597
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLHlkkeQPGNHD-RIEGLEhiDKVIVIdqspigRTPRSNpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 598 --IGIVSQEPVLFaCSIMDNIKYGDNTKEIPME-RVIA-----AAKQAqlHDFVMSLP---EKYET---------NVGSQ 657
Cdd:cd03271 90 tyTGVFDEIRELF-CEVCKGKRYNRETLEVRYKgKSIAdvldmTVEEA--LEFFENIPkiaRKLQTlcdvglgyiKLGQP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 658 GSQLSRGEKQRIAIARAIVR---DPKILLLDEATSALDTESEKTVQVALDKARE-GRTCIVIAHRLSTIQNADII 728
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
534-722 |
2.78e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL-ERFYDP--DQGKVMIDGHdskKVNVQFLRSnIGIVSQEPV-LFA 609
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTTGviTGGDRLVNGR---PLDSSFQRS-IGYVQQQDLhLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 610 CSIMDNIKYG---DNTKEIP----MERViaaakqaqlhDFVMSLPE--KY-ETNVGSQGSQLSRGEKQRIAIARAIVRDP 679
Cdd:TIGR00956 851 STVRESLRFSaylRQPKSVSksekMEYV----------EEVIKLLEmeSYaDAVVGVPGEGLNVEQRKRLTIGVELVAKP 920
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767920345 680 KILL-LDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTI 722
Cdd:TIGR00956 921 KLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAI 965
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-35 |
3.52e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.45 E-value: 3.52e-06
10 20 30
....*....|....*....|....*....|....*
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNES 35
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
659-736 |
3.76e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 659 SQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVM-----A 732
Cdd:PRK13409 211 SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIAygepgA 290
|
....
gi 767920345 733 QGVV 736
Cdd:PRK13409 291 YGVV 294
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2-44 |
4.33e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 48.33 E-value: 4.33e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLS 44
Cdd:PRK13539 129 SAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIR 171
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
240-454 |
4.63e-06 |
|
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: 48.99 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 240 VCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIG 319
Cdd:cd18549 44 IGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDISELAHHGPE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 320 MIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQT-RMLTGF-ASRDKQAlEMVGQITNeALSNIRTVAGIGK 397
Cdd:cd18549 122 DLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNkKMKKAFrRVREKIG-EINAQLED-SLSGIRVVKAFAN 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 398 ERRFIEALETELEKpFKTAIQKANIY-GFCFAFAQCIMFIANSASYRYGGYLISNEGL 454
Cdd:cd18549 200 EEYEIEKFDEGNDR-FLESKKKAYKAmAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEI 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-88 |
5.18e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHT--IISVAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVaEIADRVLVMYQGEAV 248
|
90
....*....|.
gi 767920345 78 ERGTHEELLER 88
Cdd:PRK10261 249 ETGSVEQIFHA 259
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
527-692 |
5.48e-06 |
|
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: 48.03 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 527 FTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL----ERFYDPDqGKVMIDGHDSKKVNVQFlRSNIGIVS 602
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrtEGNVSVE-GDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 603 QEPVLFAcsimdnikygdntkEIPMERVIAAAKQAQLHDFVmslpekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKIL 682
Cdd:cd03233 90 EEDVHFP--------------TLTVRETLDFALRCKGNEFV---------------RGISGGERKRVSIAEALVSRASVL 140
|
170
....*....|
gi 767920345 683 LLDEATSALD 692
Cdd:cd03233 141 CWDNSTRGLD 150
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-87 |
5.50e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVeRISHRVAVMYLGQIVE 544
|
....*....
gi 767920345 79 RGTHEELLE 87
Cdd:PRK10261 545 IGPRRAVFE 553
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
660-747 |
6.60e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.03 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 660 QLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTI-QNADIIAVMAQGVV 736
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 767920345 737 IEKGTHEELMA 747
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-86 |
6.63e-06 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 48.19 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALI-------RNPKILLLDMATSALDneseamvqevlskIQHGHTIISVAHRLS------------- 60
Cdd:COG4559 134 LSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD-------------LAHQHAVLRLARQLArrgggvvavlhdl 200
|
90 100
....*....|....*....|....*...
gi 767920345 61 --TVRAADTIIGFEHGTAVERGTHEELL 86
Cdd:COG4559 201 nlAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
538-729 |
7.12e-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: 49.40 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQ-----TLAFVGSSGCGKSTSIQLLERFYDPDQGKVmidghdSKKVNV----QFLRSNIGIVSQEpVLF 608
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKIsykpQYISPDYDGTVEE-FLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 609 AC--SIMDNIKYgdNTkEIpmerviaaAKQAQLHDFvmslpekYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDE 686
Cdd:COG1245 424 SAntDDFGSSYY--KT-EI--------IKPLGLEKL-------LDKNV----KDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767920345 687 ATSALDTESEKTVQVALDKAREGR--TCIVIAHRLSTIqnaDIIA 729
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIS 523
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
537-747 |
8.75e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.86 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLerF--YDPDQGKVMIDGhdsKKVNV----QFLRSNIGIVS----QEPV 606
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDG---KPVRIrsprDAIRAGIAYVPedrkGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 607 LFACSIMDNI------KYGDNtkeipmeRVIAAAKQAQL-HDFVMSLPEKY---ETNVGSqgsqLSRGEKQRIAIARAIV 676
Cdd:COG1129 342 VLDLSIRENItlasldRLSRG-------GLLDRRRERALaEEYIKRLRIKTpspEQPVGN----LSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 677 RDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIahrlST-----IQNADIIAVMAQGVVI-----EKGTHEEL 745
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIRElAAEGKAVIVI----SSelpelLGLSDRILVMREGRIVgeldrEEATEEAI 486
|
..
gi 767920345 746 MA 747
Cdd:COG1129 487 MA 488
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
537-747 |
8.78e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.87 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL--ERfyDPDQGKVMIDGHDSKKVNV-QFLRSNIGIVSQEPVLFAC--- 610
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRLGVAYIPEDRLGRGLvpd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 -SIMDNIKYGDNTKEiPMER--VI---AAAKQAQlhdfvmSLPEKYE---TNVGSQGSQLSRGEKQRIAIARAIVRDPKI 681
Cdd:COG3845 351 mSVAENLILGRYRRP-PFSRggFLdrkAIRAFAE------ELIEEFDvrtPGPDTPARSLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 682 LLLDEATSALDTESEKTVQVALDKAR-EGRTCIVIAHRLSTIQN-ADIIAVMAQG-----VVIEKGTHEEL---MA 747
Cdd:COG3845 424 LIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGrivgeVPAAEATREEIgllMA 499
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
194-454 |
8.86e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 48.24 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 194 WPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEQrsqINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRL 273
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDG---LTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 274 RKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVqgaagSQI---GMI--VNSFTNVTVAMIIAFSFSWKLSLVILC 348
Cdd:cd18540 78 RKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRL-----GEIiswGLVdlVWGITYMIGILIVMLILNWKLALIVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 349 FFPFLAL-SGATQTRMLtgFASRdkQALEMVGQIT---NEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYG 424
Cdd:cd18540 151 VVPVLAVvSIYFQKKIL--KAYR--KVRKINSRITgafNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSA 226
|
250 260 270
....*....|....*....|....*....|
gi 767920345 425 FCFAFAQCIMFIANSASYRYGGYLISNEGL 454
Cdd:cd18540 227 LFLPIVLFLGSIATALVLWYGGILVLAGAI 256
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1-85 |
1.10e-05 |
|
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: 47.93 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQE-VLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVER 79
Cdd:cd03291 160 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEsCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFY 239
|
....*.
gi 767920345 80 GTHEEL 85
Cdd:cd03291 240 GTFSEL 245
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-60 |
1.25e-05 |
|
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: 48.59 E-value: 1.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIqhGHTIISVAHRLS 60
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-87 |
1.27e-05 |
|
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: 48.65 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL--SKIQHGHTIISVAHRLSTVR-AADTIIGFEHGTAV 77
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLdVCDRAALMRDGKIV 507
|
90
....*....|
gi 767920345 78 ERGTHEELLE 87
Cdd:TIGR03269 508 KIGDPEEIVE 517
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-32 |
1.33e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.92 E-value: 1.33e-05
10 20 30
....*....|....*....|....*....|.
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALD 32
Cdd:PRK11650 136 SGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-57 |
1.45e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQevlskiQHGH----TIISVAH 57
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE------QFLHdypgTVVAVTH 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-68 |
1.54e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 1.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 6 KQRVAIARALIRNPKILLLDMATSALD-NESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTI 68
Cdd:PRK15439 146 RQIVEILRGLMRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRI 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-85 |
1.55e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 47.29 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 4 GQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 80
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrnEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANG 236
|
....*
gi 767920345 81 THEEL 85
Cdd:PRK11300 237 TPEEI 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
536-740 |
1.67e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 536 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL----ERFYDPDQGKVMIDGHDSKKVnVQFLRSNIGIVSQEPVLFA-C 610
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFPhL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 611 SIMDNIKYGDNTKEiPMERVIAAAKQ---AQLHDFVMS---LPEKYETNVGS---QGsqLSRGEKQRIAIARAIVRDPKI 681
Cdd:TIGR00956 154 TVGETLDFAARCKT-PQNRPDGVSREeyaKHIADVYMAtygLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 682 LLLDEATSALDTESektvqvALDKAREGRTCIVIAHRLSTI------QNA----DIIAVMAQGVVIEKG 740
Cdd:TIGR00956 231 QCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFG 293
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1-61 |
1.70e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.34 E-value: 1.70e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESE-AMVQEVLSKIQHGHTIISVAHRLST 61
Cdd:PLN03211 207 ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2-69 |
2.01e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 46.32 E-value: 2.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQE-VLSKI-QHGHTIISVAHRLSTVRAADTII 69
Cdd:COG4136 135 SGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIrQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
545-695 |
2.31e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 545 ISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDghdsKKVNVQFLRsnigivsQEP---VlfACSIMDNIKYGdn 621
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARLQ-------QDPprnV--EGTVYDFVAEG-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 622 TKEI-----------------PMERVIA--AAKQA--------QLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARA 674
Cdd:PRK11147 91 IEEQaeylkryhdishlvetdPSEKNLNelAKLQEqldhhnlwQLENRINEVLAQLGLDPDAALSSLSGGWLRKAALGRA 170
|
170 180
....*....|....*....|.
gi 767920345 675 IVRDPKILLLDEATSALDTES 695
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIET 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-78 |
2.62e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 2.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 4 GQKQRVAIARALIRNPKILLLDMATSAL-DNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-57 |
2.86e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.93 E-value: 2.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAH 57
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH 205
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-25 |
3.37e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 45.79 E-value: 3.37e-05
10 20
....*....|....*....|....
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLD 25
Cdd:COG1137 138 SGGERRRVEIARALATNPKFILLD 161
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
661-747 |
3.69e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 661 LSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAR-EGRTCIVIAHRLSTIQN-ADIIAVMAQGVV-- 736
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsg 475
|
90
....*....|....
gi 767920345 737 ---IEKGTHEELMA 747
Cdd:PRK10762 476 eftREQATQEKLMA 489
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1-85 |
3.69e-05 |
|
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: 47.32 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIR---NPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRAADTII------G 70
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKTADYIIdlgpegG 909
|
90
....*....|....*
gi 767920345 71 FEHGTAVERGTHEEL 85
Cdd:TIGR00630 910 DGGGTVVASGTPEEV 924
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
650-746 |
3.72e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 650 YETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADI 727
Cdd:PRK10982 385 HRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTDR 460
|
90 100
....*....|....*....|....
gi 767920345 728 IAVMAQGVV-----IEKGTHEELM 746
Cdd:PRK10982 461 ILVMSNGLVagivdTKTTTQNEIL 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
530-747 |
3.78e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 530 PSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPD--QGKVMIDGhdsKKVNV----QFLRSNIGIVSQ 603
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGrwEGEIFIDG---KPVKIrnpqQAIAQGIAMVPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 604 E-------PVLfacSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSqLSRGEKQRIAIARAIV 676
Cdd:PRK13549 346 DrkrdgivPVM---GVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIAR-LSGGNQQKAVLAKCLL 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 677 RDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQG-----VVIEKGTHEELMA 747
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIyKLINQLVQQGVAIIVISSELPEVLGlSDRVLVMHEGklkgdLINHNLTQEQVME 499
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
243-454 |
4.08e-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: 46.04 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 243 LFVAMGCVSLFtQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLAtDASQVQGAAGSQIGMIV 322
Cdd:cd18566 48 VVIAILLESLL-RLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFLTGQALLAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 323 NSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFI 402
Cdd:cd18566 124 LDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQML 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767920345 403 EALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGL 454
Cdd:cd18566 204 RRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDL 255
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
506-747 |
5.07e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 506 YNTAGEKWDNFQGKIDFVDCKFTypsRPDSQVLNGLSVSISPGQTLAFVGSSGCGKStsiQLLERFYDPDQ---GKVMID 582
Cdd:PRK09700 250 FNAMKENVSNLAHETVFEVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFGVDKragGEIRLN 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 583 GHD-SKKVNVQFLRSNIGIVSQ---EPVLFA-CSIMDNIKYGDNTK-----------EIPMERVIAAAKQAQLHDFVMSL 646
Cdd:PRK09700 324 GKDiSPRSPLDAVKKGMAYITEsrrDNGFFPnFSIAQNMAISRSLKdggykgamglfHEVDEQRTAENQRELLALKCHSV 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 647 pekyETNVGsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQNA 725
Cdd:PRK09700 404 ----NQNIT----ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITV 475
|
250 260
....*....|....*....|....*....
gi 767920345 726 -DIIAVMAQGVV------IEKGTHEELMA 747
Cdd:PRK09700 476 cDRIAVFCEGRLtqiltnRDDMSEEEIMA 504
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-86 |
5.10e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 46.37 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD-NESEAMVQEVLSKIQHGHTIISVAHRLS-TVRAADTIIGFEHGTAVE 78
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRA 219
|
....*...
gi 767920345 79 RGTHEELL 86
Cdd:PRK09536 220 AGPPADVL 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-90 |
5.48e-05 |
|
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: 44.83 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAH--RLSTVRAADTIIGFEHGTAVE 78
Cdd:cd03217 106 SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
90
....*....|....
gi 767920345 79 RGTHE--ELLERKG 90
Cdd:cd03217 186 SGDKElaLEIEKKG 199
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-74 |
5.63e-05 |
|
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: 44.35 E-value: 5.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHG 74
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELaDAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-96 |
5.64e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.85 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 77
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRII 234
|
90
....*....|....*....
gi 767920345 78 ERGTHEELLERKGVYFTLV 96
Cdd:COG4586 235 YDGSLEELKERFGPYKTIV 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
542-744 |
6.38e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 542 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNVQFLRSNI--GIV------SQEPVLFACSIM 613
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIraGIMlcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 614 DNIKYGDNTKEIPMERVIAAAKQAQLHD-FVMSLpeKYETNVGSQG-SQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 691
Cdd:PRK11288 350 DNINISARRHHLRAGCLINNRWEAENADrFIRSL--NIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 692 DTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEE 744
Cdd:PRK11288 428 DVGAKHEIyNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-59 |
6.82e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 45.46 E-value: 6.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRL 59
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNM 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-68 |
8.25e-05 |
|
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: 45.97 E-value: 8.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 3 GGQKQRVAIARALIRNPKILLLDMATSAL-DNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTI 68
Cdd:TIGR02633 144 GGQQQLVEIAKALNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTI 211
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
661-745 |
8.88e-05 |
|
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: 46.16 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 661 LSRGEKQRIAIARAIVRD---PKILLLDEATSALDTES-EKTVQVALDKAREGRTCIVIAHRLSTIQNAD-IIAV----- 730
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDiKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADyIIDLgpegg 909
|
90
....*....|....*
gi 767920345 731 MAQGVVIEKGTHEEL 745
Cdd:TIGR00630 910 DGGGTVVASGTPEEV 924
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1-75 |
9.12e-05 |
|
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: 44.63 E-value: 9.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGT 75
Cdd:cd03267 154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNreRGTTVLLTSHYMKDIEAlARRVLVIDKGR 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
541-734 |
9.39e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 541 LSVSISPGQTLAFVGSSGCGKStsiQLLERFY---DPDQGKVMIDGHDSKKVNVQfLRSNIGIV-----SQEPVLF---- 608
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYldap 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 609 ----ACSIMDNIK--YGDNTKEipmerviaaakQAQLhdfvmslpEKYETNVG---SQGSQ----LSRGEKQRIAIARAI 675
Cdd:PRK15439 358 lawnVCALTHNRRgfWIKPARE-----------NAVL--------ERYRRALNikfNHAEQaartLSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 676 VRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQG 734
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIyQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQG 479
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-85 |
9.73e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD-NESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 78
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSaREIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
....*..
gi 767920345 79 rgTHEEL 85
Cdd:PRK11288 221 --TFDDM 225
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
659-734 |
9.98e-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: 43.85 E-value: 9.98e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 659 SQLSRGEKQRIAIARAIVRDPK--ILLLDEATSALDTESEKTVQVALDKAR-EGRTCIVIAHRLSTIQNADIIAVMAQG 734
Cdd:cd03238 86 STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-88 |
1.07e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.44 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQhGhTIISVAH-R--LSTVraADTIIGFEHGTAV 77
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVR 508
|
90
....*....|..
gi 767920345 78 ER-GTHEELLER 88
Cdd:COG0488 509 EYpGGYDDYLEK 520
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-102 |
1.17e-04 |
|
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: 45.77 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVER 79
Cdd:TIGR01257 1062 LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCS 1141
|
90 100
....*....|....*....|....*....
gi 767920345 80 GTHEELLE--RKGVYFTLV----TLQSQG 102
Cdd:TIGR01257 1142 GTPLFLKNcfGTGFYLTLVrkmkNIQSQR 1170
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-86 |
1.37e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.79 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAHRLSTV-RAADTIIGFEHGTAV 77
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLsQWADKINVLYCGQTV 238
|
....*....
gi 767920345 78 ERGTHEELL 86
Cdd:PRK15093 239 ETAPSKELV 247
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-69 |
1.38e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 1.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQhgHTIISVAHRLSTVRAADTII 69
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ--GSIIFISHDRSFIRNMATRI 223
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
657-730 |
1.39e-04 |
|
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: 43.33 E-value: 1.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 657 QGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAV 730
Cdd:cd03222 68 QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHV 144
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-91 |
1.54e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 44.10 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALdneSEAMVQEVLSKIQH----GHTIISVAHRLS-TVRAADTIIGFEHGT 75
Cdd:PRK11614 138 MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEQlreqGMTIFLVEQNANqALKLADRGYVLENGH 214
|
90
....*....|....*.
gi 767920345 76 AVERGTHEELLERKGV 91
Cdd:PRK11614 215 VVLEDTGDALLANEAV 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-64 |
1.62e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.95 E-value: 1.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA 64
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMA 186
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-25 |
1.71e-04 |
|
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: 43.69 E-value: 1.71e-04
10 20
....*....|....*....|....
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLD 25
Cdd:cd03218 135 SGGERRRVEIARALATNPKFLLLD 158
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-76 |
1.86e-04 |
|
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: 44.78 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVR-AADTIIGFE-----H 73
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaeNRGKTAMVVDHDIYLIDyISDRLMVFEgepgvH 536
|
...
gi 767920345 74 GTA 76
Cdd:COG1245 537 GHA 539
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-62 |
2.21e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 43.72 E-value: 2.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTV 62
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
538-754 |
2.38e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 538 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvNVQFLRSNIGIVSQ----EPVLFACSIM 613
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQltgiENIEFKMLCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 614 dnikyGDNTKEIP--MERVIaaaKQAQLHDFVMSLPEKYetnvgsqgsqlSRGEKQRIAIARAIVRDPKILLLDEATSAL 691
Cdd:PRK13546 114 -----GFKRKEIKamTPKII---EFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 692 DtesEKTVQVALDKARE----GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQKGAYYK 754
Cdd:PRK13546 175 D---QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLN 239
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1-72 |
2.57e-04 |
|
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: 42.56 E-value: 2.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSK-IQHGH-TIISVAHRLSTVR-AADTIIGFE 72
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRlSEEGKkTALVVEHDLAVLDyLSDRIHVFE 146
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1-75 |
3.43e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 3.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPK---ILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTVRAADTIIGFEHGT 75
Cdd:PRK00635 1700 LSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLrTLVSLGHSVIYIDHDPALLKQADYLIEMGPGS 1778
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-162 |
3.71e-04 |
|
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: 44.23 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMV-QEVLSKIQHGHTIISVAHRLSTVRAADTIIGFE-HGTAVER 79
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMvKGAFQCL 2151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 80 GTHEELLERKGVYFtLVTLQsqgnqalneedIKdATEDDML-----ARTFSRGSYQDSLRasiRQRSKSQLSYLVHEPPL 154
Cdd:TIGR01257 2152 GTIQHLKSKFGDGY-IVTMK-----------IK-SPKDDLLpdlnpVEQFFQGNFPGSVQ---RERHYNMLQFQVSSSSL 2215
|
170
....*....|...
gi 767920345 155 A-----VVDHKST 162
Cdd:TIGR01257 2216 ArifqlLISHKDS 2228
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
626-734 |
3.73e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 626 PMERVIAAAKQAQLHDFVMSLPekyetnVGSQGSQLSRGEKQRIAIARAIVRDPK---ILLLDEATSALDTESEKTVQVA 702
Cdd:PRK00635 1671 PFLKKIQKPLQALIDNGLGYLP------LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQ 1744
|
90 100 110
....*....|....*....|....*....|...
gi 767920345 703 LDK-AREGRTCIVIAHRLSTIQNADIIAVMAQG 734
Cdd:PRK00635 1745 LRTlVSLGHSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-40 |
3.91e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.55 E-value: 3.91e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNE-SEAMVQ 40
Cdd:PRK10908 138 LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAlSEGILR 178
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
217-454 |
4.48e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. 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). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 42.88 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 217 LFSQILgTFSIP----------DKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDI 286
Cdd:cd18555 12 LLLQLL-TLLIPiltqyvidnvIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 287 AWFDdlRNSPGALTTRlATDASQVQGAAGSQ-IGMIVNSFTNVTVAmIIAFSFSWKLSLVILCFFPFLALsgatqTRMLT 365
Cdd:cd18555 91 SFFE--NRSSGDLLFR-ANSNVYIRQILSNQvISLIIDLLLLVIYL-IYMLYYSPLLTLIVLLLGLLIVL-----LLLLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 366 GFASRDKQALEMVGQ-----ITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSA 440
Cdd:cd18555 162 RKKIKKLNQEEIVAQtkvqsYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLL 241
|
250
....*....|....
gi 767920345 441 SYRYGGYLISNEGL 454
Cdd:cd18555 242 ILWIGAYLVINGEL 255
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1-57 |
4.86e-04 |
|
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: 42.09 E-value: 4.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAH 57
Cdd:cd03231 126 LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-86 |
4.99e-04 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 42.52 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIR-----NP--KILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLS-TVRAADTIIGFE 72
Cdd:COG4138 128 SGGEWQRVRLAAVLLQvwptiNPegQLLLLDEPMNSLDVAQQAALDRLLRELcQQGITVVMSSHDLNhTLRHADRVWLLK 207
|
90
....*....|....
gi 767920345 73 HGTAVERGTHEELL 86
Cdd:COG4138 208 QGKLVASGETAEVM 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-25 |
5.00e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.47 E-value: 5.00e-04
10 20
....*....|....*....|....
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLD 25
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILD 419
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-32 |
5.07e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 5.07e-04
10 20 30
....*....|....*....|....*....|..
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD 32
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
537-717 |
5.24e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 537 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSkkvnvqflrsnIGIVSQEPVLFACSIMDNI 616
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQ-----------LAWVNQETPALPQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 617 KYGDntKEI-PMERVIAAAKQAQLHDFVMSLPEKYET---------------NVGSQGSQLSR-------GEKQRIAIAR 673
Cdd:PRK10636 85 IDGD--REYrQLEAQLHDANERNDGHAIATIHGKLDAidawtirsraasllhGLGFSNEQLERpvsdfsgGWRMRLNLAQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767920345 674 AIVRDPKILLLDEATSALDTESEKTVQVALdKAREGrTCIVIAH 717
Cdd:PRK10636 163 ALICRSDLLLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISH 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
660-743 |
5.30e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 660 QLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKARegRTCIVIAHR---LSTIQnADIIAVMAQGVV 736
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSHArefLNTVV-TDILHLHGQKLV 420
|
....*..
gi 767920345 737 IEKGTHE 743
Cdd:PLN03073 421 TYKGDYD 427
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1-57 |
6.45e-04 |
|
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: 42.01 E-value: 6.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 57
Cdd:cd03237 116 LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaeNNEKTAFVVEH 174
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1-60 |
7.33e-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: 41.97 E-value: 7.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD-NESEAMVQEVLSKIQHGHTIISVAHRLS 60
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLDiKQRLNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
290-492 |
8.81e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 42.10 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 290 DDLRNSPGALTTRLATDASQVQGAAgSQIGMIVNSFTNVTVAMIIAFSFSWKLSLV----ILCFFP---FLA-LSGATQT 361
Cdd:cd18596 108 EKSSASVGKINNLMSVDANRISEFA-AFLHLLVSAPLQIVIAIVFLYRLLGWSALVglavMVLLLPlngYLAkRYSRAQK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 362 RMLtgfASRDKQAlemvgQITNEALSNIRTVagigK----ERRFIEAL----ETELekpfkTAIQKANIYGFCFAFAQ-- 431
Cdd:cd18596 187 ELM---KARDARV-----QLVTEVLQGIRMI----KffawERKWEERIlearEEEL-----KWLRKRFLLDLLLSLLWfl 249
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 432 ---CIMFIAnsasyrYGGY-LISNEGLHFSYVFrviSAVVLSAT---ALGRAFSYTPSYAKAKISAAR 492
Cdd:cd18596 250 ipiLVTVVT------FATYtLVMGQELTASVAF---TSLALFNMlrgPLNVLPELITQLLQAKVSLDR 308
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-76 |
8.99e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVR-AADTIIGFE-----H 73
Cdd:PRK13409 455 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIaeEREATALVVDHDIYMIDyISDRLMVFEgepgkH 534
|
...
gi 767920345 74 GTA 76
Cdd:PRK13409 535 GHA 537
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
315-454 |
9.44e-04 |
|
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: 41.78 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 315 GSQIGMIVNSFTnVTVAMIIAFSFSWKLSLVILCFFP-FLALSGATQTRMLTG----FASRDKQALEMVgqitnEALSNI 389
Cdd:cd18568 117 RSALTTILDLLM-VFIYLGLMFYYNLQLTLIVLAFIPlYVLLTLLSSPKLKRNsreiFQANAEQQSFLV-----EALTGI 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 390 RTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGL 454
Cdd:cd18568 191 ATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQL 255
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-48 |
9.94e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 41.42 E-value: 9.94e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESeamVQEVLSKIQH 48
Cdd:PRK10895 138 LSGGERRRVEIARALAANPKFILLDEPFAGVDPIS---VIDIKRIIEH 182
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
534-727 |
1.30e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERfyDPDQG---KVMIDGH---------DSKKvnvqflrsNIGIV 601
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysnDLTLFGRrrgsgetiwDIKK--------HIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 602 SQEPVL---FACSIMDNIKYG--DNtkeIPMERVIAAAKQaQLHDFVMSLPEKYETNVGSQGSQLSRGEkQRIA-IARAI 675
Cdd:PRK10938 342 SSSLHLdyrVSTSVRNVILSGffDS---IGIYQAVSDRQQ-KLAQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRAL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920345 676 VRDPKILLLDEATSALDTESEKTVQVALDK-AREGRT--------------CivIAHRLSTIQNADI 727
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHRLEFVPDGDI 481
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-86 |
1.35e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 41.22 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALD-NESEAMVQeVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTA 76
Cdd:COG4604 136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMMK-LLRRLadELGKTVVIVLHDINFASCyADHIVAMKDGRV 214
|
90
....*....|
gi 767920345 77 VERGTHEELL 86
Cdd:COG4604 215 VAQGTPEEII 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-78 |
1.44e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 40.71 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA--ADTIIGFEHGTA 76
Cdd:COG2401 137 LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarRAGITLVVATHHYDVIDDlqPDLLIFVGYGGV 216
|
..
gi 767920345 77 VE 78
Cdd:COG2401 217 PE 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-57 |
1.68e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 1.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNES-EAMVQEvLSKIQHGhtIISVAH 57
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQG-LVLFQGG--VLMVSH 682
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
534-563 |
2.15e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 2.15e-03
10 20 30
....*....|....*....|....*....|
gi 767920345 534 DSQVLNGLSVSISPGQTLAFVGSSGCGKST 563
Cdd:PRK01889 181 DGEGLDVLAAWLSGGKTVALLGSSGVGKST 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-80 |
2.39e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.29 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVE 232
|
..
gi 767920345 79 RG 80
Cdd:PRK11701 233 SG 234
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
332-464 |
2.54e-03 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 40.69 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 332 MIIAFSFSW-KLSLVILCFFPFLALSGATQTRMLTGFAS-RDKQAL---EMVGqITNEALSNIRTVAGIGKERRF---IE 403
Cdd:cd18594 126 VIVLTGLLWrEIGPSSLAGLGVLLLLLPLQAYLGKLFAKyRRKTAGltdERVK-IMNEIISGMRVIKMYTWEESFaklIE 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920345 404 AL-ETELEKPFKTA-IQKAN--IYGFCFAFAQCIMFIansasyrygGYLISNEGLHFSYVFRVIS 464
Cdd:cd18594 205 NIrKKELKLIRKAAyIRAFNmaFFFFSPTLVSFATFV---------PYVLTGNTLTARKVFTVIS 260
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1-81 |
3.30e-03 |
|
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: 39.91 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIR---NPKILLLDMATSALDNESEAMVQEVLSK-IQHGHTIISVAHRLSTVRAADTII------G 70
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCADWIIdlgpegG 249
|
90
....*....|.
gi 767920345 71 FEHGTAVERGT 81
Cdd:cd03271 250 DGGGQVVASGT 260
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-80 |
3.49e-03 |
|
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: 39.82 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVER 79
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFD 223
|
.
gi 767920345 80 G 80
Cdd:cd03220 224 G 224
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
660-742 |
3.91e-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: 38.88 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 660 QLSRGEKQRIAIA-----RAIVRDPkILLLDEATSALDTES-EKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMaq 733
Cdd:cd03227 77 QLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI-- 153
|
....*....
gi 767920345 734 GVVIEKGTH 742
Cdd:cd03227 154 KKVITGVYK 162
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
659-728 |
3.94e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 3.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920345 659 SQLSRGEKQRIAIAR---AIVRDPKILLLDEATSALDTESEKT-VQVALDKAREGRTCIVIAHRLSTIQNADII 728
Cdd:PRK00635 808 SSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKAlIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1-86 |
4.05e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 39.53 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIR-----NP--KILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLS-TVRAADTIIGF 71
Cdd:PRK03695 127 LSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNhTLRHADRVWLL 206
|
90
....*....|....*
gi 767920345 72 EHGTAVERGTHEELL 86
Cdd:PRK03695 207 KQGKLLASGRRDEVL 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-62 |
4.11e-03 |
|
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: 40.58 E-value: 4.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV 62
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEV 466
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1-57 |
5.48e-03 |
|
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: 38.88 E-value: 5.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAH 57
Cdd:TIGR01189 128 LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLrAHLARGGIVLLTTH 185
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
198-400 |
5.65e-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: 39.44 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 198 LVGSVGAAVNGTVTPLYAFLFSQILgTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFG 277
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIREL-VDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 278 FRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQI-GMIVNSFTNVTVAmIIAFSFSWKLSLVILCFFPFLALS 356
Cdd:cd18778 80 YDKLQRLSLRYFDD--RQTGDLMSRVINDVANVERLIADGIpQGITNVLTLVGVA-IILFSINPKLALLTLIPIPFLALG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767920345 357 GATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERR 400
Cdd:cd18778 157 AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEE 200
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-80 |
5.71e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.15 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 78
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVC 225
|
..
gi 767920345 79 RG 80
Cdd:PRK09700 226 SG 227
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
654-752 |
7.50e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 654 VGSQGSQLSRGEKQRIAIARAIVRDP--KIL-LLDEATSALDTES-EKTVQVaLDKARE-GRTCIVIAHRLSTIQNADII 728
Cdd:PRK00349 824 LGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDiRKLLEV-LHRLVDkGNTVVVIEHNLDVIKTADWI 902
|
90 100 110
....*....|....*....|....*....|
gi 767920345 729 AVM------AQGVVIEKGTHEELMAQKGAY 752
Cdd:PRK00349 903 IDLgpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-92 |
7.74e-03 |
|
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: 39.07 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 1 MSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 80
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYD 218
|
90
....*....|..
gi 767920345 81 THEELLERKGVY 92
Cdd:cd03289 219 SIQKLLNEKSHF 230
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
220-417 |
8.24e-03 |
|
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: 39.11 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 220 QILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQF---LQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSP 296
Cdd:cd18782 21 NPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVltaLRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFD--KRPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 297 GALTTRLAtDASQVQG-AAGSQIGMIVNS-FtnVTVAMIIAFSFSWKLSLVILCFFPFLAL-----SGATQTRMLTGFAS 369
Cdd:cd18782 99 GELSTRIS-ELDTIRGfLTGTALTTLLDVlF--SVIYIAVLFSYSPLLTLVVLATVPLQLLltflfGPILRRQIRRRAEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767920345 370 RDKQALEMVgqitnEALSNIRTVAGIGKERRFIEALETE----LEKPFKTAI 417
Cdd:cd18782 176 SAKTQSYLV-----ESLTGIQTVKAQNAELKARWRWQNRyarsLGEGFKLTV 222
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
641-718 |
9.54e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920345 641 DFVMSLPEKYETNVGSQG------SQLSRGEKQRIAIA-----RAIVR-----DPKILLLDEA-TSALDTESEKTVQVAL 703
Cdd:PHA02562 443 DYNFTLDEEFNETIKSRGredfsyASFSQGEKARIDLAllftwRDVASkvsgvDTNLLILDEVfDGALDAEGTKALLSIL 522
|
90
....*....|....*
gi 767920345 704 DKArEGRTCIVIAHR 718
Cdd:PHA02562 523 DSL-KDTNVFVISHK 536
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-57 |
9.59e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 9.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767920345 2 SGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQhgHTIISVAH 57
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| |
