|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
273-1469 |
0e+00 |
|
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: 770.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 273 LWRALYGAFGRCYLALGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVT 352
Cdd:TIGR00957 307 LFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSG 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 353 LQARGAVLNILYCKALQLGPS--RPPT-GEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLIL 429
Cdd:TIGR00957 387 MRIKTAVMGAVYRKALVITNSarKSSTvGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAV 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 430 ALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYL 509
Cdd:TIGR00957 467 MVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFT 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 510 WAALPVVISIVIFITYVLMGHQ--LTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLFLDLPNHNPQAYYS 587
Cdd:TIGR00957 547 WVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIER 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 588 PDPPAEPSTVLELHGALFSW---DPVGTSLETFishlEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlsk 664
Cdd:TIGR00957 627 RTIKPGEGNSITVHNATFTWardLPPTLNGITF----SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--- 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 665 GFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEK 744
Cdd:TIGR00957 700 SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 745 ELYLLDDPLAAVDADVANHLLHRCI--LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPK-- 820
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEfl 859
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 821 ---AWAENGQESDSATAQSVQNPEKTKEGLE----------------------------------------EEQSTSGRL 857
Cdd:TIGR00957 860 rtyAPDEQQGHLEDSWTALVSGEGKEAKLIEngmlvtdvvgkqlqrqlsasssdsgdqsrhhgssaelqkaEAKEETWKL 939
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 858 LQEESKKEGAVALHVYQAYWKAVGQGLALAILFSLLLMQATRNAADWWLSHWISQLKAeNSSQEaqpstspasmglfspq 937
Cdd:TIGR00957 940 MEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMV-NGTQN---------------- 1002
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 938 lllfspgnlyipvfplpkaapngssDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFN 1017
Cdd:TIGR00957 1003 -------------------------NTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE 1057
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1018 ATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGS 1097
Cdd:TIGR00957 1058 RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLES 1137
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1098 LTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQg 1177
Cdd:TIGR00957 1138 VSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHS- 1216
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1178 lANPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTCDLPQEP-QGQPLQLGTGWLTQGGVEFQDVVLAYR 1256
Cdd:TIGR00957 1217 -LSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQETAPPSGWPPRGRVEFRNYCLRYR 1295
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1257 PGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGT 1336
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGS 1375
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1337 VRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGEL-GEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQK 1415
Cdd:TIGR00957 1376 LRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEcAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1416 TDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:TIGR00957 1456 TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
215-1466 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 714.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 215 EDGESWLSRFSYAWLAPLLARGacgeLRQP---QDICRLPHRLQPTYLARVFQAHWQEGAR-----LWRALYGAFGRCYL 286
Cdd:PLN03232 229 ERYASIFSRIYFSWMTPLMQLG----YRKPiteKDVWQLDQWDQTETLIKRFQRCWTEESRrpkpwLLRALNNSLGGRFW 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 287 ALGLLKLVGTMLGFSGPLLLSLLVGFLEEGqEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCK 366
Cdd:PLN03232 305 LGGIFKIGHDLSQFVGPVILSHLLQSMQEG-DPAWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 367 ALQL---GPSRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATR 443
Cdd:PLN03232 384 SLRLtheARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRK 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 444 IMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFI 523
Cdd:PLN03232 464 MRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 524 TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQ-LFLdlpnhNPQAYYSPDPPAEPST-VLELH 601
Cdd:PLN03232 544 VFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEeLLL-----SEERILAQNPPLQPGApAISIK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 602 GALFSWDPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGEL-HRLRGHVAVRGlskGFGLATQEPWIQFATI 680
Cdd:PLN03232 619 NGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELsHAETSSVVIRG---SVAYVPQVSWIFNATV 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 681 RDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADV 760
Cdd:PLN03232 696 RENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 761 ANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEiLPLVQAVPKAWAENGQESDSATAQSVQNP 840
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAGKMDATQEVNTNDE 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 841 EKTKEGLEEEQSTSGR--------------LLQEESKKEGAVALHVYQAYWKAVGQGLALAILFS-LLLMQATRNAADWW 905
Cdd:PLN03232 855 NILKLGPTVTIDVSERnlgstkqgkrgrsvLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVcYLTTEVLRVSSSTW 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 906 LSHWISQLKAENssqeaqpstspasmglfspqlllFSPGnlyipvfplpkaapngssdirFYLTVYATIAGVNSLCTLLR 985
Cdd:PLN03232 935 LSIWTDQSTPKS-----------------------YSPG---------------------FYIVVYALLGFGQVAVTFTN 970
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 986 AVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLP 1065
Cdd:PLN03232 971 SFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVST 1050
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1066 WLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATS 1145
Cdd:PLN03232 1051 ISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANT 1130
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1146 ATMQWLDIRLQLMGAAVVSAIAGIALVQH-----QQGLANpgLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEE 1220
Cdd:PLN03232 1131 SSNRWLTIRLETLGGVMIWLTATFAVLRNgnaenQAGFAS--TMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGN 1208
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1221 YTcDLPQEP-----QGQPLqlgTGWLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFR 1295
Cdd:PLN03232 1209 YI-DLPSEAtaiieNNRPV---SGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFR 1284
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1296 LLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVIT-SMGGLDGE 1374
Cdd:PLN03232 1285 IVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDrNPFGLDAE 1364
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1375 LGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQA 1454
Cdd:PLN03232 1365 VSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSS 1444
|
1290
....*....|..
gi 312176403 1455 GRVVELDSPATL 1466
Cdd:PLN03232 1445 GQVLEYDSPQEL 1456
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
203-1466 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 714.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 203 PLLPEDQEPEVAED---GE--------SWLSRFSYAWLAPLLARGACGELRQPqDICRLPHRLQPTYLARVFQAHWQEGA 271
Cdd:PLN03130 206 PIGSESVDDYEYEElpgGEqicperhaNIFSRIFFGWMTPLMQLGYKRPLTEK-DVWKLDTWDQTETLYRSFQKCWDEEL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 272 R-----LWRALYGAFGRCYLALGLLKLVGTMLGFSGPLLLSLLVGFLEEGqEPLSHGLLYALGLAGGAVLGAVLQNQYGY 346
Cdd:PLN03130 285 KkpkpwLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNG-EPAWIGYIYAFSIFVGVVLGVLCEAQYFQ 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 347 EVYKVTLQARGAVLNILYCKALQL---GPSRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAF 423
Cdd:PLN03130 364 NVMRVGFRLRSTLVAAVFRKSLRLtheGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVAS 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 424 VGGLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLD 503
Cdd:PLN03130 444 LIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLS 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 504 AACVYLWAALPVVISIVIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQ-LFLdlpnhNP 582
Cdd:PLN03130 524 AFNSFILNSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEeLLL-----AE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 583 QAYYSPDPPAEPST-VLELHGALFSWDPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGEL-HRLRGHVAVR 660
Cdd:PLN03130 599 ERVLLPNPPLEPGLpAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 661 GlskGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAV 740
Cdd:PLN03130 679 G---TVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAV 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 741 YQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL---PLVQ- 816
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSnngPLFQk 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 817 ----------AVPKAWAENGQESDSATAQSVQNPEKTKEGLEEEQSTSGR--LLQEESKKEGAVALHVYQAYWKAVGQGL 884
Cdd:PLN03130 836 lmenagkmeeYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKsvLIKQEERETGVVSWKVLERYKNALGGAW 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 885 ALAILF-SLLLMQATRNAADWWLSHWISQlkaenssqeaqpsTSPASMGlfspqlllfsPGnlyipvfplpkaapngssd 963
Cdd:PLN03130 916 VVMILFlCYVLTEVFRVSSSTWLSEWTDQ-------------GTPKTHG----------PL------------------- 953
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 964 irFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFIL 1043
Cdd:PLN03130 954 --FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFV 1031
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1044 NILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGAT 1123
Cdd:PLN03130 1032 NMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAY 1111
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1124 YRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQH-----QQGLANpgLVGLSLSYALSLTGLL 1198
Cdd:PLN03130 1112 DRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNgraenQAAFAS--TMGLLLSYALNITSLL 1189
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1199 SGLVSSFTQTEAMLVSVERLEEYTcDLPQEPqgqPLQLGT-----GWLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPG 1273
Cdd:PLN03130 1190 TAVLRLASLAENSLNAVERVGTYI-DLPSEA---PLVIENnrpppGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPS 1265
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1274 EKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALW 1353
Cdd:PLN03130 1266 EKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLW 1345
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1354 QALKQCHLSEVI-TSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKT 1432
Cdd:PLN03130 1346 ESLERAHLKDVIrRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCT 1425
|
1290 1300 1310
....*....|....*....|....*....|....
gi 312176403 1433 VLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 1466
Cdd:PLN03130 1426 MLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
273-1466 |
5.26e-169 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 549.38 E-value: 5.26e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 273 LWRALYGAFGRCYLALGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVT 352
Cdd:PTZ00243 234 LLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 353 LQARGAVLNILYCKALQLGP---SRPP--TGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGL 427
Cdd:PTZ00243 314 LQYRSALNALIFEKCFTISSkslAQPDmnTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 428 ILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACV 507
Cdd:PTZ00243 394 AVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 508 YLWAALPVVISIVIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLFLDLPN-------- 579
Cdd:PTZ00243 474 FVNNATPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNatcstvqd 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 580 ----------HNP-------------QAYYSPDPPAEPSTVLELHGALFSW----------------------------- 607
Cdd:PTZ00243 554 meeywreqreHSTacqlaavlenvdvTAFVPVKLPRAPKVKTSLLSRALRMlcceqcrptkrhpspsvvvedtdygspss 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 608 -----DPVGTS-------------------LETFIS----------HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRL 653
Cdd:PTZ00243 634 asrhiVEGGTGggheatptsersaktpkmkTDDFFElepkvllrdvSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 654 RGHVAVrglSKGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRAR 733
Cdd:PTZ00243 714 EGRVWA---ERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKAR 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 734 IALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL- 812
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMr 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 813 -PLVQAVPKAWAEN--GQESDS-----------ATAQSVQNPEKTKEGLEEEQ------STSGRLLQEESKKEGAVALHV 872
Cdd:PTZ00243 871 tSLYATLAAELKENkdSKEGDAdaevaevdaapGGAVDHEPPVAKQEGNAEGGdgaaldAAAGRLMTREEKASGSVPWST 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 873 YQAYWKAVGQGL-ALAILFSLLLMQATRNAADWWLSHWisqlkaenssqeaqpstSPASMGLfspqlllfspgnlyipvf 951
Cdd:PTZ00243 951 YVAYLRFCGGLHaAGFVLATFAVTELVTVSSGVWLSMW-----------------STRSFKL------------------ 995
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 952 plpkaapngSSDIrfYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSD 1031
Cdd:PTZ00243 996 ---------SAAT--YLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRD 1064
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1032 VACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTL 1111
Cdd:PTZ00243 1065 IDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEAL 1144
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1112 AGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLA--NPGLVGLSLS 1189
Cdd:PTZ00243 1145 QGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATsqEIGLVSLSLT 1224
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1190 YALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTCDLPQE--PQ--------------------------GQPLQLGTGWL 1241
Cdd:PTZ00243 1225 MAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEdmPEldeevdalerrtgmaadvtgtvviepASPTSAAPHPV 1304
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1242 TQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRS 1321
Cdd:PTZ00243 1305 QAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1322 QLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLT-D 1399
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSnYSVGQRQLMCMARALLKkG 1464
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 1400 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 1466
Cdd:PTZ00243 1465 SGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
288-571 |
1.49e-133 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 413.87 E-value: 1.49e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 288 LGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKA 367
Cdd:cd18598 2 LGLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 368 LQLGPSR---PPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRI 444
Cdd:cd18598 82 LRVRSSSlskFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 445 MASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFIT 524
Cdd:cd18598 162 GALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 312176403 525 YVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18598 242 YVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
287-571 |
2.98e-126 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 394.27 E-value: 2.98e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 287 ALGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCK 366
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 367 ALQLGPS---RPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATR 443
Cdd:cd18559 81 ALRSPISffeRTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 444 IMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFI 523
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 312176403 524 TYVLMGH--QLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18559 241 AYVSRHSlaGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
219-1469 |
2.91e-117 |
|
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: 403.91 E-value: 2.91e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 219 SWLSRFSYAWLAPLLARGACGELrQPQDICRLPHRLQPTYLARVFQAHW-------QEGARLWRALYGAFGRCYLALGLL 291
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKL-ELSDIYQIPSFDSADNLSERLEREWdrelasaKKNPKLLNALRRCFFWRFVFYGIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 292 KLVGTMLGFSGPLLLSLLVG-FLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKALQL 370
Cdd:TIGR01271 89 LYFGEATKAVQPLLLGRIIAsYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 371 GP---SRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRIMAS 447
Cdd:TIGR01271 169 SSrvlDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 448 NQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVI---KYLDAACVYLWAALPVVISIVifiT 524
Cdd:TIGR01271 249 RDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIaylRYFYSSAFFFSGFFVVFLSVV---P 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 525 YVLMgHQLTATKVFTALALVRMLILPLN-NFPWVINGLLEAKVSLDRIQLFLDLPNHNPQAYyspdppAEPSTVLELHGA 603
Cdd:TIGR01271 326 YALI-KGIILRRIFTTISYCIVLRMTVTrQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEY------NLTTTEVEMVNV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 604 LFSWDP-VGTSLET-----------------FISHLE-------------VKKGMLVGIVGKVGCGKSSLLAAIAGELHR 652
Cdd:TIGR01271 399 TASWDEgIGELFEKikqnnkarkqpngddglFFSNFSlyvtpvlknisfkLEKGQLLAVAGSTGSGKSSLLMMIMGELEP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 653 LRGHVAVRGLskgFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRA 732
Cdd:TIGR01271 479 SEGKIKHSGR---ISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 733 RIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI- 811
Cdd:TIGR01271 556 RISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELq 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 812 ---------LPLVQAVPKAWAENGQ------------ESDSATA-------QSVQNP-----EKTK-------------- 844
Cdd:TIGR01271 636 akrpdfsslLLGLEAFDNFSAERRNsiltetlrrvsiDGDSTVFsgpetikQSFKQPppefaEKRKqsiilnpiasarkf 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 845 ----------EGLEEEQSTSGRL-----------LQEESKKEGAVALH--VYQAYWK----------AVGQGL--ALAIL 889
Cdd:TIGR01271 716 sfvqmgpqkaQATTIEDAVREPSerkfslvpedeQGEESLPRGNQYHHglQHQAQRRqsvlqlmthsNRGENRreQLQTS 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 890 FSLLLMQATRNAADWWLSHWISQLKAENS------------------SQEAQPSTSPASMGL---FSPQLLLF------- 941
Cdd:TIGR01271 796 FRKKSSITQQNELASELDIYSRRLSKDSVyeiseeineedlkecfadERENVFETTTWNTYLryiTTNRNLVFvlifclv 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 942 --------SPGNLYI----PVFPL----------------PKAAPNGSSdirfYLTVYATIAGVNSLCTL--LRAVLFAA 991
Cdd:TIGR01271 876 iflaevaaSLLGLWLitdnPSAPNyvdqqhanasspdvqkPVIITPTSA----YYIFYIYVGTADSVLALgfFRGLPLVH 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 992 GTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLL 1071
Cdd:TIGR01271 952 TLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAA 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1072 PPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWL 1151
Cdd:TIGR01271 1032 IPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWF 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1152 DIRLQLMGAAVVSAIAGIALVQHQQGlanPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTcDLPQEP-- 1229
Cdd:TIGR01271 1112 QMRIDIIFVFFFIAVTFIAIGTNQDG---EGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFI-DLPQEEpr 1187
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1230 ---QGQPLQLGTG-----------WLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFR 1295
Cdd:TIGR01271 1188 psgGGGKYQLSTVlvienphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR 1267
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1296 LLEpSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGEL 1375
Cdd:TIGR01271 1268 LLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFV 1346
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1376 GEGGRS-LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQA 1454
Cdd:TIGR01271 1347 LVDGGYvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEG 1426
|
1450
....*....|....*
gi 312176403 1455 GRVVELDSPATLRNQ 1469
Cdd:TIGR01271 1427 SSVKQYDSIQKLLNE 1441
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
885-1222 |
3.82e-103 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 331.03 E-value: 3.82e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 885 ALAILFSLLLMQATRNAADWWLSHWISQLKAENSSQeaqpstspasmglfspqlllfspgnlyipvfplpkaapnGSSDI 964
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNF---------------------------------------INDSF 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 965 RFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILN 1044
Cdd:cd18605 42 NFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1045 ILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATY 1124
Cdd:cd18605 122 ILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1125 RFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGL-ANPGLVGLSLSYALSLTGLLSGLVS 1203
Cdd:cd18605 202 RFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAVVQHFFGLsIDAGLIGLALSYALPITGLLSGLLN 281
|
330
....*....|....*....
gi 312176403 1204 SFTQTEAMLVSVERLEEYT 1222
Cdd:cd18605 282 SFTETEKEMVSVERVRQYF 300
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1244-1463 |
1.97e-102 |
|
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: 325.99 E-value: 1.97e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1244 GGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1323
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKI 1402
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGEnLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1403 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 1463
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
598-801 |
1.81e-100 |
|
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: 319.80 E-value: 1.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 598 LELHGALFSWDPVGTSLETFIS--HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlskGFGLATQEPWI 675
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKdiNLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG---SIAYVSQEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 676 QFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:cd03250 78 QNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 312176403 756 VDADVANHLLHRCILGMLSYT-TRLLCTHRTEYLERADAVLLMEAGR 801
Cdd:cd03250 158 VDAHVGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
288-571 |
3.93e-89 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 291.31 E-value: 3.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 288 LGLLKLVGTMLGFSGPLLLSLLVGFLEE-GQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCK 366
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 367 ALQLGPS---RPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATR 443
Cdd:cd18579 82 ALRLSSSarqETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 444 IMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFI 523
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 312176403 524 TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18579 242 TYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
962-1469 |
1.59e-78 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 271.65 E-value: 1.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 962 SDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVA----CADD 1037
Cdd:COG1132 58 SALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDaveqFLAH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1038 SLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRlgslTLSPLYSHLADTLAGLSVL 1117
Cdd:COG1132 138 GLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQE----ALAELNGRLQESLSGIRVV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1118 RATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYALSLTGL 1197
Cdd:COG1132 214 KAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1198 LSGLVSSFTQTEAMLVSVERLEEY---TCDLPQEPQGQPLQLgtgwlTQGGVEFQDVVLAYRPGLPnALDGVTFCVQPGE 1274
Cdd:COG1132 294 LRQLANVLNQLQRALASAERIFELldePPEIPDPPGAVPLPP-----VRGEIEFENVSFSYPGDRP-VLKDISLTIPPGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1275 KLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQglHKDRA 1351
Cdd:COG1132 368 TVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPD--ATDEE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1352 LWQALKQCHLSEVITSM------------GgldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 1419
Cdd:COG1132 446 VEEAAKAAQAHEFIEALpdgydtvvgergV-----------NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEAL 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 312176403 1420 LQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:COG1132 515 IQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
289-571 |
2.70e-78 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 260.48 E-value: 2.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 289 GLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKAL 368
Cdd:cd18595 3 ALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 369 QLGP-SRP--PTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRIM 445
Cdd:cd18595 83 RLSNsARKksTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 446 ASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITY 525
Cdd:cd18595 163 KLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 312176403 526 VLMG--HQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18595 243 VLSDpdNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1240-1463 |
4.76e-76 |
|
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: 250.79 E-value: 4.76e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1240 WLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL 1319
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1320 RSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKqchLSEvitsmggldgelgeGGRSLSLGQRQLLCLARALLTD 1399
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR---VSE--------------GGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1400 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 1463
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
287-571 |
1.50e-66 |
|
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: 227.76 E-value: 1.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 287 ALGLLKLVGTMLGFSGPLLLSLLVGFLEE-GQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYC 365
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLEDpGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 366 KALQL----GPSRPP------------------TGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGV-A 422
Cdd:cd18596 81 KALRRrdksGSSKSSeskkkdkeededekssasVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWsA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 423 FVGGLILALLLvPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYL 502
Cdd:cd18596 161 LVGLAVMVLLL-PLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 503 DAACVYLWAALPVVISIVIFITYVL-MGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18596 240 DLLLSLLWFLIPILVTVVTFATYTLvMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
955-1469 |
9.23e-66 |
|
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: 237.81 E-value: 9.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 955 KAAPNGSSDIRFYLTVYATIAGV-NSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVA 1033
Cdd:COG2274 185 RVLPNQDLSTLWVLAIGLLLALLfEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVES 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1034 CAD-----------DSLPFILNILLanaagllgllavlgsglpwlllllpplsIMYYH--------------------VQ 1082
Cdd:COG2274 265 IREfltgslltallDLLFVLIFLIV----------------------------LFFYSpplalvvllliplyvllgllFQ 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1083 RHYRASSRELRRLGSLtlspLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAV 1162
Cdd:COG2274 317 PRLRRLSREESEASAK----RQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLA 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1163 VSAI--AGIALVQHQQ-------------GLANPGLVGLslsyalsltgllsglVSSFTQTEAMLVSVERLEEYTcDLPQ 1227
Cdd:COG2274 393 TVALlwLGAYLVIDGQltlgqliafnilsGRFLAPVAQL---------------IGLLQRFQDAKIALERLDDIL-DLPP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1228 EPQGQPLQLGTGWLtQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLD 1307
Cdd:COG2274 457 EREEGRSKLSLPRL-KGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1308 GVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQglHKDRALWQALKQCHLSEVITSMGG-LDGELGEGGRSLS 1383
Cdd:COG2274 536 GIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDPD--ATDEEIIEAARLAGLHDFIEALPMgYDTVVGEGGSNLS 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1384 LGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 1463
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTH 693
|
....*.
gi 312176403 1464 ATLRNQ 1469
Cdd:COG2274 694 EELLAR 699
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
886-1222 |
5.87e-64 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 219.68 E-value: 5.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 886 LAILFSLLLMQATRNAADWWLSHWISQlkaenssqeaqpstspasmglfspqlllfspgnlyipvfplpkAAPNGSSDIR 965
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSD-------------------------------------------WSSSPNSSSG 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 966 FYLTVYATIAGVNS-LCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILN 1044
Cdd:cd18580 39 YYLGVYAALLVLASvLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1045 ILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATY 1124
Cdd:cd18580 119 DFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1125 RFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQglANPGLVGLSLSYALSLTGLLSGLVSS 1204
Cdd:cd18580 199 RFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALLAVLLRSS--ISAGLVGLALTYALSLTGSLQWLVRQ 276
|
330
....*....|....*...
gi 312176403 1205 FTQTEAMLVSVERLEEYT 1222
Cdd:cd18580 277 WTELETSMVSVERILEYT 294
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1244-1459 |
4.53e-62 |
|
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: 211.70 E-value: 4.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1244 GGVEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1323
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEPFLFSGTVRENLDPQGLHKDRALWQ-ALKQCHLSEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARALLTDAK 1401
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNgYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1402 ILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1459
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1246-1456 |
9.68e-61 |
|
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: 205.69 E-value: 9.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1325
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSGTVRENLdpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKILCI 1405
Cdd:cd03228 81 VPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1406 DEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGR 1456
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
289-571 |
1.63e-60 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p 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.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 209.62 E-value: 1.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 289 GLLKLVGTMLGFSGPLLLSLLVGFLEEGQE-----PLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNIL 363
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLINFVEDAYLggpppSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 364 YCKALQL-GPSR--PPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVI 440
Cdd:cd18597 83 YRKSLRLsGKSRheFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 441 ATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIV 520
Cdd:cd18597 163 MKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASML 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 312176403 521 IFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18597 243 SFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
954-1222 |
1.62e-58 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 204.25 E-value: 1.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 954 PKAAPNGSSDIR-FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDV 1032
Cdd:cd18603 29 PALNGTQDTEQRdYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1033 ACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLA 1112
Cdd:cd18603 109 DTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1113 GLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlaNPGLVGLSLSYAL 1192
Cdd:cd18603 189 GASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLFAALFAVLSRDSL--SPGLVGLSISYAL 266
|
250 260 270
....*....|....*....|....*....|
gi 312176403 1193 SLTGLLSGLVSSFTQTEAMLVSVERLEEYT 1222
Cdd:cd18603 267 QITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1244-1469 |
1.55e-56 |
|
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: 197.05 E-value: 1.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1244 GGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1323
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLD-GELGEGGRSLSLGQRQLLCLARALLTDAKI 1402
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 1403 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1246-1459 |
5.54e-55 |
|
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: 191.68 E-value: 5.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1325
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSGTVRENL---DPQGLHKDraLWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAK 1401
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGATREE--VEEAARAANAHEFIMELPEGYDTVIGERGVkLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1402 ILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1459
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
272-812 |
6.79e-55 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 202.32 E-value: 6.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 272 RLWRALYGAFGRCYLALgLLKLVGTMLGFSGPLLLSLLVGFLEEGQePLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKV 351
Cdd:COG1132 11 RLLRYLRPYRGLLILAL-LLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLLLLLLGLALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 352 TLQARGAVLNILYCKALQLGPS---RPPTGEALNLLGTDSERLLNFAG-SFHEAWGLPLQLAITL-YLLYQQVGVAFVGG 426
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSffdRRRTGDLLSRLTNDVDAVEQFLAhGLPQLVRSVVTLIGALvVLFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 427 LILALLLVPVnKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEAcRARELGR--LRVIKYLDA 504
Cdd:COG1132 169 LVLPLLLLVL-RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE-ANEELRRanLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 505 --ACVYLWAALPVVISIVIFITYVLMGhQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLFLDLPNHNP 582
Cdd:COG1132 247 ffPLMELLGNLGLALVLLVGGLLVLSG-SLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 583 QAYySPDPPAEPSTVLELHGALFSWDPVGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAG-------------- 648
Cdd:COG1132 326 DPP-GAVPLPPVRGEIEFENVSFSYPGDRPVLKDI--SLTIPPGETVALVGPSGSGKSTLVNLLLRfydptsgrilidgv 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 649 -----ELHRLRGHVAVrglskgfglATQEPWIQFATIRDNILFGK---TfDAQLyKEVLEACALNDDLSILPAGDQTEVG 720
Cdd:COG1132 403 dirdlTLESLRRQIGV---------VPQDTFLFSGTIRENIRYGRpdaT-DEEV-EEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 721 EKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAG 800
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETE-ALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
570
....*....|..
gi 312176403 801 RLIRAGPPSEIL 812
Cdd:COG1132 551 RIVEQGTHEELL 562
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
886-1222 |
9.10e-55 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) 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: 350048 [Multi-domain] Cd Length: 297 Bit Score: 193.45 E-value: 9.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 886 LAILFSLLLMQATRNAADWWLSHWisqlkaenSSQEAQPSTSPASmglfspqlllfspgnlyipvfplpkaapngSSDIR 965
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIW--------ASAYETSSALPPS------------------------------EVSVL 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 966 FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNI 1045
Cdd:cd18604 44 YYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1046 LLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYR 1125
Cdd:cd18604 124 LLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEER 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1126 FEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQqglANPGLVGLSLSYALSLTGLLSGLVSSF 1205
Cdd:cd18604 204 FIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSFATAALLVYGPG---IDAGLAGFSLSFALGFSSAILWLVRSY 280
|
330
....*....|....*..
gi 312176403 1206 TQTEAMLVSVERLEEYT 1222
Cdd:cd18604 281 NELELDMNSVERIQEYL 297
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1227-1469 |
3.32e-54 |
|
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: 199.98 E-value: 3.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1227 QEPQGQPLQLGTGWLTQGGVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL 1306
Cdd:COG4988 318 PEPAAPAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1307 DGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGG-LDGELGEGGRSL 1382
Cdd:COG4988 397 NGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRPDA--SDEELEAALEAAGLDEFVAALPDgLDTPLGEGGRGL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1383 SLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDS 1462
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGT 554
|
....*..
gi 312176403 1463 PATLRNQ 1469
Cdd:COG4988 555 HEELLAK 561
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
598-800 |
1.10e-52 |
|
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: 184.46 E-value: 1.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 598 LELHGALFSWDPVGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV-------------AVRGLSK 664
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNI--NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 665 G-FGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQE 743
Cdd:cd03290 79 YsVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 744 KELYLLDDPLAAVDADVANHLLHRCILGMLSYTTR--LLCTHRTEYLERADAVLLMEAG 800
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRtlVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
885-1222 |
2.24e-52 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 186.66 E-value: 2.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 885 ALAILFSLLLMQATRNAADWWLSHWisqlkaenssQEAQPSTSPASMGLFSPQLLlfspgnlyipvfplpkaapngSSDI 964
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADW----------TEANHDVASVVFNITSSSLE---------------------DDEV 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 965 RFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILN 1044
Cdd:cd18602 50 SYYISVYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1045 ILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATY 1124
Cdd:cd18602 130 RLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1125 RFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYALSLTGLLSGLVSS 1204
Cdd:cd18602 210 RFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRN 289
|
330
....*....|....*...
gi 312176403 1205 FTQTEAMLVSVERLEEYT 1222
Cdd:cd18602 290 LADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
886-1222 |
3.93e-52 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p 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.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 185.37 E-value: 3.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 886 LAILFSLLLMQATRNAADWWLSHWISQLkaenssqeaqpstspasmglfspqlllfspgnlyipvFPLPKAapngssdir 965
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTEDF-------------------------------------FGLSQG--------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 966 FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLP----- 1040
Cdd:cd18606 36 FYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPdslrm 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1041 -----------FILNIllanaagllgllavlgSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLAD 1109
Cdd:cd18606 116 flytlssiigtFILII----------------IYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1110 TLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVqhQQGLANPGLVGLSLS 1189
Cdd:cd18606 180 SLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVT--RRFSISPSSTGLVLS 257
|
330 340 350
....*....|....*....|....*....|...
gi 312176403 1190 YALSLTGLLSGLVSSFTQTEAMLVSVERLEEYT 1222
Cdd:cd18606 258 YVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1246-1466 |
1.32e-51 |
|
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: 181.97 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAY--RPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1323
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEPFLFSGTVRENL---DPQGLHKDRAlwQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTD 1399
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygKPDATDEEVE--EAAKKANIHDFIMSLPDGYDTLVGERGSqLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 1400 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 1466
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
974-1459 |
5.17e-51 |
|
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: 190.70 E-value: 5.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 974 IAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDV----ACADDSLPFILNILLAN 1049
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSeqvaSAATDAFIVLVRETLTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1050 AAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRL-GSLTLSplyshLADTLAGLSVLRATGA----TY 1124
Cdd:TIGR02203 143 IGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSmGQVTTV-----AEETLQGYRVVKLFGGqayeTR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1125 RFEEENLRLLELNQRCQFATSAtmqwLDIRLQLMGAAVVSAIAGIALVQHQQGLANPG-LVGLSLSYALSLTGLLSGL-V 1202
Cdd:TIGR02203 218 RFDAVSNRNRRLAMKMTSAGSI----SSPITQLIASLALAVVLFIALFQAQAGSLTAGdFTAFITAMIALIRPLKSLTnV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1203 SSFTQTeaMLVSVERLEEYTcDLPQEPQGQPLQLGTgwlTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRT 1282
Cdd:TIGR02203 294 NAPMQR--GLAAAESLFTLL-DSPPEKDTGTRAIER---ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1283 GSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQGLHKDRALwQALKQC 1359
Cdd:TIGR02203 368 GSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTEQADRAEIE-RALAAA 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1360 HLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAH 1438
Cdd:TIGR02203 447 YAQDFVDKLPLGLDTPIGENGVlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAH 526
|
490 500
....*....|....*....|.
gi 312176403 1439 RLNTILNSDRVLVLQAGRVVE 1459
Cdd:TIGR02203 527 RLSTIEKADRIVVMDDGRIVE 547
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1246-1466 |
4.95e-49 |
|
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: 174.73 E-value: 4.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1325
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGGLDGELGEGgRSLSL--GQRQLLCLARALLTDA 1400
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPDA--TDEEVIEAAKAAQIHDKIMRFPDGYDTIVGE-RGLKLsgGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1401 KILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 1466
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
881-1222 |
1.69e-48 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 175.83 E-value: 1.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 881 GQGLALAILFSLLLMQATRNAADWWLSHWISQLKAENSSQEAQPSTSPASMglfspqlllfspgnlyipvfplpkaapNG 960
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNI---------------------------SD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 961 SSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLP 1040
Cdd:cd18599 54 NPDLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1041 FILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRAT 1120
Cdd:cd18599 134 FTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1121 GATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHqqGLANPGLVGLSLSYALSLTGLLSG 1200
Cdd:cd18599 214 NKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITALLVVLLK--GSISPAFAGLALSYALQLSGLFQF 291
|
330 340
....*....|....*....|..
gi 312176403 1201 LVSSFTQTEAMLVSVERLEEYT 1222
Cdd:cd18599 292 TVRLASETEARFTSVERILEYI 313
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
316-812 |
1.05e-47 |
|
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: 180.72 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 316 GQEPLSHGLLYALGLAGGAVLGAVL---QNQYGYEV-YKVTLQARGAVLNilycKALQLGP---SRPPTGEALNLLGTDS 388
Cdd:COG4988 50 GGAPLSALLPLLGLLLAVLLLRALLawlRERAAFRAaARVKRRLRRRLLE----KLLALGPawlRGKSTGELATLLTEGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 389 ERLLNFAGSFheawgLP-------LQLAITLYLLYQQVGVAFVggLILALLLVPVNKVIATRIMASNQEmlQHKDARVKL 461
Cdd:COG4988 126 EALDGYFARY-----LPqlflaalVPLLILVAVFPLDWLSGLI--LLVTAPLIPLFMILVGKGAAKASR--RQWRALARL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 462 ---VTELLSGIRVIKFCGWEQALGARV----EACRARELGRLRV----IKYLDAAcVYLWAALpvvisIVIFITYVLMGH 530
Cdd:COG4988 197 sghFLDRLRGLTTLKLFGRAKAEAERIaeasEDFRKRTMKVLRVaflsSAVLEFF-ASLSIAL-----VAVYIGFRLLGG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 531 QLTATKVFTALALVRMLILPLNNFpwvinGL-----LEAKVSLDRIQLFLDLPNHNPQAYYSPDPPAEPSTvLELHGALF 605
Cdd:COG4988 271 SLTLFAALFVLLLAPEFFLPLRDL-----GSfyharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPS-IELEDVSF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 606 SWDPVGTSLEtFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWI 675
Cdd:COG4988 345 SYPGGRPALD-GLS-LTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpasWRRQIAWVPQNPYL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 676 QFATIRDNILFGKTF--DAQLyKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:COG4988 423 FAGTIRENLRLGRPDasDEEL-EAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 754 AAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG4988 502 AHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
426-812 |
1.46e-47 |
|
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: 183.11 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 426 GLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCG--------WEQALGARVEAcrarelgRLR 497
Cdd:COG2274 301 VLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGaesrfrrrWENLLAKYLNA-------RFK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 498 VIKYLDAAcvYLWA-ALPVVISIVIFI--TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLF 574
Cdd:COG2274 374 LRRLSNLL--STLSgLLQQLATVALLWlgAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDI 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 575 LDLPNHNPQAYYSPDPPAEPSTVlELHGALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLR 654
Cdd:COG2274 452 LDLPPEREEGRSKLSLPRLKGDI-ELENVSFRYPGDSPPVLDNIS-LTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 655 GHVAV----------RGLSKGFGLATQEPWIQFATIRDNILFGKTF--DAQLYkEVLEACALNDDLSILPAGDQTEVGEK 722
Cdd:COG2274 530 GRILIdgidlrqidpASLRRQIGVVLQDVFLFSGTIRENITLGDPDatDEEII-EAARLAGLHDFIEALPMGYDTVVGEG 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 723 GVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRL 802
Cdd:COG2274 609 GSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
410
....*....|
gi 312176403 803 IRAGPPSEIL 812
Cdd:COG2274 688 VEDGTHEELL 697
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
289-571 |
1.44e-46 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 170.11 E-value: 1.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 289 GLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALG--------------LAGGAVLGAVLQNQYGYEVYKVT-- 352
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVsyvtveeffsngyvLAVILFLALLLQATFSQASYHIVir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 353 --LQARGAVLNILYCKALQLGPSRPP-----TGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVG 425
Cdd:cd18591 83 egIRLKTALQAMIYEKALRLSSWNLSsgsmtIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 426 GLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAA 505
Cdd:cd18591 163 GAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 506 CVYLWAALPVVISIVIFITYVLMGHQ-LTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18591 243 MTFLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1246-1466 |
1.91e-46 |
|
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: 167.28 E-value: 1.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1325
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSGTVRENL---DPqGLHKDRALWQA-LKQCHlsEVITSMGGLDGELGEGG-RSLSLGQRQLLCLARALLTDA 1400
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP-GMSMERVIEAAkLAGAH--DFISELPEGYDTIVGEQgAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1401 KILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 1466
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
312-572 |
4.92e-46 |
|
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: 167.81 E-value: 4.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 312 FLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKALQLGP---SRPPTGEALNLLGTDS 388
Cdd:cd18594 27 FVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSsalSKITTGHIVNLLSNDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 389 ERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSG 468
Cdd:cd18594 107 QKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 469 IRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITYVLMGHQLTATKVFTALAL---VR 545
Cdd:cd18594 187 MRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTARKVFTVISLlnaLR 266
|
250 260
....*....|....*....|....*..
gi 312176403 546 MLIlpLNNFPWVINGLLEAKVSLDRIQ 572
Cdd:cd18594 267 MTI--TRFFPESIQTLSESRVSLKRIQ 291
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
377-812 |
7.71e-46 |
|
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: 175.34 E-value: 7.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 377 TGEALNLLGTDSERLLNF-------AGSfheAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVnkvIATRIM-ASN 448
Cdd:COG4987 111 SGDLLNRLVADVDALDNLylrvllpLLV---ALLVILAAVAFLAFFSPALALVLALGLLLAGLLLPL---LAARLGrRAG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 449 QEMLQHKDARVKLVTELLSGIRVIKFCG-WEQALGA--RVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITY 525
Cdd:COG4987 185 RRLAAARAALRARLTDLLQGAAELAAYGaLDRALARldAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 526 VLMGHQ---LTATKVFTALALVRMLiLPLnnfPWVINGLLEAKVSLDRIQlflDLPNHNPQAYYSPDPPAEPSTV-LELH 601
Cdd:COG4987 265 VAAGALsgpLLALLVLAALALFEAL-APL---PAAAQHLGRVRAAARRLN---ELLDAPPAVTEPAEPAPAPGGPsLELE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 602 GALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQ 671
Cdd:COG4987 338 DVSFRYPGAGRPVLDGLS-LTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddLRRRIAVVPQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 672 EPWIQFATIRDNILFGK---TfDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYL 748
Cdd:COG4987 417 RPHLFDTTLRENLRLARpdaT-DEELW-AALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILL 494
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176403 749 LDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG4987 495 LDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
621-811 |
4.79e-45 |
|
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: 164.64 E-value: 4.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLskgFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLE 700
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR---ISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 701 ACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLL 780
Cdd:cd03291 135 ACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRIL 214
|
170 180 190
....*....|....*....|....*....|.
gi 312176403 781 CTHRTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:cd03291 215 VTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1244-1458 |
6.02e-44 |
|
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: 159.29 E-value: 6.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1244 GGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1323
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEPFLFSGTVRENL---DPqgLHKDRALWQALKQCHLSEVI-TSMGGLDGELGEGGRSLSLGQRQLLCLARALLTD 1399
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAP--LADDERILRAAELAGVTDFVnKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 1400 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVV 1458
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
883-1222 |
1.63e-42 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 158.64 E-value: 1.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 883 GLALAILFSLLlMQATRNAADWWLSHWisqlkaeNSSQEAQPSTSPASMGLFSpqlllfspGNLYIPVfplpkaapngsS 962
Cdd:cd18601 4 VFILLVLLNIA-AQVLYVLSDWWLSYW-------ANLEEKLNDTTDRVQGENS--------TNVDIED-----------L 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 963 DIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFI 1042
Cdd:cd18601 57 DRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1043 LNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGA 1122
Cdd:cd18601 137 FLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1123 TYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVqhqqgLA---NPGLVGLSLSYALSLTGLLS 1199
Cdd:cd18601 217 QERFQEEFDAHQDLHSEAWFLFLATSRWLAVRLDALCALFVTVVAFGSLF-----LAeslDAGLVGLSLSYALTLMGTFQ 291
|
330 340
....*....|....*....|...
gi 312176403 1200 GLVSSFTQTEAMLVSVERLEEYT 1222
Cdd:cd18601 292 WCVRQSAEVENLMTSVERVLEYS 314
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1216-1470 |
3.23e-42 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 166.82 E-value: 3.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1216 ERLEEYTCDLPQEPQgqPLQLGTGWLtQGGVEFQDVVLAY--RPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVL 1293
Cdd:TIGR00958 452 EKVFEYLDRKPNIPL--TGTLAPLNL-EGLIEFQDVSFSYpnRPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1294 FRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLdPQGLHK--DRALWQALKQCHLSEVITSMGGL 1371
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENI-AYGLTDtpDEEIMAAAKAANAHDFIMEFPNG 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1372 DGELGEGGRS-LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTicKRFANKTVLTIAHRLNTILNSDRVL 1450
Cdd:TIGR00958 607 YDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQIL 684
|
250 260
....*....|....*....|
gi 312176403 1451 VLQAGRVVELDSPATLRNQP 1470
Cdd:TIGR00958 685 VLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
319-571 |
5.75e-41 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 153.15 E-value: 5.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 319 PLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKALQLGPS---RPPTGEALNLLGTDSERLLNFA 395
Cdd:cd18593 35 SLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAalgKTTVGQIVNLLSNDVNRFDQAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 396 GSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIAtRIMASN-QEMLQHKDARVKLVTELLSGIRVIKF 474
Cdd:cd18593 115 LFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG-KLFSKLrRKTAARTDKRIRIMNEIINGIRVIKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 475 CGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITYVLMGHQLTATKVFTALALVRMLILPLNN- 553
Cdd:cd18593 194 YAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILTAERVFVTMALYNAVRLTMTLf 273
|
250
....*....|....*...
gi 312176403 554 FPWVINGLLEAKVSLDRI 571
Cdd:cd18593 274 FPFAIQFGSELSVSIRRI 291
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1224-1459 |
8.91e-41 |
|
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: 160.76 E-value: 8.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1224 DLPQE----PQGQPLQLgtgwlTQGGVEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP 1299
Cdd:COG5265 337 DQPPEvadaPDAPPLVV-----GGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1300 SSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQGLHKDraLWQALKQCHLSEVItsmggldgelg 1376
Cdd:COG5265 411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPDASEEE--VEAAARAAQIHDFI----------- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1377 eggRS---------------LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLN 1441
Cdd:COG5265 478 ---ESlpdgydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLS 554
|
250
....*....|....*...
gi 312176403 1442 TILNSDRVLVLQAGRVVE 1459
Cdd:COG5265 555 TIVDADEILVLEAGRIVE 572
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1243-1459 |
4.22e-39 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 155.12 E-value: 4.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1243 QGGVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ 1322
Cdd:PRK13657 332 KGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1323 LAIIPQEPFLFSGTVRENL---DPQGLHKDraLWQALKQCHLSEVI-TSMGGLDGELGEGGRSLSLGQRQLLCLARALLT 1398
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIrvgRPDATDEE--MRAAAERAQAHDFIeRKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1399 DAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1459
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1244-1469 |
8.29e-39 |
|
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: 146.54 E-value: 8.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1244 GGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEpSSGRVLLDGVDTSQLELAQLRSQL 1323
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKI 1402
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCvLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 1403 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1243-1457 |
1.70e-38 |
|
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: 143.77 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1243 QGGVEFQDVVLAY--RPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLR 1320
Cdd:cd03248 9 KGIVKFQNVTFAYptRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1321 SQLAIIPQEPFLFSGTVRENLdPQGLHK--DRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALL 1397
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNI-AYGLQScsFECVKEAAQKAHAHSFISELASGYDTEVGEKGSqLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1398 TDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRV 1457
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1246-1459 |
1.23e-37 |
|
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: 139.76 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLAI 1325
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSGTVRENLDpqglhkdralwqalkqchlsevitsmggldgelgeggRSLSLGQRQLLCLARALLTDAKILCI 1405
Cdd:cd03247 80 LNQRPYLFDTTLRNNLG-------------------------------------RRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1406 DEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1459
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1247-1457 |
1.32e-37 |
|
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: 139.27 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1247 EFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAII 1326
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1327 PQEPFLFSGTVRENLdpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKILCID 1406
Cdd:cd03246 82 PQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 312176403 1407 EATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILNSDRVLVLQAGRV 1457
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1243-1469 |
7.35e-36 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 145.16 E-value: 7.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1243 QGGVEFQDVVLAYrPGLPN-ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRS 1321
Cdd:PRK11176 339 KGDIEFRNVTFTY-PGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1322 QLAIIPQEPFLFSGTVRENLD--PQGLHKDRALWQALKQCHLSEVITSMGGLD-GELGEGGRSLSLGQRQLLCLARALLT 1398
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLdTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1399 DAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1241-1469 |
9.25e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 144.97 E-value: 9.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1241 LTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLR 1320
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1321 SQLAIIPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALL 1397
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 1398 TDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
290-571 |
2.77e-35 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 136.54 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 290 LLKLVGTMLGFSGPLLL-SLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKAL 368
Cdd:cd18592 4 LLLLISLIFGFIGPTILiRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 369 QL-GPSRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQL----AITLYLLyqqvG-VAFVGGLILaLLLVPVNKVIAT 442
Cdd:cd18592 84 RLrSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLilgiVYSTYLL----GpWALLGMLVF-LLFYPLQAFIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 443 RIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIF 522
Cdd:cd18592 159 LTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTF 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 312176403 523 ITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18592 239 LAHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
598-806 |
1.53e-34 |
|
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: 132.33 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 598 LELHGALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFG 667
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVS-LTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 668 LATQEPWIQFATIRDNILFGKTF-DAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKEL 746
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 747 YLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 806
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1228-1452 |
2.12e-34 |
|
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: 140.11 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1228 EPQGQPL--QLGTGWLTQGGVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVL 1305
Cdd:TIGR02857 302 DAAPRPLagKAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1306 LDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGGLDGELG-EGGRS 1381
Cdd:TIGR02857 381 VNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--SDAEIREALERAGLDEFVAALPQGLDTPIgEGGAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1382 LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVL 1452
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1206-1459 |
3.05e-34 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 140.62 E-value: 3.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1206 TQTEAML----VSVERLEEYTcDLPQEPQGQPLQLgtgwLTQGGVEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGR 1281
Cdd:PRK10790 302 TTQQSMLqqavVAGERVFELM-DGPRQQYGNDDRP----LQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1282 TGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDpqgLHKD---RALWQALKQ 1358
Cdd:PRK10790 376 TGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVT---LGRDiseEQVWQALET 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1359 CHLSEVITSMGGLDGELGEGG-RSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIA 1437
Cdd:PRK10790 453 VQLAELARSLPDGLYTPLGEQgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
250 260
....*....|....*....|..
gi 312176403 1438 HRLNTILNSDRVLVLQAGRVVE 1459
Cdd:PRK10790 533 HRLSTIVEADTILVLHRGQAVE 554
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1244-1469 |
4.37e-34 |
|
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: 141.42 E-value: 4.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1244 GGVEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1323
Cdd:TIGR01193 472 GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEPFLFSGTVRENL---DPQGLHKDRaLWQALKQCHLSEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARALLTD 1399
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLllgAKENVSQDE-IWAACEIAEIKDDIENMPLgYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 1400 AKILCIDEATASVdqktDQLLQQTICKRFAN---KTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:TIGR01193 630 SKVLILDESTSNL----DTITEKKIVNNLLNlqdKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
323-797 |
7.63e-34 |
|
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: 138.19 E-value: 7.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 323 GLLYALGLAGGAVLG-AVLQNQYGYEVYKVTLQARGAVLNILYCKALQLGP---SRPPTGEALNLLGTDSERLLNFAGSF 398
Cdd:TIGR02857 42 ELLPALGALALVLLLrALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPrwlQGRPSGELATLALEGVEALDGYFARY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 399 heawgLP-LQLA--ITLYLLYQQVGVAFVGGLIL--ALLLVPVNKV-IATRIMASNQEMLQHKDARVKLVTELLSGIRVI 472
Cdd:TIGR02857 122 -----LPqLVLAviVPLAILAAVFPQDWISGLILllTAPLIPIFMIlIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 473 KFCGWEQALGARV----EACRARELGRLRvIKYLDAACVYLWAALPVVIsIVIFITYVLMGHQLTATKVFTALALVRMLI 548
Cdd:TIGR02857 197 KLFGRAKAQAAAIrrssEEYRERTMRVLR-IAFLSSAVLELFATLSVAL-VAVYIGFRLLAGDLDLATGLFVLLLAPEFY 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 549 LPLNNFPWVINGLLEAKVSLDRIQLFLDlpnHNPQAYYSPDP-PAEPSTVLELHGALFSW---DPVGTSLEtfishLEVK 624
Cdd:TIGR02857 275 LPLRQLGAQYHARADGVAAAEALFAVLD---AAPRPLAGKAPvTAAPASSLEFSGVSVAYpgrRPALRPVS-----FTVP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 625 KGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGKTF-DAQ 693
Cdd:TIGR02857 347 PGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadsWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 694 LYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGML 773
Cdd:TIGR02857 427 EIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA-LRALA 505
|
490 500
....*....|....*....|....
gi 312176403 774 SYTTRLLCTHRTEYLERADAVLLM 797
Cdd:TIGR02857 506 QGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1243-1470 |
1.61e-33 |
|
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: 139.32 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1243 QGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ 1322
Cdd:TIGR03797 449 SGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1323 LAIIPQEPFLFSGTVRENL-DPQGLHKDRAlWQALKQCHLSEVITSM-GGLDGELGEGGRSLSLGQRQLLCLARALLTDA 1400
Cdd:TIGR03797 529 LGVVLQNGRLMSGSIFENIaGGAPLTLDEA-WEAARMAGLAEDIRAMpMGMHTVISEGGGTLSGGQRQRLLIARALVRKP 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1401 KILCIDEATASVDQKTDQLLQQTICKrfANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:TIGR03797 608 RILLFDEATSALDNRTQAIVSESLER--LKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1246-1470 |
8.27e-33 |
|
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: 135.03 E-value: 8.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPN---ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQL 1319
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1320 RSQLAIIPQEPF--LFSG-TVRENL-DPQGLH--------KDRALwQALKQCHLSEvitsmggldGELGEGGRSLSLGQR 1387
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIaEPLRLHgllsraerRERVA-ELLERVGLPP---------DLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1388 QLLCLARALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1463
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVqAQILNllRDLQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....*..
gi 312176403 1464 ATLRNQP 1470
Cdd:COG1123 490 EEVFANP 496
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1247-1456 |
5.48e-32 |
|
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: 124.50 E-value: 5.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1247 EFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAII 1326
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1327 PQEPF--LFSGTVRE----NLDPQGLHKD---RALWQALKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLARALL 1397
Cdd:cd03225 81 FQNPDdqFFGPTVEEevafGLENLGLPEEeieERVEEALELVGLEG----------LRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1398 TDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGR 1456
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1266-1470 |
8.74e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 133.05 E-value: 8.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1266 VTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLePSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---D 1342
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1343 PQGlhKDRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQ 1421
Cdd:PRK11174 448 PDA--SDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAgLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 312176403 1422 QTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1263-1410 |
9.43e-31 |
|
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: 118.90 E-value: 9.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSG-TVRENL 1341
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1342 -------DPQGLHKDRALWQALKQCHLSEVITSmggldgELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATA 1410
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDLADR------PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1246-1459 |
1.64e-30 |
|
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: 121.07 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRP--GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL---R 1320
Cdd:cd03257 2 LEVKNLSVSFPTggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1321 SQLAIIPQEPFL---FSGTVRENL-DPQGLHKD--------RALWQALKQCHLSEVITSMggldgelgeGGRSLSLGQRQ 1388
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGEQIaEPLRIHGKlskkearkEAVLLLLVGVGLPEEVLNR---------YPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 1389 LLCLARALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 1459
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1086-1440 |
3.52e-30 |
|
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: 127.09 E-value: 3.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1086 RASSRELRRLgsltLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQL-MGAAVVS 1164
Cdd:TIGR02868 179 RAAEQALARL----RGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLaAGLAVLG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1165 AI--AGIALVQHQQG---LANPGLVGLSLSYALSLTGLlsglvsSFTQTEAMLVSVERLEEYTCDLPQEPQGQPLQLGTG 1239
Cdd:TIGR02868 255 ALwaGGPAVADGRLApvtLAVLVLLPLAAFEAFAALPA------AAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1240 WLTQGGVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL 1319
Cdd:TIGR02868 329 GLGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1320 RSQLAIIPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARA 1395
Cdd:TIGR02868 408 RRRVSVCAQDAHLFDTTVRENLrlaRPDA--TDEELWAALERVGLADWLRALPDgLDTVLGEGGARLSGGERQRLALARA 485
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 312176403 1396 LLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRL 1440
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
621-801 |
2.56e-29 |
|
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: 115.56 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILfgktf 690
Cdd:cd03228 23 LTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldlesLRKNIAYVPQDPFLFSGTIRENIL----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 691 daqlykevleacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCIL 770
Cdd:cd03228 98 ------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPE-TEALILEALR 140
|
170 180 190
....*....|....*....|....*....|.
gi 312176403 771 GMLSYTTRLLCTHRTEYLERADAVLLMEAGR 801
Cdd:cd03228 141 ALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
355-784 |
3.64e-29 |
|
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: 124.01 E-value: 3.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 355 ARGAVLNILYCKALqLGPSRPPTGEALNLLGTDSERLLNFagsfHEAWGLPLQLAITLYL--------LYQQVGVAFVGG 426
Cdd:TIGR02868 88 LRVRVYERLARQAL-AGRRRLRRGDLLGRLGADVDALQDL----YVRVIVPAGVALVVGAaavaaiavLSVPAALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 427 LILALLLVPVNKVIATRimASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEAcRARELGRLR----VIKYL 502
Cdd:TIGR02868 163 LLLAGFVAPLVSLRAAR--AAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEE-ADRELTRAErraaAATAL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 503 DAACVYLWAALPVVISIVIFITYVlMGHQLT----ATKVFTALALVRmlilPLNNFPWVINGLLEAKVSLDRIqlfLDLP 578
Cdd:TIGR02868 240 GAALTLLAAGLAVLGALWAGGPAV-ADGRLApvtlAVLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERI---VEVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 579 NHNPQAYYSPDPPAEPSTV----LELHGALFSWDPvGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLR 654
Cdd:TIGR02868 312 DAAGPVAEGSAPAAGAVGLgkptLELRDLSAGYPG-APPVLDGVS-LDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 655 GHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGK--TFDAQLYkEVLEACALNDDLSILPAGDQTEVGEK 722
Cdd:TIGR02868 390 GEVTLDGvpvssldqdeVRRRVSVCAQDAHLFDTTVRENLRLARpdATDEELW-AALERVGLADWLRALPDGLDTVLGEG 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 723 GVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHR 784
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHH 529
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1246-1470 |
7.38e-29 |
|
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: 116.14 E-value: 7.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDV--VLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 1320
Cdd:cd03258 2 IELKNVskVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1321 SQLAIIPQEPFLFSG-TVREN----LDPQGLHKDRALWQA---LKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCL 1392
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENvalpLEIAGVPKAEIEERVlelLELVGLEDKADA----------YPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1393 ARALLTDAKILCIDEATASVDQKTDQ----LLQQTICKRfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLR 1467
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQsilaLLRDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
...
gi 312176403 1468 NQP 1470
Cdd:cd03258 230 ANP 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
621-812 |
1.11e-28 |
|
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: 116.10 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAI-------AGELHrLRGH----VAVRGLSKGFGLATQEPWIQFATIRDNILFGKt 689
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEIL-LDGVdirdLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 690 FDAQLyKEVLEAC--ALNDDLSI-LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD---VANH 763
Cdd:cd03249 102 PDATD-EEVEEAAkkANIHDFIMsLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEsekLVQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 312176403 764 LLHRCILGMlsytTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03249 181 ALDRAMKGR----TTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1247-1456 |
1.56e-28 |
|
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: 112.72 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1247 EFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAII 1326
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1327 PQepflfsgtvrenldpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKILCID 1406
Cdd:cd00267 79 PQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312176403 1407 EATASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGR 1456
Cdd:cd00267 106 EPTSGLDPASRERLLELL-RELAeeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1216-1458 |
8.77e-28 |
|
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: 120.24 E-value: 8.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1216 ERLEEYTCDLPQEPQGQPLQLgtgwlTQGGVEFQDVVLAYrPGLPNA-LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLF 1294
Cdd:COG4618 306 RRLNELLAAVPAEPERMPLPR-----PKGRLSVENLTVVP-PGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLV 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1295 RLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVREN------LDPQglhkdrALWQALKQCHLSEVI--- 1365
Cdd:COG4618 380 GVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENiarfgdADPE------KVVAAAKLAGVHEMIlrl 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1366 -----TsmggldgELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHR 1439
Cdd:COG4618 454 pdgydT-------RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVVVITHR 526
|
250
....*....|....*....
gi 312176403 1440 LNTILNSDRVLVLQAGRVV 1458
Cdd:COG4618 527 PSLLAAVDKLLVLRDGRVQ 545
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
620-812 |
1.03e-27 |
|
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: 112.70 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGK- 688
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrksLRSMIGVVLQDTFLFSGTIMENIRLGRp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 689 TFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANhLLHRC 768
Cdd:cd03254 103 NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK-LIQEA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 312176403 769 ILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03254 182 LEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1246-1457 |
1.73e-27 |
|
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: 110.18 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLpnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlELAQLRSQLAI 1325
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSG-TVRENLDpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKILC 1404
Cdd:cd03230 78 LPEEPSLYENlTVRENLK---------------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1405 IDEATASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRV 1457
Cdd:cd03230 119 LDEPTSGLDPESRREFWELL-RELKkeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1246-1457 |
2.62e-27 |
|
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: 111.43 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 1320
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1321 -SQLAIIPQE----PFLfsgTVRENL--------DPQGLHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQR 1387
Cdd:cd03255 81 rRHIGFVFQSfnllPDL---TALENVelplllagVPKKERRERAE-ELLERVGLGDRLNHY----------PSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 1388 QLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQAGRV 1457
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1246-1459 |
4.46e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 110.90 E-value: 4.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 1320
Cdd:COG1136 5 LELRNLTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1321 SQ-LAIIPQEPFLFSG-TVREN----LDPQGLHK----DRALwQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLL 1390
Cdd:COG1136 85 RRhIGFVFQFFNLLPElTALENvalpLLLAGVSRkerrERAR-ELLERVGLGDRLDHRP----------SQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 1391 CLARALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTILNSDRVLVLQAGRVVE 1459
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTgEEVLEllRELNREL-GTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1246-1470 |
7.04e-27 |
|
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: 116.93 E-value: 7.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDGVDTSQLELAQLRSQ 1322
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1323 LAIIPQEPF--LFSGTVRENLD--------PQGLHKDRALWqALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCL 1392
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAealenlglSRAEARARVLE-LLEAVGLERRLDRYPH----------QLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1393 ARALLTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
.
gi 312176403 1470 P 1470
Cdd:COG1123 234 P 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1246-1466 |
3.23e-26 |
|
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: 108.42 E-value: 3.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGlpNALDGVTFCVQPGEKLGIVGRTGSGKSSL-----LLVLFRLLEPSSGRVLLDGVD--TSQLELAQ 1318
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLlrllnRLNDLIPGAPDEGEVLLDGKDiyDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1319 LRSQLAIIPQEPFLFSGTVRENLD----PQGLHKDRAL----WQALKQCHLSEvitsmgglDGELGEGGRSLSLGQRQLL 1390
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEELdervEEALRKAALWD--------EVKDRLHALGLSGGQQQRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1391 CLARALLTDAKILCIDEATASVD----QKTDQLLQQtICKRFankTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPAT 1465
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDpistAKIEELIAE-LKKEY---TIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 312176403 1466 L 1466
Cdd:cd03260 227 I 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
621-812 |
5.29e-26 |
|
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: 108.09 E-value: 5.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAI-------AGELhRLRGH----VAVRGLSKGFGLATQEPWIQFATIRDNILFGKt 689
Cdd:cd03251 23 LDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRI-LIDGHdvrdYTLASLRRQIGLVSQDVFLFNDTVAENIAYGR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 690 FDAQLyKEVLEA---CALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDaDVANHLLH 766
Cdd:cd03251 101 PGATR-EEVEEAaraANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD-TESERLVQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 312176403 767 RCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03251 179 AALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
620-806 |
6.28e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 114.56 E-value: 6.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAG-------------ELHRL-----RGHVAVRGlskgfglatQEPWIQFATIR 681
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingiELRELdpeswRKHLSWVG---------QNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 682 DNILFGKTF--DAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:PRK11174 441 DNVLLGNPDasDEQLQ-QALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 312176403 760 VANHLLHRCILGMLSYTTrLLCTHRTEYLERADAVLLMEAGRLIRAG 806
Cdd:PRK11174 520 SEQLVMQALNAASRRQTT-LMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
598-812 |
8.56e-26 |
|
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: 107.57 E-value: 8.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 598 LELHGALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFG 667
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNIS-LRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 668 LATQEPWIQFATIRDNILFGKTfdAQLYKEVLEACAL---NDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEK 744
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADP--GMSMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 745 ELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03252 158 RILIFDEATSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1246-1471 |
9.25e-26 |
|
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: 107.97 E-value: 9.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1323
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEPFLfS----GTVRENLD-PQGLHK----DRALWQALKQCHLSEvitsmggldGELGEGGRSLSLGQRQLLCLAR 1394
Cdd:COG1124 82 QMVFQDPYA-SlhprHTVDRILAePLRIHGlpdrEERIAELLEQVGLPP---------SFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1395 ALLTDAKILCIDEATASVD---Q-KTDQLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:COG1124 152 ALILEPELLLLDEPTSALDvsvQaEILNLLKDL--REERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAG 229
|
..
gi 312176403 1470 PH 1471
Cdd:COG1124 230 PK 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1246-1464 |
2.36e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 105.90 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ 1322
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1323 LAIIPQE-PFLFSGTVREN----LDPQGLHKD---RALWQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLAR 1394
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENvalpLRVTGKSRKeirRRVREVLDLVGLSDKAKAL----------PHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1395 ALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRfaNKTVLtIA-HRLNtILNS--DRVLVLQAGRVVELDSPA 1464
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETsWEIMEllEEINRR--GTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVRDEARG 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1246-1471 |
7.37e-25 |
|
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: 105.08 E-value: 7.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1325
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSG-TVREN--LDPQGLH------KDRALwQALKQCHLSEvitsmgglDGELGEGGRSLSLGQRQLLCLARAL 1396
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPKLLKwpkekiRERAD-ELLALVGLDP--------AEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1397 LTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLN-TILNSDRVLVLQAGRVVELDSPATLRNQPH 1471
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFkrLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1262-1470 |
1.51e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 110.19 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL 1341
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1342 -----DPQGLHKDRALWQA--------LKQCHLSEVitsmggldgelgeGGRS--LSLGQRQLLCLARALLTDAKILCID 1406
Cdd:PRK10789 410 algrpDATQQEIEHVARLAsvhddilrLPQGYDTEV-------------GERGvmLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1407 EATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1262-1471 |
3.57e-24 |
|
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: 102.90 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLAI-----IPQepfLFSG- 1335
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIgrtfqIPR---LFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1336 TVRENL-------------DPQGLHKDRALW----QALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALLT 1398
Cdd:cd03219 91 TVLENVmvaaqartgsgllLARARREEREAReraeELLERVGLADL----------ADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1399 DAKILCIDEATASV-DQKTDQLLqQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQPH 1471
Cdd:cd03219 161 DPKLLLLDEPAAGLnPEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
621-808 |
5.58e-24 |
|
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: 101.80 E-value: 5.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNI-LFGKT 689
Cdd:cd03244 25 FSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdLRSRISIIPQDPVLFSGTIRSNLdPFGEY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 690 FDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLLHRCI 769
Cdd:cd03244 105 SDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETD-ALIQKTI 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 312176403 770 LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPP 808
Cdd:cd03244 183 REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1246-1459 |
7.80e-24 |
|
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: 101.39 E-value: 7.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVdtsqlELAQLRSQL 1323
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEPFLFS-GTVREN----LDPQGLHK----DRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLAR 1394
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvalgLELQGVPKaearERAE-ELLELVGLSGFENAY----------PHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1395 ALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLN-TILNSDRVLVLQA--GRVVE 1459
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1246-1471 |
7.87e-24 |
|
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: 101.81 E-value: 7.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ 1322
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1323 LAIIPQEPFLFSG-TVRENL---------DPQGLHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCL 1392
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVafplrehtrLSEEEIREIVL-EKLEAVGLRGAEDLY----------PAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1393 ARALLTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIrsLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
..
gi 312176403 1470 PH 1471
Cdd:cd03261 228 DD 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1246-1463 |
9.32e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.76 E-value: 9.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1325
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEP---FLFSgTVRENLdPQGLHKDRalwqaLKQCHLSEVITSMGGLDGELGEGGR---SLSLGQRQLLCLARALLTD 1399
Cdd:PRK13632 88 IFQNPdnqFIGA-TVEDDI-AFGLENKK-----VPPKKMKDIIDDLAKKVGMEDYLDKepqNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1400 AKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 1463
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMvdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1241-1452 |
2.13e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 108.58 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1241 LTQGGVEFQDVVLAY--RPGLPNALDgVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE-------------------- 1298
Cdd:PTZ00265 1161 DIKGKIEIMDVNFRYisRPNVPIYKD-LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtne 1239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1299 ----------------------------------PSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDpq 1344
Cdd:PTZ00265 1240 qdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-- 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1345 gLHKDRALWQALKQ----CHLSEVITSMGGLD-GELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 1419
Cdd:PTZ00265 1318 -FGKEDATREDVKRackfAAIDEFIESLPNKYdTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1396
|
250 260 270
....*....|....*....|....*....|....*
gi 312176403 1420 LQQTIC--KRFANKTVLTIAHRLNTILNSDRVLVL 1452
Cdd:PTZ00265 1397 IEKTIVdiKDKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1246-1456 |
2.31e-23 |
|
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: 99.47 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPG---LPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVlldgvdtsqlelaQLRSQ 1322
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1323 LAIIPQEPFLFSGTVREN------LDPQglhkdRaLWQALKQCHL------------SEV----ITsmggldgelgeggr 1380
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENilfgkpFDEE-----R-YEKVIKACALepdleilpdgdlTEIgekgIN-------------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1381 sLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT-DQLLQQTICKRFA-NKTVLTIAHRLNTILNSDRVLVLQAGR 1456
Cdd:cd03250 128 -LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVgRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1253-1458 |
3.56e-23 |
|
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: 98.28 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1253 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQepfl 1332
Cdd:cd03214 5 LSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1333 fsgtvrenldpqglhkdralwqALKQC---HLSEvitsmggldgelgEGGRSLSLGQRQLLCLARALLTDAKILCIDEAT 1409
Cdd:cd03214 81 ----------------------ALELLglaHLAD-------------RPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1410 ASVD----QKTDQLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1458
Cdd:cd03214 126 SHLDiahqIELLELLRRL--ARERGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1246-1466 |
5.01e-23 |
|
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: 100.12 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGlpNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1325
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFL-FSGTVRE----------NLDPQGLHKDRAL-WQALKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLA 1393
Cdd:COG1120 80 VPQEPPApFGLTVRElvalgryphlGLFGRPSAEDREAvEEALERTGLEH----------LADRPVDELSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1394 RALLTDAKILCIDEATASVD---QKtdQLLQqtICKRFA---NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 1466
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDlahQL--EVLE--LLRRLArerGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEV 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1246-1471 |
7.79e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.39 E-value: 7.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRpGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDtsqleLAQLRSQLAI 1325
Cdd:COG1121 7 IELENLTVSYG-GRP-VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFL---FSGTVRE----NLDPQ-GL-----HKDRAL-WQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLLC 1391
Cdd:COG1121 80 VPQRAEVdwdFPITVRDvvlmGRYGRrGLfrrpsRADREAvDEALERVGLEDLADRPI----------GELSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1392 LARALLTDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTIL-NSDRVLVLqAGRVVELDSPATLRNQ 1469
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAHGPPEEVLTP 228
|
..
gi 312176403 1470 PH 1471
Cdd:COG1121 229 EN 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1247-1458 |
1.32e-22 |
|
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: 97.60 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1247 EFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqLELAQLRSQLAII 1326
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1327 PQE---PFLFSGTVRE----NLDPQG--------LHKDRALwQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLC 1391
Cdd:cd03235 74 PQRrsiDRDFPISVRDvvlmGLYGHKglfrrlskADKAKVD-EALERVGLSELADR----------QIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 1392 LARALLTDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILNS-DRVLVLqAGRVV 1458
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLL-NRTVV 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
621-802 |
2.95e-22 |
|
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: 97.16 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFG-KT 689
Cdd:cd03248 35 FTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkyLHSKVSLVGQEPVLFARSLQDNIAYGlQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 690 FDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCI 769
Cdd:cd03248 115 CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQVQQAL 193
|
170 180 190
....*....|....*....|....*....|...
gi 312176403 770 LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRL 802
Cdd:cd03248 194 YDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
621-804 |
6.21e-22 |
|
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: 96.00 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV-----AVRGLSKGFGLATQE----PWiqfATIRDNILFGKTF- 690
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgePVTGPGPDRGYVFQQdallPW---LTVLDNVALGLELq 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 691 ---DAQLYKEVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 761
Cdd:cd03293 102 gvpKAEARERAEELLEL--------------VGLSGFenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 312176403 762 NHlLHRCILGMLSYT--TRLLCTHRTE---YLerADAVLLMEA--GRLIR 804
Cdd:cd03293 168 EQ-LQEELLDIWRETgkTVLLVTHDIDeavFL--ADRVVVLSArpGRIVA 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1262-1456 |
9.05e-22 |
|
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: 94.18 E-value: 9.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLE--LAQLRSQLAIIPQEPFLFSG-TVR 1338
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1339 ENLdpqglhkdrALwqalkqchlsevitsmggldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 1418
Cdd:cd03229 95 ENI---------AL----------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 312176403 1419 LLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGR 1456
Cdd:cd03229 138 EVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1247-1458 |
9.55e-22 |
|
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: 96.10 E-value: 9.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1247 EFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQL 1323
Cdd:cd03256 2 EVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEPFLFSG-TVREN------------------LDPQglHKDRALwQALKQCHLSEVITSMGGLdgelgeggrsLSL 1384
Cdd:cd03256 81 GMIFQQFNLIERlSVLENvlsgrlgrrstwrslfglFPKE--EKQRAL-AALERVGLLDKAYQRADQ----------LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 1385 GQRQLLCLARALLTDAKILCIDEATASVDQKTDQ----LLQQtICKRFaNKTVLTIAHRLNTIL-NSDRVLVLQAGRVV 1458
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRqvmdLLKR-INREE-GITVIVSLHQVDLAReYADRIVGLKDGRIV 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1262-1458 |
1.14e-21 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 95.13 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlELAQLRSQLAIIPQEPFLFSG-TVREN 1340
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 LDP-QGLH--KDRALWQALkqchlsEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTD 1417
Cdd:cd03266 99 LEYfAGLYglKGDELTARL------EELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 312176403 1418 QLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1458
Cdd:cd03266 173 RALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1246-1459 |
1.90e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.46 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 1320
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1321 SQLAIIPQEPFLFSG-TVREN----------------------LDPQGLhKDRAlwqalkQCHLSEvitsmggldgelge 1377
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENvalpleiagvpkaeirkrvaelLELVGL-SDKA------DAYPSQ-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1378 ggrsLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ----LLQQtICKRFaNKTVLTIAHRLNTILN-SDRVLVL 1452
Cdd:COG1135 141 ----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLKD-INREL-GLTIVLITHEMDVVRRiCDRVAVL 214
|
....*..
gi 312176403 1453 QAGRVVE 1459
Cdd:COG1135 215 ENGRIVE 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
620-821 |
2.52e-21 |
|
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: 100.21 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEpwIQF--ATIRDNI-LF 686
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreeLGRHIGYLPQD--VELfdGTIAENIaRF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 GKTfDAQlykEVLEACALND--DLsI--LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN 762
Cdd:COG4618 430 GDA-DPE---KVVAAAKLAGvhEM-IlrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEA 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 763 HLLhRCILGM-LSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPKA 821
Cdd:COG4618 505 ALA-AAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1246-1462 |
3.24e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.79 E-value: 3.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLP--NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 1320
Cdd:PRK11153 2 IELKNISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1321 SQLAIIPQEpF--LFSGTVREN----------------------LDPQGL--HKDRALWQalkqchlsevitsmggldge 1374
Cdd:PRK11153 82 RQIGMIFQH-FnlLSSRTVFDNvalplelagtpkaeikarvtelLELVGLsdKADRYPAQ-------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1375 lgeggrsLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ----LLQQtICKRFaNKTVLTIAHRLNTILN-SDRV 1449
Cdd:PRK11153 141 -------LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRsileLLKD-INREL-GLTIVLITHEMDVVKRiCDRV 211
|
250
....*....|...
gi 312176403 1450 LVLQAGRVVELDS 1462
Cdd:PRK11153 212 AVIDAGRLVEQGT 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
620-754 |
4.23e-21 |
|
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: 91.17 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQ-FATIRDNILFG- 687
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderksLRKEIGYVFQDPQLFpRLTVRENLRLGl 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176403 688 -------KTFDAQLYkEVLEACALNDDLSilpagdqTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:pfam00005 85 llkglskREKDARAE-EALEKLGLGDLAD-------RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
621-811 |
4.60e-21 |
|
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: 93.94 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGfGLATQEPWIQFA----------TIRDNILFG--- 687
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT-DVPVQERNVGFVfqhyalfrhmTVFDNVAFGlrv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 --------KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:cd03296 102 kprserppEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 760 VANHL------LHRCIlgmlsYTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:cd03296 171 VRKELrrwlrrLHDEL-----HVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
428-811 |
4.66e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.80 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 428 ILALLLVP----VNKVIATRIMASNQEmLQHKDARV-KLVTELLSGIRVIKFCGWEQalgarVEACRARE-------LGR 495
Cdd:TIGR00958 305 MVTLINLPlvflAEKVFGKRYQLLSEE-LQEAVAKAnQVAEEALSGMRTVRSFAAEE-----GEASRFKEaleetlqLNK 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 496 LRVIKYLdaacVYLWAAlpVVISIVIFITYVLMGHQLTATKVFTALALVRMLILP------LNNFPWVINGLLEAKVSLD 569
Cdd:TIGR00958 379 RKALAYA----GYLWTT--SVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQeqlgeaVRVLSYVYSGMMQAVGASE 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 570 RIQLFLDL-PNHNPQAYYSPDPPaepSTVLELHGALFSW-----DPVGTSLeTFishlEVKKGMLVGIVGKVGCGKSSLL 643
Cdd:TIGR00958 453 KVFEYLDRkPNIPLTGTLAPLNL---EGLIEFQDVSFSYpnrpdVPVLKGL-TF----TLHPGEVVALVGPSGSGKSTVA 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 644 AAI-------AGEL------------HRLRGHVAVRGlskgfglatQEPWIQFATIRDNILFGKTF--DAQLYKEVLEAC 702
Cdd:TIGR00958 525 ALLqnlyqptGGQVlldgvplvqydhHYLHRQVALVG---------QEPVLFSGSVRENIAYGLTDtpDEEIMAAAKAAN 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 703 AlNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVaNHLLH--RCILGMlsytTRLL 780
Cdd:TIGR00958 596 A-HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-EQLLQesRSRASR----TVLL 669
|
410 420 430
....*....|....*....|....*....|.
gi 312176403 781 CTHRTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:TIGR00958 670 IAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
620-807 |
4.70e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 99.40 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAI-------AGE------------LHRLRGHVAVrglskgfglATQEPWIQFATI 680
Cdd:PRK10789 335 NFTLKPGQMLGICGPTGSGKSTLLSLIqrhfdvsEGDirfhdipltklqLDSWRSRLAV---------VSQTPFLFSDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 681 RDNILFGKTfDA--QLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:PRK10789 406 ANNIALGRP-DAtqQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312176403 759 DVANHLLHRcilgmLS----YTTRLLCTHRTEYLERADAVLLMEAGRLIRAGP 807
Cdd:PRK10789 485 RTEHQILHN-----LRqwgeGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
605-812 |
5.72e-21 |
|
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: 93.45 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 605 FSWDPVGTSLETfIShLEVKKGMLVGIVGKVGCGKSSLLAAiageLHRL----RGHVAVRG----------LSKGFGLAT 670
Cdd:cd03253 8 FAYDPGRPVLKD-VS-FTIPAGKKVAIVGPSGSGKSTILRL----LFRFydvsSGSILIDGqdirevtldsLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 671 QEPWIQFATIRDNILFGK--TFDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYL 748
Cdd:cd03253 82 QDTVLFNDTIGYNIRYGRpdATDEEVI-EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176403 749 LDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03253 161 LDEATSALDT-HTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1246-1459 |
6.99e-21 |
|
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: 92.58 E-value: 6.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLpnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRsqLAI 1325
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSG-TVRENL--------DPQGLHKDRALWqALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARAL 1396
Cdd:cd03259 77 VFQDYALFPHlTVAENIafglklrgVPKAEIRARVRE-LLELVGLEGLLNRY----------PHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1397 LTDAKILCIDEATASVDQKTDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVE 1459
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALAlADRIAVMNEGRIVQ 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1262-1470 |
7.56e-21 |
|
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: 95.12 E-value: 7.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP---SSGRVLLDGVDTSQL---ELAQLR-SQLAIIPQEPF--- 1331
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLsekELRKIRgREIQMIFQDPMtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1332 --LFsgTVRENL-DPQGLH--------KDRALwQALKQCHLSEVITSMggldgelgeggRS----LSLGQRQLLCLARAL 1396
Cdd:COG0444 100 npVM--TVGDQIaEPLRIHgglskaeaRERAI-ELLERVGLPDPERRL-----------DRypheLSGGMRQRVMIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1397 LTDAKILCIDEATASVD---QKtdQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:COG0444 166 ALEPKLLIADEPTTALDvtiQA--QILNllKDLQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1263-1465 |
1.23e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.30 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFL-FSGTVRE-- 1339
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEvv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1340 --NLDPQGLHK---DRALWQALKQC---HLSEvitsmggldgelgEGGRSLSLGQRQLLCLARALL------TDAKILCI 1405
Cdd:PRK13548 98 amGRAPHGLSRaedDALVAAALAQVdlaHLAG-------------RDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1406 DEATASVDqktdqLLQQ----TICKRFANK---TVLTIAHRLN-TILNSDRVLVLQAGRVVELDSPAT 1465
Cdd:PRK13548 165 DEPTSALD-----LAHQhhvlRLARQLAHErglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
621-806 |
1.49e-20 |
|
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: 90.45 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG---------LSKGFGLATQEPWIQFATIRDNIlfgktfd 691
Cdd:cd03247 23 LELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekaLSSLISVLNQRPYLFDTTLRNNL------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 692 aqlykevleacalnddlsilpagdqtevgekGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhRCILG 771
Cdd:cd03247 96 -------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL-SLIFE 143
|
170 180 190
....*....|....*....|....*....|....*
gi 312176403 772 MLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 806
Cdd:cd03247 144 VLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1246-1464 |
1.80e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.16 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1325
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEP-FLFSG-TVREN----LDPQGLHKD---RALWQALKQCHLSEVITsmggldgelgEGGRSLSLGQRQLLCLARAL 1396
Cdd:PRK13635 86 VFQNPdNQFVGaTVQDDvafgLENIGVPREemvERVDQALRQVGMEDFLN----------REPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1397 LTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPA 1464
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
621-806 |
2.12e-20 |
|
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: 91.04 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------KGFGLATQE----PWIqfaTIRDNILFG- 687
Cdd:cd03259 21 LTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperRNIGMVFQDyalfPHL---TVAENIAFGl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 ---KTFDAQLYKEVLEACALNDDLSILpagdqtevGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL 764
Cdd:cd03259 98 klrGVPKAEIRARVRELLELVGLEGLL--------NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 312176403 765 LH--RCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 806
Cdd:cd03259 170 REelKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
621-801 |
2.96e-20 |
|
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: 90.60 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFG- 687
Cdd:cd03225 22 LTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkeLRRKVGLVFQNPDDQFfgPTVEEEVAFGl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 ------KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD---- 757
Cdd:cd03225 102 enlglpEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDpagr 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 312176403 758 ADVANHLLHRCILGMlsytTRLLCTHRTEYLER-ADAVLLMEAGR 801
Cdd:cd03225 171 RELLELLKKLKAEGK----TIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
621-804 |
4.41e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 91.69 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV-----AVRGLSKGFGLATQE----PWiqfATIRDNILFG---- 687
Cdd:COG1116 32 LTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVlvdgkPVTGPGPDRGVVFQEpallPW---LTVLDNVALGlelr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 ---KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHl 764
Cdd:COG1116 109 gvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRER- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 312176403 765 LHRCILGMLSYT--TRLLCTHRTE---YLerADAVLLMEA--GRLIR 804
Cdd:COG1116 177 LQDELLRLWQETgkTVLFVTHDVDeavFL--ADRVVVLSArpGRIVE 221
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
962-1218 |
4.42e-20 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 93.33 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 962 SDIRFYLTVYATIAGVNSLCTL--LRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSL 1039
Cdd:cd18600 65 TFTSSYYVFYIYVGVADSLLAMgfFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1040 PFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRA 1119
Cdd:cd18600 145 PLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1120 TGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlanPGLVGLSLSYALSLTGLLS 1199
Cdd:cd18600 225 FGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDG---EGRVGIILTLAMNIMSTLQ 301
|
250
....*....|....*....
gi 312176403 1200 GLVSSFTQTEAMLVSVERL 1218
Cdd:cd18600 302 WAVNTSIDVDSLMRSVSRI 320
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1263-1470 |
5.57e-20 |
|
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: 90.68 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlRSQLAII--PQEPFLFSG-TVRE 1339
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1340 NLDP--QGLHKDRALWQA-----LKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASV 1412
Cdd:cd03218 95 NILAvlEIRGLSKKEREEkleelLEEFHITHLRKSKAS----------SLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1413 DQKTDQLLQQTIcKRFANKT--VLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:cd03218 165 DPIAVQDIQKII-KILKDRGigVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1262-1458 |
6.12e-20 |
|
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: 88.25 E-value: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAIIPQepflfsgtvren 1340
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 ldpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKILCIDEATASVDQK-TDQL 1419
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 312176403 1420 LQqtICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVV 1458
Cdd:cd03216 122 FK--VIRRLRAqgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
510-850 |
8.23e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.41 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 510 WAALPVV-------ISIV-IFI--TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVsldRIQLFLDLPN 579
Cdd:PRK13657 238 WWALASVlnraastITMLaILVlgAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAP---KLEEFFEVED 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 580 HNPQAYYSPD--PPAEPSTVLELHGALFSWDPVGTSLE--TFishlEVKKGMLVGIVGKVGCGKSSLLAAiageLHRL-- 653
Cdd:PRK13657 315 AVPDVRDPPGaiDLGRVKGAVEFDDVSFSYDNSRQGVEdvSF----EAKPGQTVAIVGPTGAGKSTLINL----LQRVfd 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 654 --RGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGKT--FDAQLYkEVLEACALNDDLSILPAGDQTEV 719
Cdd:PRK13657 387 pqSGRILIDGtdirtvtrasLRRNIAVVFQDAGLFNRSIEDNIRVGRPdaTDEEMR-AAAERAQAHDFIERKPDGYDTVV 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 720 GEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEA 799
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV-ETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDN 544
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 312176403 800 GRLIRAGPPSEILplvqavpkawAENGQESDSATAQSVQNPEKTKEGLEEE 850
Cdd:PRK13657 545 GRVVESGSFDELV----------ARGGRFAALLRAQGMLQEDERRKQPAAE 585
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1214-1465 |
8.54e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.26 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1214 SVERLEEYTCDLpQEPQGQPLQLGTGWLTQGG-VEFQDVVLAyrpgLPNA---LDGVTFCVQPGEKLGIVGRTGSGKSSl 1289
Cdd:COG4178 331 TVDRLAGFEEAL-EAADALPEAASRIETSEDGaLALEDLTLR----TPDGrplLEDLSLSLKPGERLLITGPSGSGKST- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1290 llvlfrllepssgrvLLDGvdtsqleLAQL------------RSQLAIIPQEPFLFSGTVRENL---DPQGLHKDRALWQ 1354
Cdd:COG4178 405 ---------------LLRA-------IAGLwpygsgriarpaGARVLFLPQRPYLPLGTLREALlypATAEAFSDAELRE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1355 ALKQCHLSEVITSMGGLDGELgeggRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVL 1434
Cdd:COG4178 463 ALEAVGLGHLAERLDEEADWD----QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVI 538
|
250 260 270
....*....|....*....|....*....|.
gi 312176403 1435 TIAHRLNTILNSDRVLVLQAGRVVELDSPAT 1465
Cdd:COG4178 539 SVGHRSTLAAFHDRVLELTGDGSWQLLPAEA 569
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1247-1468 |
1.11e-19 |
|
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: 89.42 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1247 EFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAI 1325
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSG-TVRENLD--PQGLHKDRALWQ---------ALKQchlsevitsmggldgELGEGGRSLSLGQRQLLCLA 1393
Cdd:cd03224 80 VPEGRRIFPElTVEENLLlgAYARRRAKRKARlervyelfpRLKE---------------RRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1394 RALLTDAKILCIDEATAS-----VDQKTDQLlqQTICKRfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLR 1467
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGlapkiVEEIFEAI--RELRDE--GVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
.
gi 312176403 1468 N 1468
Cdd:cd03224 221 A 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
621-812 |
2.90e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 90.98 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH------RLRGHVAVRGLS---KGFGLATQepwiQFA-----TIRDNILF 686
Cdd:COG1118 23 LEIASGELVALLGPSGSGKTTLLRIIAGLETpdsgriVLNGRDLFTNLPpreRRVGFVFQ----HYAlfphmTVAENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 GktfdaqlykevleacalnddLSILPAGDQtEVGEKgVT------------------LSGGQRARIALARAVYQEKELYL 748
Cdd:COG1118 99 G--------------------LRVRPPSKA-EIRAR-VEellelvqlegladrypsqLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 749 LDDPLAAVDADVANHL------LHRCILGmlsytTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1118 157 LDEPFGALDAKVRKELrrwlrrLHDELGG-----TTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1262-1459 |
4.11e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAIIPQEPFLFSG-TVRE 1339
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1340 NL------------DPQGLHKdRALwQALKQCHLS-----EVitsmggldgelgeggRSLSLGQRQLLCLARALLTDAKI 1402
Cdd:COG1129 99 NIflgreprrggliDWRAMRR-RAR-ELLARLGLDidpdtPV---------------GDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1403 LCIDEATASVDQK-TDQLLQqtICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVE 1459
Cdd:COG1129 162 LILDEPTASLTEReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
621-812 |
4.74e-19 |
|
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: 87.77 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFG- 687
Cdd:COG1122 22 LSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlreLRRKVGLVFQNPDDQLfaPTVEEDVAFGp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 -------KTFDAQLyKEVLEACALND--DLSILpagdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:COG1122 102 enlglprEEIRERV-EEALELVGLEHlaDRPPH-------------ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 759 DVANHLLHrcILGML--SYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1122 168 RGRRELLE--LLKRLnkEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1246-1457 |
6.87e-19 |
|
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: 87.08 E-value: 6.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ 1322
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1323 LAIIPQEPFLFSG-TVREN--LDPQGLHKDRALWQ-----ALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLAR 1394
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENvaFALEVTGVPPREIRkrvpaALELVGLSHKHRALPA----------ELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1395 ALLTDAKILCIDEATASVDQKTD----QLLQQtICKRFANKTVLTIAHRL-NTIlnSDRVLVLQAGRV 1457
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTweimNLLKK-INKAGTTVVVATHAKELvDTT--RHRVIALERGKL 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1262-1470 |
7.93e-19 |
|
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: 88.08 E-value: 7.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ-LAIIPQEPFLFSG-T 1336
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRKkISMVFQSFALLPHrT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1337 VREN----LDPQGLHK----DRALwQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLLCLARALLTDAKILCIDEA 1408
Cdd:cd03294 119 VLENvafgLEVQGVPRaereERAA-EALELVGLEGWEHKYP----------DELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1409 TASVD-----QKTDQLLQqtiCKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:cd03294 188 FSALDplirrEMQDELLR---LQAELQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
621-802 |
1.02e-18 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 86.41 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS----------KGFGLATQEPWIQFATIRDNILF---- 686
Cdd:COG4619 21 LTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrRQVAYVPQEPALWGGTVRDNLPFpfql 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 -GKTFDAQLYKEVLEACALNDDlsILpagdQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLL 765
Cdd:COG4619 101 rERKFDRERALELLERLGLPPD--IL----DKPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT-RRV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 312176403 766 HRCILGMLSY--TTRLLCTHRTEYLER-ADAVLLMEAGRL 802
Cdd:COG4619 170 EELLREYLAEegRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1262-1470 |
1.47e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 88.64 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQLAIIPQEPF--L---- 1332
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDPYasLnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1333 -FSGTVRENLDPQGLH-----KDRALwQALKQCHLSEvitsmggldgelGEGGR---SLSLGQRQLLCLARALLTDAKIL 1403
Cdd:COG4608 113 tVGDIIAEPLRIHGLAskaerRERVA-ELLELVGLRP------------EHADRyphEFSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1404 CIDEATASVD---QKtdQ---LLQ--QticKRFaNKTVLTIAHRLNT---IlnSDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:COG4608 180 VCDEPVSALDvsiQA--QvlnLLEdlQ---DEL-GLTYLFISHDLSVvrhI--SDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
621-812 |
1.47e-18 |
|
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: 87.02 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFA-TIRDNILFGKT 689
Cdd:COG1120 22 LSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrreLARRIAYVPQEPPAPFGlTVRELVALGRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 690 --------FDAQLYKEVLEACAlnddlsilpagdQTEVG---EKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:COG1120 102 phlglfgrPSAEDREAVEEALE------------RTGLEhlaDRPVdELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 758 advANHLLHrcILGMLSYTTR------LLCTH------RTeylerADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1120 170 ---LAHQLE--VLELLRRLARergrtvVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1263-1470 |
1.56e-18 |
|
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: 86.62 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSqlELAQLRSQLAIIPQEPFLFSG-TVRENL 1341
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1342 DpQGLHKDRALWQALKQchlsEV--ITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 1419
Cdd:cd03299 93 A-YGLKKRKVDKKEIER----KVleIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1420 LQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:cd03299 168 LREELKKirKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
621-812 |
1.63e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 86.27 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS---------KGFGLATQEPWI-QFATIRDNILF---- 686
Cdd:COG1131 21 LTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvardpaevrRRIGYVPQEPALyPDLTVRENLRFfarl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 ---GKTFDAQLYKEVLEACALNDDLsilpagdqtevGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANH 763
Cdd:COG1131 101 yglPRKEARERIDELLELFGLTDAA-----------DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP-EARR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 312176403 764 LLHRCILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1131 169 ELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELK 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1263-1424 |
1.80e-18 |
|
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: 85.61 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLAIIPQEPFLFSG-TVRENL 1341
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPElTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1342 D----PQGLHKDRA-LWQALKQCHLSEVITsmggldgelgEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 1416
Cdd:COG4133 97 RfwaaLYGLRADREaIDEALEAVGLAGLAD----------LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
....*...
gi 312176403 1417 DQLLQQTI 1424
Cdd:COG4133 167 VALLAELI 174
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1246-1470 |
1.97e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL-ELAQLRSQLA 1324
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1325 IIPQEP-FLFSG-TVRENL--DPQGL---------HKDRALWQA--LKQCHLSEvitsmggldgelgeggRSLSLGQRQL 1389
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDLafGPENLclppieirkRVDRALAEIglEKYRHRSP----------------KTLSGGQGQC 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1390 LCLARALLTDAKILCIDEATASVDQKTDQLLQQTIcKRF--ANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLR 1467
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERI-KKLheKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
...
gi 312176403 1468 NQP 1470
Cdd:PRK13644 224 SDV 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
620-806 |
2.12e-18 |
|
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: 85.42 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVK---KGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL-----SKGFGLATQEPWIQFA----------TIR 681
Cdd:cd03297 14 TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVfqqyalfphlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 682 DNILFGKTF-----DAQLYKEVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:cd03297 94 ENLAFGLKRkrnreDRISVDELLDLLGL------------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 756 VDADVANHLLH--RCILGMLSYTTrLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:cd03297 162 LDRALRLQLLPelKQIKKNLNIPV-IFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
622-808 |
2.20e-18 |
|
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: 85.16 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 622 EVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNI-LFGKTF 690
Cdd:cd03369 30 KVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledLRSSLTIIPQDPTLFSGTIRSNLdPFDEYS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 691 DAQLYKevleacALnddlsilpagdqtEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCIL 770
Cdd:cd03369 110 DEEIYG------AL-------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA-TDALIQKTIR 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 312176403 771 GMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPP 808
Cdd:cd03369 170 EEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
567-812 |
2.90e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.58 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 567 SLDRIQLFLDLPNHNPQAYYSPDPPAepstvlelhgalfSWdPVGTSLETFISHLEVKKGM---------------LVGI 631
Cdd:PLN03232 1202 SVERVGNYIDLPSEATAIIENNRPVS-------------GW-PSRGSIKFEDVHLRYRPGLppvlhglsffvspseKVGV 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 632 VGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYkEVLE 700
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdLRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDADLW-EALE 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 701 ACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVaNHLLHRCILGMLSYTTRLL 780
Cdd:PLN03232 1347 RAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-DSLIQRTIREEFKSCTMLV 1425
|
250 260 270
....*....|....*....|....*....|..
gi 312176403 781 CTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PLN03232 1426 IAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
620-811 |
2.98e-18 |
|
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: 85.31 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAG-----ELHRLRGHVAVRG------------LSKGFGLATQEPWIQFATIRD 682
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGkdiydldvdvleLRRRVGMVFQKPNPFPGSIYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 683 NILFG--------KTFDAQLYKEVLEACALNDDLSilpagDQTevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:cd03260 100 NVAYGlrlhgiklKEELDERVEEALRKAALWDEVK-----DRL----HALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 755 AVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:cd03260 171 ALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
620-812 |
3.87e-18 |
|
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: 85.68 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGF---------GLATQEPWI-QFATIRDNILFgkt 689
Cdd:COG4555 21 SFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKeprearrqiGVLPDERGLyDRLTVRENIRY--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 690 FdAQLYKEVLEACALNDDlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRC 768
Cdd:COG4555 98 F-AELYGLFDEELKKRIE-ELIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM-ARRLLREI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 312176403 769 ILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG4555 175 LRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
621-801 |
4.08e-18 |
|
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: 83.06 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFglatqepwIQFATIRDNIlfgktfdaqlykevle 700
Cdd:cd00267 20 LTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--------LPLEELRRRI---------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 701 acalnddlSILPagdQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLLHRCILGML-SYTTRL 779
Cdd:cd00267 76 --------GYVP---Q---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAeEGRTVI 134
|
170 180
....*....|....*....|...
gi 312176403 780 LCTHRTEYLERA-DAVLLMEAGR 801
Cdd:cd00267 135 IVTHDPELAELAaDRVIVLKDGK 157
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1246-1463 |
4.31e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.42 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG----VDTSQLELAQ 1318
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1319 LRSQLAIIPQ--EPFLFSGTVRENLD--PQ--GLHKDRALWQA---LKQCHLSEVITSMGGLdgelgeggrSLSLGQRQL 1389
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEfgPKnfGFSEDEAKEKAlkwLKKVGLSEDLISKSPF---------ELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1390 LCLARALLTDAKILCIDEATASVDQKT-DQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1463
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASP 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1262-1470 |
6.09e-18 |
|
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: 89.36 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSlLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQLAIIPQEPFlfsG--- 1335
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKST-LGLALLRLIPSEGEIRFDGQDLDGLsrrALRPLRRRMQVVFQDPF---Gsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1336 -------TVRENLDPQGLHKDRA-----LWQALKQCHLSEvitsmggldgelGEGGR---SLSLGQRQLLCLARALLTDA 1400
Cdd:COG4172 377 prmtvgqIIAEGLRVHGPGLSAAerrarVAEALEEVGLDP------------AARHRyphEFSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 1401 KILCIDEATASVD---QKtdQLLQ--QTICKRFaNKTVLTIAHRLNTI--LnSDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:COG4172 445 KLLVLDEPTSALDvsvQA--QILDllRDLQREH-GLAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
621-816 |
9.20e-18 |
|
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: 84.09 E-value: 9.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------------LSKGFGLATQepwiQFA-----TIRD 682
Cdd:cd03261 21 LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrLRRRMGMLFQ----SGAlfdslTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 683 NILF--------GKTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:cd03261 97 NVAFplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 755 AVD---ADVANHLLHRC--ILGMlsytTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL----PLVQ 816
Cdd:cd03261 166 GLDpiaSGVIDDLIRSLkkELGL----TSIMVTHDlDTAFAIADRIAVLYDGKIVAEGTPEELRasddPLVR 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1263-1466 |
1.10e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.17 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEP-FLFSG-TVREN 1340
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdNQFVGaTVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 ----LDPQGL-HKD--RALWQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVD 1413
Cdd:PRK13650 103 vafgLENKGIpHEEmkERVNEALELVGMQDFKEREPA----------RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 1414 QKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 1466
Cdd:PRK13650 173 PEGRLELIKTIkgIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
620-802 |
1.45e-17 |
|
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: 81.88 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILfgkt 689
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpneLGDHVGYLPQDDELFSGSIAENIL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 690 fdaqlykevleacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCI 769
Cdd:cd03246 98 -------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVE-GERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....
gi 312176403 770 LGM-LSYTTRLLCTHRTEYLERADAVLLMEAGRL 802
Cdd:cd03246 140 AALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
621-837 |
2.41e-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: 87.27 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGEL---HRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNIL 685
Cdd:COG1123 27 LTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGrdllelsealRGRRIGMVFQDPMTQLnpVTVGDQIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 686 FG----KTFDAQLYKEVLEACALnddlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 761
Cdd:COG1123 107 EAlenlGLSRAEARARVLELLEA--------VGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 762 NHLLHrcILGML---SYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEILPLVQ---AVPKAWAENGQESDSATA 834
Cdd:COG1123 179 AEILD--LLRELqreRGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQalaAVPRLGAARGRAAPAAAA 256
|
...
gi 312176403 835 QSV 837
Cdd:COG1123 257 AEP 259
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1255-1454 |
2.61e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.45 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1255 YRPGLPNALDGVTFCVQPGE-KLgIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLF 1333
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEfKL-ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1334 SGTVRENL-----------DPQGLHKDRALWqALKQCHLSEVITsmggldgelgeggrSLSLGQRQLLCLARALLTDAKI 1402
Cdd:PRK10247 94 GDTVYDNLifpwqirnqqpDPAIFLDDLERF-ALPDTILTKNIA--------------ELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1403 LCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQA 1454
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRyvREQNIAVLWVTHDKDEINHADKVITLQP 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
621-812 |
2.95e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 82.83 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfgLATQEPWI-----------QF-ATIRDNILFG- 687
Cdd:COG1121 27 LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP----PRRARRRIgyvpqraevdwDFpITVRDVVLMGr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 -------KTFDAQLYKEVLEACALnddLSILPAGDQTeVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADV 760
Cdd:COG1121 103 ygrrglfRRPSRADREAVDEALER---VGLEDLADRP-IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 761 ANHLLHrcILGMLS--YTTRLLCTHRTEYLER-ADAVLLMeAGRLIRAGPPSEIL 812
Cdd:COG1121 175 EEALYE--LLRELRreGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVL 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
286-571 |
3.58e-17 |
|
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: 83.75 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 286 LALGLLkLVGTMLGFSGPLLLSLLVGFLEeGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYC 365
Cdd:cd07346 3 LALLLL-LLATALGLALPLLTKLLIDDVI-PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 366 KALQLGPS---RPPTGEALNLLGTDSERLLNFAGS-FHEAWGLPLQLAITL-YLLYQQVGVAFVGgLILALLLVPVNKVI 440
Cdd:cd07346 81 HLQRLSLSffdRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALvILFYLNWKLTLVA-LLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 441 ATRIMASNQEmLQHKDARV-KLVTELLSGIRVIKFCGWEQALGARVEAcRARELGRLRV-IKYLDAACVYLWAALPVVIS 518
Cdd:cd07346 160 RRRIRKASRE-VRESLAELsAFLQESLSGIRVVKAFAAEEREIERFRE-ANRDLRDANLrAARLSALFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 519 IVIFI--TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd07346 238 ALVLLygGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
286-551 |
3.71e-17 |
|
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: 83.46 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 286 LALGLLKLVGTMLGFSGPLLLSLLVG-FLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILY 364
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDvLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 365 CKALQLGPS---RPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLL--YQQVGVAFVGgLILALLLVPVNKV 439
Cdd:pfam00664 82 KKILRQPMSffdTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVmfYYGWKLTLVL-LAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 440 IATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGR-LRVIKYLDAACVYLWAALPVVIS 518
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAgIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 312176403 519 IVIFI-TYVLMGHQLTATKVFTALALVRMLILPL 551
Cdd:pfam00664 241 LALWFgAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
621-802 |
6.63e-17 |
|
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: 79.75 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlskgfglatQEPWIQFATIRDNILFgktfdaqlykeVLE 700
Cdd:cd03230 21 LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG---------KDIKKEPEEVKRRIGY-----------LPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 701 ACALNDDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS--YTTR 778
Cdd:cd03230 81 EPSLYENLT----------VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE--LLRELKkeGKTI 148
|
170 180
....*....|....*....|....*
gi 312176403 779 LLCTHRTEYLER-ADAVLLMEAGRL 802
Cdd:cd03230 149 LLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
621-812 |
7.16e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.03 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLA-------AIAGELhRLRGH----VAVRGLSKGFGLATQEPWIQFATIRDNILFGK- 688
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQlltrawdPQQGEI-LLNGQpiadYSEAALRQAISVVSQRVHLFSATLRDNLLLAAp 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 689 -TFDAQLyKEVLEACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhR 767
Cdd:PRK11160 440 nASDEAL-IEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIL-E 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 312176403 768 CILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK11160 517 LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
621-806 |
7.28e-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: 81.04 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL-----SKGFGLATQEPWIQF---ATIRDNIL------- 685
Cdd:cd03235 20 FEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekeRKRIGYVPQRRSIDRdfpISVRDVVLmglyghk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 686 -FGKTFDAQLYKEVLEAcalnddlsiLPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVD----AD 759
Cdd:cd03235 100 gLFRRLSKADKAKVDEA---------LERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDpktqED 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 312176403 760 VANHLLHRCILGMlsytTRLLCTH-RTEYLERADAVLLMeAGRLIRAG 806
Cdd:cd03235 171 IYELLRELRREGM----TILVVTHdLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1261-1467 |
7.47e-17 |
|
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: 81.33 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1261 NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ-LAIIPQ-EPFLFSG 1335
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRARhVGFVFQsFQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1336 TVREN------LDPQGLHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARALLTDAKILCIDEAT 1409
Cdd:COG4181 106 TALENvmlpleLAGRRDARARAR-ALLERVGLGHRLDHY----------PAQLSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 1410 ASVDQKT-----DQLLQQTickRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVElDSPATLR 1467
Cdd:COG4181 175 GNLDAATgeqiiDLLFELN---RERGTTLVLVTHDPALAARCDRVLRLRAGRLVE-DTAATAA 233
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
938-1221 |
1.01e-16 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 82.65 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 938 LLLFS-PGNLYIPV-FPLPKAAPngSSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTF 1015
Cdd:cd18559 11 NHVFSgPSNLWLLLwFDDPVNGP--QEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1016 FNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYhVQRHYRASSRELRRL 1095
Cdd:cd18559 89 FERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVP-VNRVYAASSRQLKRL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1096 GSLTLSPLYSHLADTLAGLSVLRATGATYRFeEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQ 1175
Cdd:cd18559 168 ESVSKDPRYKLFNETLLGISVIKAFEWEEAF-IRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRH 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 312176403 1176 QglaNPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEY 1221
Cdd:cd18559 247 S---LAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1255-1464 |
1.05e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.40 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1255 YRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTS--QLELAQLRSQLAIIPQE 1329
Cdd:PRK13637 12 YMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1330 P--FLFSGTVrenldpqglHKDRALwqALKQCHLSE------VITSMGGLDGELGEGG-RS---LSLGQRQLLCLARALL 1397
Cdd:PRK13637 92 PeyQLFEETI---------EKDIAF--GPINLGLSEeeienrVKRAMNIVGLDYEDYKdKSpfeLSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1398 TDAKILCIDEATASVDQKT-DQLLQQ--TICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPA 1464
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGrDEILNKikELHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1263-1458 |
1.72e-16 |
|
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: 79.52 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLF--RLLEPSSGRVLLDGVdtsQLELAQLRSQLAIIPQEPFLFSG-TVRE 1339
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILHPTlTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1340 nldpqglhkdrALWQALKqchlsevitsmggldgelgegGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 1419
Cdd:cd03213 102 -----------TLMFAAK---------------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 312176403 1420 LQQTIcKRFA--NKTVLTIAHRL-NTILNS-DRVLVLQAGRVV 1458
Cdd:cd03213 150 VMSLL-RRLAdtGRTIICSIHQPsSEIFELfDKLLLLSQGRVI 191
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1257-1459 |
2.09e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1257 PGLpNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTS-QLELAQLRSQLAIIPQE----PF 1331
Cdd:PRK11288 15 PGV-KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQElhlvPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1332 LfsgTVRENLD----PQ--GLHKDRAL-WQALKQC-HLSEVITSmggldgelGEGGRSLSLGQRQLLCLARALLTDAKIL 1403
Cdd:PRK11288 94 M---TVAENLYlgqlPHkgGIVNRRLLnYEAREQLeHLGVDIDP--------DTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1404 CIDEATASVDQK-TDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 1459
Cdd:PRK11288 163 AFDEPTSSLSAReIEQLFRVIRELRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
567-813 |
3.85e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 84.79 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 567 SLDRIQLFLDLPNHNPQAYYS--PdPPAEPST--------VLELHGALfswDPVGTSLETFISHLEVkkgmlVGIVGKVG 636
Cdd:PLN03130 1205 AVERVGTYIDLPSEAPLVIENnrP-PPGWPSSgsikfedvVLRYRPEL---PPVLHGLSFEISPSEK-----VGIVGRTG 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 637 CGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYkEVLEACALN 705
Cdd:PLN03130 1276 AGKSSMLNALFRIVELERGRILIDGcdiskfglmdLRKVLGIIPQAPVLFSGTVRFNLdPFNEHNDADLW-ESLERAHLK 1354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 706 DDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRT 785
Cdd:PLN03130 1355 DVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR-TDALIQKTIREEFKSCTMLIIAHRL 1433
|
250 260
....*....|....*....|....*...
gi 312176403 786 EYLERADAVLLMEAGRLIRAGPPSEILP 813
Cdd:PLN03130 1434 NTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
621-811 |
4.29e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.68 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------KGFGLATQEpwiqFA-----TIRDNILFG 687
Cdd:COG3842 26 LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtglppekRNVGMVFQD----YAlfphlTVAENVAFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 -------KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADV 760
Cdd:COG3842 102 lrmrgvpKAEIRARVAELLELVGLEGLADRYPH-----------QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 761 ANHL------LHRcILGmlsyTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:COG3842 171 REEMreelrrLQR-ELG----ITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
568-821 |
6.60e-16 |
|
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: 82.64 E-value: 6.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 568 LDRIQLFLDLPNHNPQAYYSPDPPAEPSTVLELHGALFSWDPVGTslETF-----IShLEVKKGMLVGIVGKVGCGKSSL 642
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGK--GGVravddVS-LTLRRGETLGLVGESGSGKSTL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 643 LAAIAGELHRLRGHVAVRG-------------LSKGFGLATQEPWIQF---ATIRDNI-----LFGKTFDAQLYK---EV 698
Cdd:COG1123 308 ARLLLGLLRPTSGSILFDGkdltklsrrslreLRRRVQMVFQDPYSSLnprMTVGDIIaeplrLHGLLSRAERRErvaEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 699 LEACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD----ADVANHLLHRCI-LGm 772
Cdd:COG1123 388 LERVGLPPDlADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDvsvqAQILNLLRDLQReLG- 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 773 LSYttrLLCTH---RTEYLerADAVLLMEAGRLIRAGPPSEIL--P-------LVQAVPKA 821
Cdd:COG1123 456 LTY---LFISHdlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFanPqhpytraLLAAVPSL 511
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
630-812 |
7.07e-16 |
|
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: 80.92 E-value: 7.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 630 GIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL-----SKGFGLAT---------QEPWIqFA--TIRDNILFG-----K 688
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsARGIFLPPhrrrigyvfQEARL-FPhlSVRGNLLYGrkrapR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 689 TFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrc 768
Cdd:COG4148 108 AERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 312176403 769 ILGMLSYTTR---LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG4148 175 YLERLRDELDipiLYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
620-806 |
7.62e-16 |
|
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: 77.09 E-value: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVavrglskgfglatqepwiqfatirdnILFGKTFDAQLYKEVL 699
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI--------------------------LLDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 700 EACAlnddlsILP-AGDQTEVG---EKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS 774
Cdd:cd03214 73 RKIA------YVPqALELLGLAhlaDRPFnELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE--LLRRLA 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 312176403 775 Y---TTRLLCTHrteYLERA----DAVLLMEAGRLIRAG 806
Cdd:cd03214 145 RergKTVVMVLH---DLNLAaryaDRVILLKDGRIVAQG 180
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1246-1458 |
1.01e-15 |
|
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: 77.71 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPglPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtSQLELAQlRSQLAI 1325
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAA-RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSG-TVRENL----DPQGLHKDRALWQA---LKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLARALL 1397
Cdd:cd03269 75 LPEERGLYPKmKVIDQLvylaQLKGLKKEEARRRIdewLERLELSE----------YANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 1398 TDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1458
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1246-1466 |
1.22e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.98 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAY-RPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLA 1324
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1325 IIPQEP-FLFSGTVREN-----LDPQGLHKDRALWQalkqchLSEVITSMGGLDGELGEGGRsLSLGQRQLLCLARALLT 1398
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDdvafgMENQGIPREEMIKR------VDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1399 DAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 1466
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1256-1470 |
1.28e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.85 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1256 RPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRS----QLAIIPQEPF 1331
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1332 LFSG-TVRENLD--------PQGLHKDRALwQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKI 1402
Cdd:PRK10070 117 LMPHmTVLDNTAfgmelagiNAEERREKAL-DALRQVGLENYAHSYPD----------ELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1403 LCIDEATASVDQKTDQLLQQTICKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:PRK10070 186 LLMDEAFSALDPLIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1246-1413 |
1.61e-15 |
|
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: 77.18 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQL 1323
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEPFLFSG-TVREN--LDP---QGLHKD----RALwQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLLCLA 1393
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENitLAPikvKGMSKAeaeeRAL-ELLEKVGLADKADAYP----------AQLSGGQQQRVAIA 147
|
170 180
....*....|....*....|
gi 312176403 1394 RALLTDAKILCIDEATASVD 1413
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALD 167
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
621-806 |
1.99e-15 |
|
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: 76.91 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL--------SKGFGLATQepwiQFA-----TIRDNILFG 687
Cdd:cd03301 21 LDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkDRDIAMVFQ----NYAlyphmTVYDNIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 ----KTFDAQLYKEVLEACALnddLSIlpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH 763
Cdd:cd03301 97 lklrKVPKDEIDERVREVAEL---LQI-----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 312176403 764 L------LHRcilgMLSYTTrLLCTH-RTEYLERADAVLLMEAGRLIRAG 806
Cdd:cd03301 169 MraelkrLQQ----RLGTTT-IYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
620-812 |
3.19e-15 |
|
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: 77.15 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGFGLAT--------QEPwiqFA------TIRDN 683
Cdd:COG1124 25 SLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpVTRRRRKAFrrrvqmvfQDP---YAslhprhTVDRI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 684 I-----LFGKTFDAQLYKEVLEACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:COG1124 102 LaeplrIHGLPDREERIAELLEQVGLPPSfLDRYPH-----------QLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 758 ADVANHLLHrcILGML---SYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1124 171 VSVQAEILN--LLKDLreeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1263-1464 |
3.26e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.50 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFL-FSGTVRE-- 1339
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1340 ---------NLDPQGLHKDRALWQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLARALLTDAKILCIDEATA 1410
Cdd:PRK09536 99 emgrtphrsRFDTWTETDRAAVERAMERTGVAQFADR----------PVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 1411 SVDQKtDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPA 1464
Cdd:PRK09536 169 SLDIN-HQVRTLELVRRLVDdgKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPA 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
621-801 |
3.68e-15 |
|
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: 74.92 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLskgfGLATQEPWIQfaTIRDNIlfGKTF-DAQLY--KE 697
Cdd:cd03229 21 LNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE----DLTDLEDELP--PLRRRI--GMVFqDFALFphLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 698 VLEACALnddlsilpagdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL--LHRCILGMLSY 775
Cdd:cd03229 93 VLENIAL--------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVraLLKSLQAQLGI 152
|
170 180
....*....|....*....|....*..
gi 312176403 776 TTrLLCTHRTEYLER-ADAVLLMEAGR 801
Cdd:cd03229 153 TV-VLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1266-1452 |
5.58e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.84 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1266 VTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL-DGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL--- 1341
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkys 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1342 ----------------------------------------------DPQGLHKDRALWQALKQCHLSEV---------IT 1366
Cdd:PTZ00265 484 lyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttDSNELIEMRKNYQTIKDSEVVDVskkvlihdfVS 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1367 SMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTI 1443
Cdd:PTZ00265 564 ALPDKYETLVGSNASkLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRLSTI 643
|
....*....
gi 312176403 1444 LNSDRVLVL 1452
Cdd:PTZ00265 644 RYANTIFVL 652
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1245-1455 |
5.85e-15 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 77.20 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1245 GVEFQDVVLAYRPGLPNaldgVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqlelaqlrsQLA 1324
Cdd:cd03291 39 NLFFSNLCLVGAPVLKN----INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1325 IIPQEPFLFSGTVRENLdPQGLHKDRALWQA-LKQCHLSEVITSMGGLDGELGEGGR-SLSLGQRQLLCLARALLTDAKI 1402
Cdd:cd03291 102 FSSQFSWIMPGTIKENI-IFGVSYDEYRYKSvVKACQLEEDITKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1403 LCIDEATASVDQKTD-QLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAG 1455
Cdd:cd03291 181 YLLDSPFGYLDVFTEkEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
621-811 |
7.15e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 77.81 E-value: 7.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGeLHRL-RGHVAV------------RGLSKGFglatQepwiQFA-----TIRD 682
Cdd:COG3839 24 LDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPtSGEILIggrdvtdlppkdRNIAMVF----Q----SYAlyphmTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 683 NILFG----KTFDAQLYKEVLEACALnddLSI------LPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDP 752
Cdd:COG3839 95 NIAFPlklrKVPKAEIDRRVREAAEL---LGLedlldrKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 753 LAAVDADVANHL------LHRcilgMLSYTTrLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:COG3839 161 LSNLDAKLRVEMraeikrLHR----RLGTTT-IYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
609-812 |
7.74e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.56 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 609 PVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKG-----------FGLATQEPWIQF 677
Cdd:PRK13644 12 PDGTPALENIN-LVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfsklqgirklVGIVFQNPETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 678 A--TIRDNILFGKTF----DAQLYKEVleacalndDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:PRK13644 91 VgrTVEEDLAFGPENlclpPIEIRKRV--------DRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 752 PLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1246-1466 |
9.78e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.94 E-value: 9.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1325
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEP---FLFSgTVREN----LDPQGLHKD---RALWQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLARA 1395
Cdd:PRK13648 88 VFQNPdnqFVGS-IVKYDvafgLENHAVPYDemhRRVSEALKQVDMLERADY----------EPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 1396 LLTDAKILCIDEATASVDQKTDQLLQQTICKRFANK--TVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 1466
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1262-1470 |
1.02e-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: 75.35 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAqlRSQLAIIPQEPFLFSG-TVREN 1340
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPHlTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 ----LDPQGLHKD---RALWQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD 1413
Cdd:cd03300 93 iafgLRLKKLPKAeikERVAEALDLVQLEGYANRK----------PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1414 QKTDQLLQQTIcKRFANK---TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:cd03300 163 LKLRKDMQLEL-KRLQKElgiTFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
621-812 |
1.35e-14 |
|
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: 75.06 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------KGFGLATQEpWIQFA--TIRDNILFG--- 687
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDitnlppekRDISYVPQN-YALFPhmTVYKNIAYGlkk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 -KTFDAQLYKEVLEacaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdvanhLLH 766
Cdd:cd03299 99 rKVDKKEIERKVLE---IAEMLGIDHLLNR-----KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV-----RTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312176403 767 RCILGMLSY------TTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03299 166 EKLREELKKirkefgVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
621-811 |
1.41e-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: 74.97 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------KGFGLATQepwiQFA-----TIRDNILFG 687
Cdd:cd03300 21 LDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpphkRPVNTVFQ----NYAlfphlTVFENIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 ----KTFDAQLYKEVLEACalndDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH 763
Cdd:cd03300 97 lrlkKLPKAEIKERVAEAL----DLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 764 L------LHRcILGMlsytTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:cd03300 169 MqlelkrLQK-ELGI----TFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
620-802 |
1.67e-14 |
|
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: 74.06 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV-----AVRGLSKG----------------FGLatqepwIQFA 678
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtDISKLSEKelaafrrrhigfvfqsFNL------LPDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 679 TIRDNILFGKTF-------DAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:cd03255 98 TALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 752 PLAAVDADVAnhllhRCILGML------SYTTRLLCTHRTEYLERADAVLLMEAGRL 802
Cdd:cd03255 167 PTGNLDSETG-----KEVMELLrelnkeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
620-802 |
1.72e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.10 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLL-------AAIAGELhrLRGHVAVRGLSKGFGLATQE----PWiqfATIRDNI---L 685
Cdd:PRK11247 32 DLHIPAGQFVAVVGRSGCGKSTLLrllagleTPSAGEL--LAGTAPLAEAREDTRLMFQDarllPW---KKVIDNVglgL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 686 FGKTFDAQLykEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdvanhlL 765
Cdd:PRK11247 107 KGQWRDAAL--QALAAVGLADRANEWPA-----------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDA------L 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 312176403 766 HRCILGMLSYT-------TRLLCTHR-TEYLERADAVLLMEAGRL 802
Cdd:PRK11247 168 TRIEMQDLIESlwqqhgfTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1270-1458 |
1.83e-14 |
|
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: 74.07 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1270 VQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAqlRSQLAIIPQEPFLFSG-TVRENLD---PQG 1345
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGlglSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1346 LHKDRALWQALkqchlsEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQ--- 1422
Cdd:cd03298 99 LKLTAEDRQAI------EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDlvl 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 312176403 1423 TICKRFANkTVLTIAHRLNTILN-SDRVLVLQAGRVV 1458
Cdd:cd03298 173 DLHAETKM-TVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
959-1191 |
3.09e-14 |
|
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: 74.60 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 959 NGSSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDS 1038
Cdd:pfam00664 35 PETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1039 LPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLR 1118
Cdd:pfam00664 115 LGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 1119 ATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYA 1191
Cdd:pfam00664 195 AFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
621-806 |
3.44e-14 |
|
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: 73.46 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH---RLRGHVAVRG--LSKG-----FGLATQ-EPWIQFATIRDNILFGKT 689
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGqpRKPDqfqkcVAYVRQdDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 690 F-----DAQLYKEVLEACALNDDLSILPAGDQTEVGekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL 764
Cdd:cd03234 108 LrlprkSSDAIRKKRVEDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 312176403 765 LHrcILGMLSYTTRL-LCT-H--RTEYLERADAVLLMEAGRLIRAG 806
Cdd:cd03234 183 VS--TLSQLARRNRIvILTiHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1262-1471 |
4.32e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.92 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSS----------LllvlfrllEPS---SGRVLLDGVD--TSQLELAQLRSQLAII 1326
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTllrclnrmndL--------IPGarvEGEILLDGEDiyDPDVDVVELRRRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1327 PQEPFLFSGTVREN----LDPQGLHKDRAL----WQALKQCHL-SEVitsmggldgelgeGGR------SLSLGQRQLLC 1391
Cdd:COG1117 98 FQKPNPFPKSIYDNvaygLRLHGIKSKSELdeivEESLRKAALwDEV-------------KDRlkksalGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1392 LARALLTDAKILCIDEATASVD----QKTDQLLQQtICKRFankTVLTIAH------RLntilnSDRVLVLQAGRVVELD 1461
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDpistAKIEELILE-LKKDY---TIVIVTHnmqqaaRV-----SDYTAFFYLGELVEFG 235
|
250
....*....|
gi 312176403 1462 SPATLRNQPH 1471
Cdd:COG1117 236 PTEQIFTNPK 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1262-1458 |
4.35e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQL--AIIPQEPFLFSG-TVR 1338
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLgiGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1339 ENLdPQGLHKDRAL-------WQALKQchLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATAS 1411
Cdd:PRK09700 99 ENL-YIGRHLTKKVcgvniidWREMRV--RAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 312176403 1412 VDQK-TDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1458
Cdd:PRK09700 176 LTNKeVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
621-803 |
5.12e-14 |
|
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: 72.92 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------------LSKGFGLATQEPwiqFA------TIR 681
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkiRRKEIQMVFQDP---MSslnprmTIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 682 DNI-----LFGKTFDAQLYKEV--LEACALNDDLSIL---PAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:cd03257 103 EQIaeplrIHGKLSKKEARKEAvlLLLVGVGLPEEVLnryPH-----------ELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 752 PLAAVDADVANHLLH--RCI---LGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLI 803
Cdd:cd03257 172 PTSALDVSVQAQILDllKKLqeeLGL----TLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1262-1458 |
5.82e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqlELAQLRS-QLAI------IPQEPFLFS 1334
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG------KPVRIRSpRDAIalgigmVHQHFMLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1335 G-TVRENL-----DPQGLHKDR-ALWQALKQchLSE-----------VitsmggldgelgeggRSLSLGQRQLLCLARAL 1396
Cdd:COG3845 94 NlTVAENIvlglePTKGGRLDRkAARARIRE--LSErygldvdpdakV---------------EDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 1397 LTDAKILCIDEATAsV--DQKTDQLLQqtICKRFAN--KTVLTIAHRLNTIL-NSDRVLVLQAGRVV 1458
Cdd:COG3845 157 YRGARILILDEPTA-VltPQEADELFE--ILRRLAAegKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
621-812 |
7.40e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.81 E-value: 7.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----LSKGFGLATQepwiqfATIRDNILFGktfdAQLY 695
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsalLELGAGFHPE------LTGRENIYLN----GRLL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 696 -------KEVLEACAlnddlsilpagDQTEVGE------KgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdvan 762
Cdd:COG1134 117 glsrkeiDEKFDEIV-----------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA---- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 763 HLLHRCILGMLSY----TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1134 180 AFQKKCLARIRELresgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1267-1466 |
7.99e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.48 E-value: 7.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1267 TFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlRSqLAIIPQEPFLFSG-TVRENLDpQG 1345
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP-VSMLFQENNLFPHlTVAQNIG-LG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1346 LHKD--------RALWQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLLCLARALLTDAKILCIDEATASVD---- 1413
Cdd:COG3840 96 LRPGlkltaeqrAQVEQALERVGLAGLLDRLP----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1414 QKTDQLLQQtICKRFANkTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 1466
Cdd:COG3840 166 QEMLDLVDE-LCRERGL-TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1246-1439 |
9.74e-14 |
|
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: 70.65 E-value: 9.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPNaLDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqlelaqlRSQLAI 1325
Cdd:cd03223 1 IELENLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSGTVRENLdpqglhkdRALWQalkqchlsevitsmggldgelgeggRSLSLGQRQLLCLARALLTDAKILCI 1405
Cdd:cd03223 69 LPQRPYLPLGTLREQL--------IYPWD-------------------------DVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....
gi 312176403 1406 DEATASVDQKTDQLLQQTICKRFAnkTVLTIAHR 1439
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1245-1470 |
1.13e-13 |
|
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: 72.37 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1245 GVEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRsQLA 1324
Cdd:cd03296 2 SIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-VQER-NVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1325 IIPQEPFLFSG-TVRENL-----------DPQGLHKDRALWQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCL 1392
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPA----------QLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1393 ARALLTDAKILCIDEATASVDQKTDQLLQQTIcKRFANKTVLT---IAHRLNTILN-SDRVLVLQAGRVVELDSPATLRN 1468
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTtvfVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
|
..
gi 312176403 1469 QP 1470
Cdd:cd03296 227 HP 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
621-811 |
1.15e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.35 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGfGLATQEPWIQFA----------TIRDNILFGKTF 690
Cdd:PRK10851 23 LDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-RLHARDRKVGFVfqhyalfrhmTVFDNIAFGLTV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 691 --------DAQLYKEV---LEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:PRK10851 102 lprrerpnAAAIKAKVtqlLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 760 VANHL------LHRcilgMLSYTTrLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK10851 171 VRKELrrwlrqLHE----ELKFTS-VFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
620-812 |
1.27e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFA-TIRDNILFGK 688
Cdd:PRK09536 23 DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraASRRVASVPQDTSLSFEfDVRQVVEMGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 689 TFDAQLYKEVLEAcalnDDLSILPAGDQTEV---GEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDadvANHL 764
Cdd:PRK09536 103 TPHRSRFDTWTET----DRAAVERAMERTGVaqfADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLD---INHQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 765 LHrcilgMLSYTTRLLCTHRTEY-----LERA----DAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK09536 176 VR-----TLELVRRLVDDGKTAVaaihdLDLAarycDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
561-812 |
1.41e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.52 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 561 LLEAKVSLDRIQLFLDlpnhNPQAYYSPDPPAEPSTVLELHGALFSWDPvGTSLETFIShLEVKKGMLVGIVGKVGCGKS 640
Cdd:PRK10790 308 LQQAVVAGERVFELMD----GPRQQYGNDDRPLQSGRIDIDNVSFAYRD-DNLVLQNIN-LSVPSRGFVALVGHTGSGKS 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 641 SLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSI 710
Cdd:PRK10790 382 TLASLLMGYYPLTEGEIRLDGrplsslshsvLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARS 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 711 LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRTEYLER 790
Cdd:PRK10790 462 LPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG-TEQAIQQALAAVREHTTLVVIAHRLSTIVE 540
|
250 260
....*....|....*....|..
gi 312176403 791 ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK10790 541 ADTILVLHRGQAVEQGTHQQLL 562
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1246-1469 |
1.41e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.89 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVD----TSQLELAQ 1318
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1319 LRSQLAIIPQ--EPFLFSGTV-RENL-DPQGLH------KDRAlWQALKQCHLSEVITSMGGLdgelgeggrSLSLGQRQ 1388
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVeREIIfGPKNFKmnldevKNYA-HRLLMDLGFSRDVMSQSPF---------QMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1389 LLCLARALLTDAKILCIDEATASVDQKT-DQLLqqTICKRFA---NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1463
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSkRQVM--RLLKSLQtdeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSP 230
|
....*.
gi 312176403 1464 ATLRNQ 1469
Cdd:PRK13646 231 KELFKD 236
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
612-812 |
1.48e-13 |
|
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: 72.25 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 612 TSLETFISHLE--VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFAT 679
Cdd:cd03288 31 NNLKPVLKHVKayIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtLRSRLSIILQDPILFSGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 680 IRDNI-LFGKTFDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:cd03288 111 IRFNLdPECKCTDDRLW-EALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 759 DVANhLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03288 190 ATEN-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
621-812 |
1.68e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.06 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSllaaIAGELHR----------LRGH----VAVRGLSKGFGLATQEPWIQFATIRDNILF 686
Cdd:PRK11176 364 FKIPAGKTVALVGRSGSGKST----IANLLTRfydidegeilLDGHdlrdYTLASLRNQVALVSQNVHLFNDTIANNIAY 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 ---GKTFDAQLYKEVLEACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANH 763
Cdd:PRK11176 440 artEQYSREQIEEAARMAYAM-DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE-SER 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 312176403 764 LLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK11176 518 AIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
659-824 |
1.94e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.84 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 659 VRGLSKGFGLATQEPWIQFATIRDNILFGKTfDAQLyKEVLEAC---ALNDDLSILPAGDQTEVGEKGVTLSGGQRARIA 735
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATR-EDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 736 LARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCT--HRTEYLERADAVLLM----EAGRLIRA-GPP 808
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITiaHRIASIKRSDKIVVFnnpdRTGSFVQAhGTH 1447
|
170
....*....|....*.
gi 312176403 809 SEILPLVQAVPKAWAE 824
Cdd:PTZ00265 1448 EELLSVQDGVYKKYVK 1463
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1246-1463 |
2.10e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.43 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPN----ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLE-LAQLR 1320
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1321 SQLAIIPQEP--FLFSGTVR-------ENLDPQGLHKDRALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLC 1391
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEedvafgpENLGIPPEEIRERVDESLKKVGMYEY----------RRHAPHLLSGGQKQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1392 LARALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 1463
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
621-811 |
2.34e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 73.72 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEP----WIQFA-----TIRDNILFGKTFD 691
Cdd:PRK11607 40 LTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPinmmFQSYAlfphmTVEQNIAFGLKQD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 692 AQLYKEVleACALNDDLSILPAgdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRC--I 769
Cdd:PRK11607 120 KLPKAEI--ASRVNEMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVvdI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 312176403 770 LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11607 196 LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1246-1458 |
2.95e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.80 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQL 1323
Cdd:PRK13636 6 LKVEELNYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEP--FLFSGTVRENLD----PQGLHKD---RALWQALKQC---HLSEVITsmggldgelgeggRSLSLGQRQLLC 1391
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSfgavNLKLPEDevrKRVDNALKRTgieHLKDKPT-------------HCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 1392 LARALLTDAKILCIDEATASVDQK-TDQLLQqtICKRFANKTVLTI---AHRLNTI-LNSDRVLVLQAGRVV 1458
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMgVSEIMK--LLVEMQKELGLTIiiaTHDIDIVpLYCDNVFVMKEGRVI 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
621-812 |
3.08e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.94 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfgLATQEPW-------IQ----FA--TIRDNILFG 687
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD----LTALPPAerpvsmlFQennlFPhlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 -------KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD--- 757
Cdd:COG3840 96 lrpglklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpal 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 758 ----ADVANHLLHRciLGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG3840 165 rqemLDLVDELCRE--RGL----TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
591-811 |
3.21e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 591 PAEPSTVLELHGALFSWDpvGTsleTFISH--LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGL 668
Cdd:PRK09452 8 PSSLSPLVELRGISKSFD--GK---EVISNldLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 669 ATQEP----WIQFA-----TIRDNILFG----KTFDAQLYKEVLEACALN--DDLSilpagdqtevGEKGVTLSGGQRAR 733
Cdd:PRK09452 83 AENRHvntvFQSYAlfphmTVFENVAFGlrmqKTPAAEITPRVMEALRMVqlEEFA----------QRKPHQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 734 IALARAVYQEKELYLLDDPLAAVDA----DVANHL--LHRcILGMlsytTRLLCTH-RTEYLERADAVLLMEAGRLIRAG 806
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYklrkQMQNELkaLQR-KLGI----TFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
....*
gi 312176403 807 PPSEI 811
Cdd:PRK09452 228 TPREI 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1246-1466 |
4.60e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLA 1324
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1325 IIPQEPFLFSG-TVRENLDPQGLHKDRALWQAlkqcHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKIL 1403
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERDQFQE----RIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 1404 CIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 1466
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQlREQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
621-817 |
4.90e-13 |
|
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: 70.39 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------------LSKGFGLATQEPwiqfA-----TIRD 682
Cdd:COG1127 26 LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyeLRRRIGMLFQGG----AlfdslTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 683 NILFG----KTFD----AQLYKEVLEACALNDDLSILPAgdqtevgEkgvtLSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:COG1127 102 NVAFPlrehTDLSeaeiRELVLEKLELVGLPGAADKMPS-------E----LSGGMRKRVALARALALDPEILLYDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 755 AVD---ADVANHLLHRC--ILGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL----PLVQA 817
Cdd:COG1127 171 GLDpitSAVIDELIRELrdELGL----TSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLasddPWVRQ 239
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1245-1466 |
5.06e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 71.31 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1245 GVEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVD-TSQ---LELA 1317
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTsknKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1318 QLRSQLAIIPQ--EPFLFSGTVRENL--DPQ--GLHKDRALWQALKQCHLSEVITSMGGLDGElgeggrSLSLGQRQLLC 1391
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVafGPQnfGVSQEEAEALAREKLALVGISESLFEKNPF------ELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1392 LARALLTDAKILCIDEATASVDQKTDQLLqQTICKRF--ANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 1466
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKEL-MTLFKKLhqSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1246-1469 |
5.14e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1325
Cdd:PRK13647 5 IEVEDLHFRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEP--FLFSGTVRENL--DPQ--GLHKD---RALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARAL 1396
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVafGPVnmGLDKDeveRRVEEALKAVRMWDF----------RDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1397 LTDAKILCIDEATASVDQKTDQLLqQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETL-MEILDRLHNqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1263-1458 |
5.52e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRsQLAI--IPQEPFLFSG-TVRE 1339
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAH-QLGIylVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1340 NL------DPQGLHKDRALWQALkQCHLSevitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD 1413
Cdd:PRK15439 106 NIlfglpkRQASMQKMKQLLAAL-GCQLD------------LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 312176403 1414 Q-KTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1458
Cdd:PRK15439 173 PaETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
621-811 |
5.87e-13 |
|
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: 70.29 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAG----------------------ELHRLRGHVAVrgLSKGFGLatqepwIQFA 678
Cdd:cd03256 22 LSINPGEFVALIGPSGAGKSTLLRCLNGlveptsgsvlidgtdinklkgkALRQLRRQIGM--IFQQFNL------IERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 679 TIRDNILFG--------KTFDAQLYK-EVLEACALNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLL 749
Cdd:cd03256 94 SVLENVLSGrlgrrstwRSLFGLFPKeEKQRALAALERVGLLDKAYQ-----RADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 750 DDPLAAVDADVAN---HLLHRciLGMLSYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEI 811
Cdd:cd03256 169 DEPVASLDPASSRqvmDLLKR--INREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
621-821 |
5.90e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.30 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV--------------RGLSKGFGLATQEPWIQF--ATIRDNI 684
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkeiKPVRKKVGVVFQFPESQLfeETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 685 LFGKTfDAQLYKEVLEACALnDDLSILpaGDQTEVGEKG-VTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH 763
Cdd:PRK13643 107 AFGPQ-NFGIPKEKAEKIAA-EKLEMV--GLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 764 LLHRCILGMLSYTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEILPLVQ-------AVPKA 821
Cdd:PRK13643 183 MMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDflkahelGVPKA 248
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
626-802 |
8.77e-13 |
|
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: 70.27 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 626 GMLVGIVGKVGCGKSSLLAAIAgELHRLRGHVAVRGLS----------KGFGLATQEPWIQFATIRDNI-LFGKTFDAQL 694
Cdd:cd03289 30 GQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSwnsvplqkwrKAFGVIPQKVFIFSGTFRKNLdPYGKWSDEEI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 695 YKeVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLS 774
Cdd:cd03289 109 WK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFA 186
|
170 180
....*....|....*....|....*...
gi 312176403 775 YTTRLLCTHRTEYLERADAVLLMEAGRL 802
Cdd:cd03289 187 DCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1255-1470 |
8.82e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.20 E-value: 8.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1255 YRPGL-----PNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtSQLELA--QLRSQ-LAII 1326
Cdd:PRK15112 16 YRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHFGdySYRSQrIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1327 PQEPF-----------LFSGTVRENLDPQGLHKDRALWQALKQCHLsevitsmggLDGELGEGGRSLSLGQRQLLCLARA 1395
Cdd:PRK15112 93 FQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGL---------LPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1396 LLTDAKILCIDEATASVD-----QKTDQLLQ----QTICKRFANKTVLTIAHRlntilnSDRVLVLQAGRVVELDSPATL 1466
Cdd:PRK15112 164 LILRPKVIIADEALASLDmsmrsQLINLMLElqekQGISYIYVTQHLGMMKHI------SDQVLVMHQGEVVERGSTADV 237
|
....
gi 312176403 1467 RNQP 1470
Cdd:PRK15112 238 LASP 241
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1246-1455 |
1.05e-12 |
|
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: 68.90 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPNaLDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ--- 1322
Cdd:cd03290 1 VQVTNGYFSWGSGLAT-LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnry 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1323 -LAIIPQEPFLFSGTVRENL---DPQGLHKDRALWQAlkqCHLSEVItSMGGLDGELGEGGRSLSL--GQRQLLCLARAL 1396
Cdd:cd03290 80 sVAYAAQKPWLLNATVEENItfgSPFNKQRYKAVTDA---CSLQPDI-DLLPFGDQTEIGERGINLsgGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 1397 LTDAKILCIDEATASVD-QKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQAG 1455
Cdd:cd03290 156 YQNTNIVFLDDPFSALDiHLSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
621-806 |
1.17e-12 |
|
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: 68.67 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPwiQFATIRDNILFgktfdAQLYKEVLE 700
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENNLF-----AHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 701 ACALNDDLSiLPAGDQTEV----GEKGV---------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhR 767
Cdd:cd03298 92 GLGLSPGLK-LTAEDRQAIevalARVGLaglekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML-D 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 312176403 768 CILGMLSYT--TRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:cd03298 170 LVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
620-759 |
1.19e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 68.66 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELH---RLRGHVAVRG--------LSKGFGLATQEPWIqFA--TIRDNILF 686
Cdd:COG4136 21 SLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGrrltalpaEQRRIGILFQDDLL-FPhlSVGENLAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 G--KTFDAQLYKEVLEAcALnddlsilpagdqTEVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:COG4136 100 AlpPTIGRAQRRARVEQ-AL------------EEAGLAGFadrdpaTLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
.
gi 312176403 759 D 759
Cdd:COG4136 167 A 167
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
621-806 |
1.36e-12 |
|
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: 68.71 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------LSKGFGLAtqepwiqfATIRDNILFG------ 687
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvssllgLGGGFNPE--------LTGRENIYLNgrllgl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 -KTFDAQLYKEVLEACALNDDLSiLPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdvanHLLH 766
Cdd:cd03220 115 sRKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDA----AFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 312176403 767 RC---ILGMLS-YTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:cd03220 180 KCqrrLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1263-1463 |
1.92e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.89 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSG-TVREnL 1341
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRE-L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1342 DPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGR--SLSLGQRQLLCLARALLTDAKILCIDEATASVD------ 1413
Cdd:PRK11231 97 VAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRltDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDinhqve 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 312176403 1414 -QKTDQLLQQtickrfANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1463
Cdd:PRK11231 177 lMRLMRELNT------QGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTP 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
621-796 |
2.60e-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: 67.50 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPWIQFA----------TIRDNILF---- 686
Cdd:COG4133 23 FTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLghadglkpelTVRENLRFwaal 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 -GKTFDAQLYKEVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLL 765
Cdd:COG4133 103 yGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-GVALL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 312176403 766 HRCIL------GMLsyttrLLCTHRTEYLERADAVLL 796
Cdd:COG4133 171 AELIAahlargGAV-----LLTTHQPLELAAARVLDL 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1225-1470 |
2.79e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.27 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1225 LPQEPQGQPLQLGTGWLTQGGVEFQDVVLAYRPGL-------PNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLL 1297
Cdd:PRK15134 257 LNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKGIlkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1298 ePSSGRVLLDGVDTSQLELAQL---RSQLAIIPQEPFlfsgtvrENLDPQgLHKDRALWQALK--QCHLS------EVIT 1366
Cdd:PRK15134 337 -NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN-------SSLNPR-LNVLQIIEEGLRvhQPTLSaaqreqQVIA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1367 SMGGLDGELGEGGR---SLSLGQRQLLCLARALLTDAKILCIDEATASVDqKTDQLLQQTICKRFANKTVLT---IAHRL 1440
Cdd:PRK15134 408 VMEEVGLDPETRHRypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAQILALLKSLQQKHQLAylfISHDL 486
|
250 260 270
....*....|....*....|....*....|.
gi 312176403 1441 NTILN-SDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:PRK15134 487 HVVRAlCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1250-1457 |
3.63e-12 |
|
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: 66.30 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1250 DVVLAYRP-GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ-LAIIP 1327
Cdd:cd03215 2 EPVLEVRGlSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1328 QEPF---LFSG-TVRENLdpqglhkdralwqalkqchlseVITSMggldgelgeggrsLSLGQRQLLCLARALLTDAKIL 1403
Cdd:cd03215 82 EDRKregLVLDlSVAENI----------------------ALSSL-------------LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 1404 CIDEATASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRV 1457
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLI-RELAdaGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1257-1470 |
3.82e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.22 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1257 PGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDT---SQLELAQLRSQLAIIPQEPF-- 1331
Cdd:PRK11308 25 ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPYgs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1332 --------------LFSGT----------VRENLDPQGL---HKDRalwqalkQCHLsevitsmggldgelgeggrsLSL 1384
Cdd:PRK11308 105 lnprkkvgqileepLLINTslsaaerrekALAMMAKVGLrpeHYDR-------YPHM--------------------FSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1385 GQRQLLCLARALLTDAKILCIDEATASVD-----QKTDQL--LQQTIckrfaNKTVLTIAHRLNTILN-SDRVLVLQAGR 1456
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDvsvqaQVLNLMmdLQQEL-----GLSYVFISHDLSVVEHiADEVMVMYLGR 232
|
250
....*....|....
gi 312176403 1457 VVELDSPATLRNQP 1470
Cdd:PRK11308 233 CVEKGTKEQIFNNP 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1258-1464 |
4.51e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.60 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1258 GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL----DGVDTSQ---LELAQLRSQLAIIPQEP 1330
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKpgpDGRGRAKRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1331 FLFS-GTVRENLD-------PQGLHKDRALWqALKQCHLSEvitsmGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKI 1402
Cdd:TIGR03269 375 DLYPhRTVLDNLTeaiglelPDELARMKAVI-TLKMVGFDE-----EKAEEILDKYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 1403 LCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPA 1464
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKarEEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPE 513
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1253-1467 |
5.05e-12 |
|
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: 67.01 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1253 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlELAQLRSQLAIIPQEPFL 1332
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1333 FSG-TVRENLDPQG--------LHKDRALwQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKIL 1403
Cdd:cd03265 85 DDElTGWENLYIHArlygvpgaERRERID-ELLDFVGLLEA----------ADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1404 CIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTI-LNSDRVLVLQAGRVVELDSPATLR 1467
Cdd:cd03265 154 FLDEPTIGLDPQTrAHVWEyiEKLKEEF-GMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
620-812 |
5.63e-12 |
|
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: 67.22 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAG--------------ELHRLRGHvAVRGLSKGFGLATQepwiQF-----ATI 680
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCINGlerptsgsvlvdgtDLTLLSGK-ELRKARRRIGMIFQ----HFnllssRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 681 RDNILF-------GKTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:cd03258 100 FENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 754 AAVDADVAnhllhRCILGMLSYTTR------LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03258 169 SALDPETT-----QSILALLRDINRelgltiVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
621-812 |
6.37e-12 |
|
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: 67.42 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH-----------RLRGHVAVRGLSKGFGLAT---QEPWIQFATIRDNILF 686
Cdd:COG1119 24 WTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygndvrlfgERRGGEDVWELRKRIGLVSpalQLRFPRDETVLDVVLS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 GKtFDA-QLYKEVLE-----ACALNDDLSILPAGDQTeVGekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDaDV 760
Cdd:COG1119 104 GF-FDSiGLYREPTDeqrerARELLELLGLAHLADRP-FG----TLSQGEQRRVLIARALVKDPELLILDEPTAGLD-LG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 761 ANHLLHRCI--LGMLSYTTRLLCTHRTEYLERA-DAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1119 177 ARELLLALLdkLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1263-1458 |
9.09e-12 |
|
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: 66.53 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDGvdtSQLELAQLRSQLAIIPQEPFLFSG-TVR 1338
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1339 ENL-----------DPQGLHKDRALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKILCIDE 1407
Cdd:cd03234 100 ETLtytailrlprkSSDAIRKKRVEDVLLRDLALTRI----------GGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1408 ATASVDQKTDQLLQQT---ICKRfaNKTVLTIAHRLNTILNS--DRVLVLQAGRVV 1458
Cdd:cd03234 170 PTSGLDSFTALNLVSTlsqLARR--NRIVILTIHQPRSDLFRlfDRILLLSSGEIV 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
597-812 |
9.45e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 9.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 597 VLELHGALFSWDPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGF 666
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 667 GLATQEPWIQF--ATIRDNILFGKTFDAQLYKEVLEACalndDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEK 744
Cdd:PRK13642 84 GMVFQNPDNQFvgATVEDDVAFGMENQGIPREEMIKRV----DEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 745 ELYLLDDPLAAVDADVANHLLhRCILGMLS--YTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIM-RVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
621-804 |
1.59e-11 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 65.84 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSK-----------GFGLatqepwIQFAT 679
Cdd:COG1136 29 LSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslsereLARlrrrhigfvfqFFNL------LPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 680 IRDNILF-------GKTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDP 752
Cdd:COG1136 103 ALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 753 LAAVDADVANH---LLHRCI--LGmlsyTTRLLCTHRTEYLERADAVLLMEAGRLIR 804
Cdd:COG1136 172 TGNLDSKTGEEvleLLRELNreLG----TTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
621-812 |
1.69e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.88 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAI-------AGEL-----HRLRGHVAVRGLSKGFGLATQepwiQF-----ATIRDN 683
Cdd:PRK09493 22 LNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLivdglKVNDPKVDERLIRQEAGMVFQ----QFylfphLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 684 ILFG-------KTFDA-QLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK09493 98 VMFGplrvrgaSKEEAeKQARELLAKVGLAERAHHYPS-----------ELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 756 VDADvanhLLHRCILGMLSYT----TRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK09493 167 LDPE----LRHEVLKVMQDLAeegmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1263-1459 |
1.96e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.25 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRS-----QL-------AIIPQEp 1330
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiQMvfqdsisAVNPRK- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1331 flfsgTVRENLDPQGLHKDRaLWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATA 1410
Cdd:PRK10419 107 -----TVREIIREPLRHLLS-LDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1411 SVD-----QKTDQL--LQQ---TICkrfanktvLTIAHRLNTILN-SDRVLVLQAGRVVE 1459
Cdd:PRK10419 181 NLDlvlqaGVIRLLkkLQQqfgTAC--------LFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1262-1470 |
2.04e-11 |
|
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: 68.56 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKS----SLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLR----SQLAIIPQEPfLF 1333
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEP-MT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1334 SgtvrenLDP---------------QGLHKD----RALwQALKQCHLSEVITSMggldgelgeggRS----LSLGQRQLL 1390
Cdd:COG4172 104 S------LNPlhtigkqiaevlrlhRGLSGAaaraRAL-ELLERVGIPDPERRL-----------DAyphqLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1391 CLARALLTDAKILCIDEATASVD---QKtdQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPA 1464
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDvtvQA--QILDllKDLQREL-GMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTA 242
|
....*.
gi 312176403 1465 TLRNQP 1470
Cdd:COG4172 243 ELFAAP 248
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1206-1468 |
2.90e-11 |
|
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: 68.89 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1206 TQTEAMLVSVERLEEYTCDlPQEPQGQPLQLGT----GWLTqgGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGR 1281
Cdd:TIGR01257 888 TREERALEKTEPLTEEMED-PEHPEGINDSFFErelpGLVP--GVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1282 TGSGKSSLLLVLFRLLEPSSGRVLLDGVDTsQLELAQLRSQLAIIPQEPFLFSG-TVRENLDPQGLHKDRALWQAlkQCH 1360
Cdd:TIGR01257 965 NGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQLKGRSWEEA--QLE 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1361 LsEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRL 1440
Cdd:TIGR01257 1042 M-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM 1120
|
250 260
....*....|....*....|....*....
gi 312176403 1441 NTI-LNSDRVLVLQAGRVVELDSPATLRN 1468
Cdd:TIGR01257 1121 DEAdLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
621-764 |
3.04e-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: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVR-GLSKGFgLAtQEPwiQF---ATIRDNILFGKTFDAQLYK 696
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGY-LP-QEP--PLdddLTVLDTVLDGDAELRALEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 697 EVLEACALNDDLSILP---AGDQTEVGEKGV--------------------------TLSGGQRARIALARAVYQEKELY 747
Cdd:COG0488 95 ELEELEAKLAEPDEDLerlAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEPDLL 174
|
170
....*....|....*..
gi 312176403 748 LLDDPlaavdadvANHL 764
Cdd:COG0488 175 LLDEP--------TNHL 183
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1261-1470 |
3.15e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.17 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1261 NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlrSQLAIIPQEPFLFSG-TVRE 1339
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1340 NLdPQGLHKDRalwqaLKQCHLSEVITSMGGLDGELGEGGR---SLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 1416
Cdd:PRK11607 111 NI-AFGLKQDK-----LPKAEIASRVNEMLGLVHMQEFAKRkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 1417 DQLLQQT---ICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:PRK11607 185 RDRMQLEvvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
621-810 |
3.25e-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: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----LSKG--------FGLATQEpwiqFA-----TIRD 682
Cdd:COG2884 23 LEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrLKRReipylrrrIGVVFQD----FRllpdrTVYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 683 NILF-----GKTfDAQLYKEVLEACALnddlsilpagdqteVG--EKG----VTLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:COG2884 99 NVALplrvtGKS-RKEIRRRVREVLDL--------------VGlsDKAkalpHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176403 752 PLAAVDADVAN---HLLHR-CILGmlsyTTRLLCTHRTEYLERADA-VLLMEAGRLIRAGPPSE 810
Cdd:COG2884 164 PTGNLDPETSWeimELLEEiNRRG----TTVLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
621-812 |
3.27e-11 |
|
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: 65.74 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL--------------SKGFGLATQepwiQFA-----TIR 681
Cdd:cd03294 45 LDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelrelrRKKISMVFQ----SFAllphrTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 682 DNILFG-------KTFDAQLYKEVLEACALNDDLSILPagDQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:cd03294 121 ENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYP--DE---------LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 755 AVD----ADVANHLLHrcILGMLSYTTrLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03294 190 ALDplirREMQDELLR--LQAELQKTI-VFITHDlDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
621-811 |
3.42e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.84 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG------------LSKGFGLATQEPWIQF--ATIRDNILF 686
Cdd:PRK13637 28 IEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdIRKKVGLVFQYPEYQLfeETIEKDIAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 GKT----FDAQLYKEVLEACALnddlsilpAG-DQTEVGEKG-VTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA-- 758
Cdd:PRK13637 108 GPInlglSEEEIENRVKRAMNI--------VGlDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkg 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 759 --DVANHL--LHRcilgmlSYT-TRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13637 180 rdEILNKIkeLHK------EYNmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
611-811 |
3.49e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.01 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 611 GTSLETF----IShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--------------LSKGFGLATQE 672
Cdd:PRK13641 15 GTPMEKKgldnIS-FELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkkLRKKVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 673 PWIQF--ATIRDNILFG-KTFDAQlykevlEACALNDDLS-ILPAGDQTEVGEKG-VTLSGGQRARIALARAVYQEKELY 747
Cdd:PRK13641 94 PEAQLfeNTVLKDVEFGpKNFGFS------EDEAKEKALKwLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 748 LLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1262-1460 |
3.85e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.27 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL---RSQLAIIPQEPfLFSGTVR 1338
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP-LASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1339 ENL-----DPQGLHKDRALWQALKQchlsEVITSMGGLDGELGEGGR---SLSLGQRQLLCLARALLTDAKILCIDEATA 1410
Cdd:PRK15079 115 MTIgeiiaEPLRTYHPKLSRQEVKD----RVKAMMLKVGLLPNLINRyphEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 1411 SVD----QKTDQLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVEL 1460
Cdd:PRK15079 191 ALDvsiqAQVVNLLQQL--QREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVEL 243
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1246-1466 |
4.09e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.39 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDT-SQLELAqlRSQLA 1324
Cdd:PRK13536 42 IDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1325 IIPQEPFL-FSGTVRENLDPQGLhkdralWQALKQCHLSEVITSM---GGLDGELGEGGRSLSLGQRQLLCLARALLTDA 1400
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLVFGR------YFGMSTREIEAVIPSLlefARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 1401 KILCIDEATASVDQKTDQLLQQTICKRFA-NKTVLTIAH------RLntilnSDRVLVLQAGRVVELDSPATL 1466
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
615-811 |
4.15e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.59 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 615 ETFIS---HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--------LSKGFGLATQE----PWIQFAt 679
Cdd:PRK11000 15 DVVISkdiNLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvppAERGVGMVFQSyalyPHLSVA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 680 irDNILFG----KTFDAQLYKEVLEACAlnddlsILPAGDQTEVGEKgvTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK11000 94 --ENMSFGlklaGAKKEEINQRVNQVAE------VLQLAHLLDRKPK--ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 756 VDADVANHL------LHRcilgmlsyttRLLC-----TH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11000 164 LDAALRVQMrieisrLHK----------RLGRtmiyvTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1272-1458 |
4.27e-11 |
|
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: 64.24 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1272 PGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGV---DTSQ-LELAQLRSQLAIIPQEPFLFSG-TVRENLDpQGL 1346
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGLVFQQYALFPHlNVRENLA-FGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1347 HKDRalwQALKQCHLSEVITSMGGLDGELGEGGRsLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQ---QT 1423
Cdd:cd03297 101 KRKR---NREDRISVDELLDLLGLDHLLNRYPAQ-LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLpelKQ 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 312176403 1424 ICKRFaNKTVLTIAHRLNTI-LNSDRVLVLQAGRVV 1458
Cdd:cd03297 177 IKKNL-NIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1262-1461 |
5.11e-11 |
|
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: 64.09 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLEL-AQLRSQLaiipqepflfsgTVREN 1340
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgGGFNPEL------------TGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 LdpqglhKDRALWQALKQ-------------CHLSEVITSmggldgelgeGGRSLSLGQRQLLCLARALLTDAKILCIDE 1407
Cdd:cd03220 105 I------YLNGRLLGLSRkeidekideiiefSELGDFIDL----------PVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 1408 ATASVD----QKTDQLLQQTICKrfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELD 1461
Cdd:cd03220 169 VLAVGDaafqEKCQRRLRELLKQ---GKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
621-812 |
5.70e-11 |
|
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: 63.99 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----------LSKGFGLATQEPWIqFA--TIRDNILFG 687
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglppherARAGIGYVPEGRRI-FPelTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 ktfdAQLYKEVLEACALNDDLSILPAGDQTEvGEKGVTLSGGQRARIALARAVYQEKELYLLDDP---LA-AVDADVANH 763
Cdd:cd03224 100 ----AYARRRAKRKARLERVYELFPRLKERR-KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLApKIVEEIFEA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 312176403 764 LLHRCILGMlsytTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03224 175 IRELRDEGV----TILLVEQNaRFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1246-1458 |
6.42e-11 |
|
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: 64.34 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAY--RPglpnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSG---RVLldGVDTSQLELAQLR 1320
Cdd:COG1119 4 LELRNVTVRRggKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1321 SQLAII-P--QEPFLFSGTVRE--------------NLDPQglHKDRAlWQALKQCHLSEVITsmggldgelgEGGRSLS 1383
Cdd:COG1119 78 KRIGLVsPalQLRFPRDETVLDvvlsgffdsiglyrEPTDE--QRERA-RELLELLGLAHLAD----------RPFGTLS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 1384 LGQRQLLCLARALLTDAKILCIDEATASVDQK-TDQLLQ--QTICKRFAnKTVLTIAHRLNTILNS-DRVLVLQAGRVV 1458
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGaRELLLAllDKLAAEGA-PTLVLVTHHVEEIPPGiTHVLLLKDGRVV 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
621-797 |
6.56e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.02 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlSKGFGLATQ---EPWIQFATIRDNILFGK--------- 688
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-GARVAYVPQrseVPDSLPLTVRDLVAMGRwarrglwrr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 689 --TFDAQLYKEVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA----DVAN 762
Cdd:NF040873 92 ltRDDRAAVDDALERVGL-ADLAGRQLG----------ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAesreRIIA 160
|
170 180 190
....*....|....*....|....*....|....*
gi 312176403 763 HLLHRCILGmlsyTTRLLCTHRTEYLERADAVLLM 797
Cdd:NF040873 161 LLAEEHARG----ATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1246-1458 |
7.13e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.74 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ 1322
Cdd:PRK10908 2 IRFEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1323 LAIIPQE-PFLFSGTVRENL-------DPQGLHKDRALWQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLAR 1394
Cdd:PRK10908 81 IGMIFQDhHLLMDRTVYDNVaipliiaGASGDDIRRRVSAALDKVGLLDKAKNFPI----------QLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1395 ALLTDAKILCIDEATASVDQKtdqlLQQTICKRFA--NK---TVLTIAHRLNTILNSD-RVLVLQAGRVV 1458
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDA----LSEGILRLFEefNRvgvTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1246-1470 |
8.74e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 64.44 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP---SSGRVLLDGVDTSQLELAQLRSQ 1322
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1323 LAIIPQEP-FLFSG-TVREN----LDPQGLHKD---RALWQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLA 1393
Cdd:PRK13640 86 VGIVFQNPdNQFVGaTVGDDvafgLENRAVPRPemiKIVRDVLADVGMLDYIDS----------EPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1394 RALLTDAKILCIDEATASVDQK-TDQLLQqtICKRFANK---TVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAgKEQILK--LIRKLKKKnnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 312176403 1470 P 1470
Cdd:PRK13640 234 V 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
621-812 |
9.27e-11 |
|
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: 66.36 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV----------------RGLSKGF-GLATQE-PWIQFATIRD 682
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgRGRAKRYiGILHQEyDLYPHRTVLD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 683 NILfgKTFDAQLYKE--------VLEACALNDD--LSILPAGDQTevgekgvtLSGGQRARIALARAVYQEKELYLLDDP 752
Cdd:TIGR03269 385 NLT--EAIGLELPDElarmkaviTLKMVGFDEEkaEEILDKYPDE--------LSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 753 LAAVD----ADVANHLLH-RCILGmlsyTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:TIGR03269 455 TGTMDpitkVDVTHSILKaREEME----QTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1246-1461 |
9.35e-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: 63.04 E-value: 9.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLE-----LAQLR 1320
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkdrdIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1321 SQLAIIPQEpflfsgTVRENLD-PQGLHK------DRALWQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLA 1393
Cdd:cd03301 79 QNYALYPHM------TVYDNIAfGLKLRKvpkdeiDERVREVAELLQIEHLLDR----------KPKQLSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1394 RALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELD 1461
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1249-1470 |
1.04e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1249 QDVVLAYRPG--LPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLePS------SGRVLLDG---VDTSQLELA 1317
Cdd:PRK15134 9 ENLSVAFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGeslLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1318 QLR-SQLAIIPQEPFLfsgtvreNLDPqgLHK-DRALWQAL-------KQCHLSEVI-----TSMGGLDGELGEGGRSLS 1383
Cdd:PRK15134 88 GVRgNKIAMIFQEPMV-------SLNP--LHTlEKQLYEVLslhrgmrREAARGEILncldrVGIRQAAKRLTDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1384 LGQRQLLCLARALLTDAKILCIDEATASVDQKTD----QLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1458
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilQLLREL--QQELNMGLLFITHNLSIVRKlADRVAVMQNGRCV 236
|
250
....*....|..
gi 312176403 1459 ELDSPATLRNQP 1470
Cdd:PRK15134 237 EQNRAATLFSAP 248
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1243-1459 |
1.11e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.78 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1243 QGGVEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE--PS---SGRVLLDGVDTSQLELA 1317
Cdd:PRK14247 1 MNKIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1318 QLRSQLAIIPQEPFLFSG-TVREN----LDPQGLHKDRA-----LWQALKQCHLSEVITSMGGLDGElgeggrSLSLGQR 1387
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNlSIFENvalgLKLNRLVKSKKelqerVRWALEKAQLWDEVKDRLDAPAG------KLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1388 QLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAH------RLntilnSDRVLVLQAGRVVE 1459
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1267-1469 |
1.27e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.06 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1267 TFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlrSQLAIIPQEPFLFSG-TVREN----L 1341
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHlTVAQNiglgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1342 DPqGL---HKDRALWQAL-KQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVD---- 1413
Cdd:PRK10771 97 NP-GLklnAAQREKLHAIaRQMGIEDLLARLPG----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 1414 QKTDQLLQQtICKRfANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:PRK10771 166 QEMLTLVSQ-VCQE-RQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSG 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1262-1458 |
1.28e-10 |
|
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: 63.12 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQ----------LELAQlRSQLA--IIPQE 1329
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKrrkkflrrigVVFGQ-KTQLWwdLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1330 PFLFSGTVReNLDPQGLHKDRAlwqalkqcHLSEvitsMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEAT 1409
Cdd:cd03267 115 SFYLLAAIY-DLPPARFKKRLD--------ELSE----LLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1410 ASVDQKTDQLLQQTIckRFANK----TVLTIAHRLNTILN-SDRVLVLQAGRVV 1458
Cdd:cd03267 182 IGLDVVAQENIRNFL--KEYNRergtTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1253-1422 |
1.35e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 62.38 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1253 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLelaqlrsqlAIIPQEPFL 1332
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ---------RDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1333 FSG---------TVRENLD---PQGLHKDRALWQALKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLARALLTDA 1400
Cdd:TIGR01189 77 YLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTG----------FEDLPAAQLSAGQQRRLALARLWLSRR 146
|
170 180
....*....|....*....|..
gi 312176403 1401 KILCIDEATASVDQKTDQLLQQ 1422
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAG 168
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
621-758 |
1.37e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 63.73 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRG-----HVAVRGLSKGFGLATQE----PWIqfaTIRDNILFGKTFD 691
Cdd:COG4525 28 LTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGeitldGVPVTGPGADRGVVFQKdallPWL---NVLDNVAFGLRLR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 692 ----AQLYKEVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:COG4525 105 gvpkAERRARAEELLAL--------------VGLADFarrriwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1217-1461 |
1.58e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.38 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1217 RLEEYTCDLPQePQGQPlqlgtGWLTqggVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRL 1296
Cdd:PRK10522 303 ALAPYKAEFPR-PQAFP-----DWQT---LELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1297 LEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTvrenLDPQGLHKDRALWQA-LKQCHLSEVITsmgglDGEL 1375
Cdd:PRK10522 373 YQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHKLE-----LEDG 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1376 GEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD--------QKTDQLLQQtickrfANKTVLTIAHRLNTILNSD 1447
Cdd:PRK10522 444 RISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDphfrrefyQVLLPLLQE------MGKTIFAISHDDHYFIHAD 517
|
250
....*....|....
gi 312176403 1448 RVLVLQAGRVVELD 1461
Cdd:PRK10522 518 RLLEMRNGQLSELT 531
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
621-811 |
1.86e-10 |
|
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: 62.39 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSS-------LLAAIAGELHrLRGHVAVR---GLSKGFGLATQEPWIQFA-TIRDNI-LFGK 688
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTtikmlttLLKPTSGRAT-VAGHDVVReprEVRRRIGIVFQDLSVDDElTGWENLyIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 689 TFD------AQLYKEVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 761
Cdd:cd03265 100 LYGvpgaerRERIDELLDFVGL------------LEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 762 NHLLhRCILGMLSY--TTRLLCTHrteYLERADA----VLLMEAGRLIRAGPPSEI 811
Cdd:cd03265 168 AHVW-EYIEKLKEEfgMTILLTTH---YMEEAEQlcdrVAIIDHGRIIAEGTPEEL 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
621-810 |
2.04e-10 |
|
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: 62.45 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAG--------------ELHRL--RGHVAVRGLSKGFGLatQ-EPWIQFATIRDN 683
Cdd:COG4181 33 LEVEAGESVAIVGASGSGKSTLLGLLAGldrptsgtvrlagqDLFALdeDARARLRARHVGFVF--QsFQLLPTLTALEN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 684 I-----LFGKTFDAQLYKEVLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:COG4181 111 VmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTGNLDA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 759 DVANHllhrcILGML------SYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSE 810
Cdd:COG4181 180 ATGEQ-----IIDLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
621-812 |
2.22e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.09 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFG- 687
Cdd:PRK13632 30 FEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkeIRKKIGIIFQNPDNQFigATVEDDIAFGl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 --KTFDAQLYKEVLeacalnDDLSilpagdqTEVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:PRK13632 110 enKKVPPKKMKDII------DDLA-------KKVGMEDYldkepqNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 760 vANHLLHRCILGMLSYTTRLL--CTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13632 177 -GKREIKKIMVDLRKTRKKTLisITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1263-1463 |
2.39e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.07 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDGVdtsQLELAQLRSQLAIIPQ-EPFLFSGTVR 1338
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM---PIDAKEMRAISAYVQQdDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1339 ENLDPQG-LHKDRALWQALKQCHLSEVITSMGGLDGE-----LGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASV 1412
Cdd:TIGR00955 118 EHLMFQAhLRMPRRVTKKEKRERVDEVLQALGLRKCAntrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 1413 DQKTDQLLQQTIcKRFANK--TVLTIAHRLNTIL--NSDRVLVLQAGRVVELDSP 1463
Cdd:TIGR00955 198 DSFMAYSVVQVL-KGLAQKgkTIICTIHQPSSELfeLFDKIILMAEGRVAYLGSP 251
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1262-1466 |
2.46e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLePS---SGRVLLDGvdtSQLELAQLR----SQLAIIPQEPFLFS 1334
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEG---EELQASNIRdterAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1335 G-TVREN------LDPQGLHKDRALWQA----LKQCHLS-EVITSMggldgelgeggRSLSLGQRQLLCLARALLTDAKI 1402
Cdd:PRK13549 96 ElSVLENiflgneITPGGIMDYDAMYLRaqklLAQLKLDiNPATPV-----------GNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1403 LCIDEATASV-DQKTDQLLqqTICKRFANKTV--LTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 1466
Cdd:PRK13549 165 LILDEPTASLtESETAVLL--DIIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGM 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1262-1466 |
2.77e-10 |
|
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: 64.82 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVL--FRLLEPSSGRVL---------------------------------L 1306
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1307 DGVDTSQLELAQLRSQLAIIPQEPFLFSG--TVREN----LDPQGLHKDRALWQA---LKQCHLSEVITSMGgldgelge 1377
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvleaLEEIGYEGKEAVGRAvdlIEMVQLSHRITHIA-------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1378 ggRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANK--TVLTIAHRLNTILN-SDRVLVLQA 1454
Cdd:TIGR03269 167 --RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLEN 244
|
250
....*....|..
gi 312176403 1455 GRVVELDSPATL 1466
Cdd:TIGR03269 245 GEIKEEGTPDEV 256
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1253-1470 |
2.84e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.68 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1253 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG---------------VDTSQLELa 1317
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvADKNQLRL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1318 qLRSQLAIIPQEPFLFSG-TVREN-----LDPQGLHKDRALWQALKqcHLSEV-ITSMGGLDGELgeggrSLSLGQRQLL 1390
Cdd:PRK10619 90 -LRTRLTMVFQHFNLWSHmTVLENvmeapIQVLGLSKQEARERAVK--YLAKVgIDERAQGKYPV-----HLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1391 CLARALLTDAKILCIDEATASVDQK-TDQLLQqtICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 1466
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPElVGEVLR--IMQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQL 239
|
....
gi 312176403 1467 RNQP 1470
Cdd:PRK10619 240 FGNP 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
621-820 |
3.72e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.41 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS-----------KGFGLATQEPWIQF-ATI-RDNILFG 687
Cdd:PRK13633 31 LEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdirNKAGMVFQNPDNQIvATIvEEDVAFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 KtfdaqlykevleacalnDDLSILPAGDQTEVGE--KGVT-----------LSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:PRK13633 111 P-----------------ENLGIPPEEIRERVDEslKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 755 AVDA----DVANHLLHrciLGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPK 820
Cdd:PRK13633 174 MLDPsgrrEVVNTIKE---LNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVEMMKK 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1263-1424 |
3.93e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.04 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTsqlELAQLRSQLAII----PQEPFLfsgTVR 1338
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLghrnAMKPAL---TVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1339 ENLdpqglhkdrALWQALKQCHLSEVITSMGGL--DGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 1416
Cdd:PRK13539 92 ENL---------EFWAAFLGGEELDIAAALEAVglAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
....*...
gi 312176403 1417 DQLLQQTI 1424
Cdd:PRK13539 163 VALFAELI 170
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
624-811 |
4.42e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.95 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 624 KKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--------------------------LSKGFGLATQEPWIQF 677
Cdd:PRK13631 50 EKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitnpyskkiknfkeLRRRVSMVFQFPEYQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 678 --ATIRDNILFG-------KTFDAQLYKEVLEACALNDD-LSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKELY 747
Cdd:PRK13631 130 fkDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 748 LLDDPLAAVDADvANHLLHRCIL-GMLSYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13631 199 IFDEPTAGLDPK-GEHEMMQLILdAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
620-811 |
5.11e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.34 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV--------------RGLSKGFGLATQEPWIQF--ATIRDN 683
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkknkklKPLRKKVGIVFQFPEHQLfeETVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 684 ILFG-KTF-----DA-QLYKEVLEACALNDDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAV 756
Cdd:PRK13634 107 ICFGpMNFgvseeDAkQKAREMIELVGLPEELLARSPFE----------LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 757 DADVANHL------LHRcILGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13634 177 DPKGRKEMmemfykLHK-EKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
621-812 |
5.50e-10 |
|
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: 61.55 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIagelHRL----RGHVAVRG----------LSKGFGLATQE----PWIqfaTIRD 682
Cdd:cd03295 22 LEIAKGEFLVLIGPSGSGKTTTMKMI----NRLieptSGEIFIDGedireqdpveLRRKIGYVIQQiglfPHM---TVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 683 NI-----LFGKTfDAQLYKEVLEACALNDdlsiLPagDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:cd03295 95 NIalvpkLLKWP-KEKIRERADELLALVG----LD--PAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 758 ADVANHL------LHRcilgmLSYTTRLLCTHRT-EYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03295 168 PITRDQLqeefkrLQQ-----ELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1246-1464 |
6.48e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.06 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL-DGVDTS---QLELAQ 1318
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSStskQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1319 LRSQLAIIPQEP--FLFSGTVRENL--DPQ--GLHKDRALWQAlkqchlSEVITSMGGLDGELGEGGRSLSLGQRQLLCL 1392
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafGPQnfGIPKEKAEKIA------AEKLEMVGLADEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1393 ARALLTDAKILCIDEATASVDQKTD-QLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPA 1464
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARiEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPS 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1262-1465 |
6.60e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 61.25 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAqlrsqLAIIPQepflFSGtvREN- 1340
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELG-----AGFHPE----LTG--RENi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 ------LdpqGLHKD--RALwqalkqchLSEVI----------TSMggldgelgeggRSLSLGQRQLLCLARALLTDAKI 1402
Cdd:COG1134 110 ylngrlL---GLSRKeiDEK--------FDEIVefaelgdfidQPV-----------KTYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1403 LCIDEATASVD----QKTDQLLQQticKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPAT 1465
Cdd:COG1134 168 LLVDEVLAVGDaafqKKCLARIRE---LRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEE 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
620-812 |
6.72e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.14 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV------------AVRGLSKGFglatQEPWIqFA--TIRDNIL 685
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhtttppSRRPVSMLF----QENNL-FShlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 686 FG-----KTFDAQlyKEVLEACA----LNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAV 756
Cdd:PRK10771 94 LGlnpglKLNAAQ--REKLHAIArqmgIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 757 DADVANHllhrcILGMLS------YTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK10771 161 DPALRQE-----MLTLVSqvcqerQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
611-820 |
7.38e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 61.68 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 611 GTSLET---FISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV--------------RGLSKGFGLATQEP 673
Cdd:PRK13649 15 GTPFEGralFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVddtlitstsknkdiKQIRKKVGLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 674 WIQ-FA-TIRDNILFG-KTFDAQlyKEVLEACALNddlSILPAGDQTEVGEKG-VTLSGGQRARIALARAVYQEKELYLL 749
Cdd:PRK13649 95 ESQlFEeTVLKDVAFGpQNFGVS--QEEAEALARE---KLALVGISESLFEKNpFELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 750 DDPLAAVDADVANHL------LHRciLGMlsytTRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEILPLVQ------ 816
Cdd:PRK13649 170 DEPTAGLDPKGRKELmtlfkkLHQ--SGM----TIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIFQDVDfleekq 243
|
....*
gi 312176403 817 -AVPK 820
Cdd:PRK13649 244 lGVPK 248
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
621-811 |
7.73e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.43 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGfglATQEPWI-----QFA-----TIRDNILFG- 687
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedVTHR---SIQQRDIcmvfqSYAlfphmSLGENVGYGl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 ---KTFDAQLYKEVLEACALNDdlsilPAG------DQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:PRK11432 104 kmlGVPKEERKQRVKEALELVD-----LAGfedryvDQ---------ISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 759 DvanhlLHRCI------LGMLSYTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11432 170 N-----LRRSMrekireLQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
621-803 |
7.85e-10 |
|
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: 59.36 E-value: 7.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlskgfglatqEPwIQFATIRDnilfgktfdAQlykevle 700
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG----------KE-VSFASPRD---------AR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 701 acalnddlsilpagdqtevgEKGVT----LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGML--S 774
Cdd:cd03216 74 --------------------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLraQ 131
|
170 180 190
....*....|....*....|....*....|
gi 312176403 775 YTTRLLCTHR-TEYLERADAVLLMEAGRLI 803
Cdd:cd03216 132 GVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1246-1458 |
8.88e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.64 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRV---LLDGVDTSQLELA-- 1317
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1318 -------------------QLRSQLAIIPQ--EPFLFSGTVRENL--DPQ--GLHKDRALWQALKQCHLSEVITSMggld 1372
Cdd:PRK13651 83 vleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVsmGVSKEEAKKRAAKYIELVGLDESY---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1373 gelgeGGRS---LSLGQRQLLCLARALLTDAKILCIDEATASVD-QKTDQLLQqtICKRF--ANKTVLTIAHRLNTILN- 1445
Cdd:PRK13651 159 -----LQRSpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILE--IFDNLnkQGKTIILVTHDLDNVLEw 231
|
250
....*....|...
gi 312176403 1446 SDRVLVLQAGRVV 1458
Cdd:PRK13651 232 TKRTIFFKDGKII 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1263-1461 |
9.17e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqlelaQLRsqLAIIPQEPFLFSG-TVRENL 1341
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------GLR--IGYLPQEPPLDDDlTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1342 dpqgLHKDRALWQALKQchLSEVITSMGGLDGELGEGGR------------------------------------SLSLG 1385
Cdd:COG0488 83 ----LDGDAELRALEAE--LEELEAKLAEPDEDLERLAElqeefealggweaearaeeilsglgfpeedldrpvsELSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1386 QRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTIcKRFANkTVLTIAHrlntilnsDRVLvLQ--AGRVVELD 1461
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL-KNYPG-TVLVVSH--------DRYF-LDrvATRILELD 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
620-800 |
9.48e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.29 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGelhrL----RGHVAVRGLSKGFGLAtQEPWIQFATIRDNILF---GKTFDA 692
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARPAGARVLFLP-QRPYLPLGTLREALLYpatAEAFSD 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 693 QLYKEVLEACALnDDLsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGM 772
Cdd:COG4178 458 AELREALEAVGL-GHL----AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREE 531
|
170 180
....*....|....*....|....*...
gi 312176403 773 LSYTTRLLCTHRTEYLERADAVLLMEAG 800
Cdd:COG4178 532 LPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1258-1459 |
1.04e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 61.66 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1258 GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDG---VDTSQLELAQLRS-QLAIIPQEP 1330
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGreiLNLPEKELNKLRAeQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1331 FlfsgtvrENLDP---------------QGLHKDRALWQALKQchLSEVitSMGGLDGELGEGGRSLSLGQRQLLCLARA 1395
Cdd:PRK09473 107 M-------TSLNPymrvgeqlmevlmlhKGMSKAEAFEESVRM--LDAV--KMPEARKRMKMYPHEFSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1396 LLTDAKILCIDEATASVDQkTDQ-----LLQQTicKRFANKTVLTIAHRLNTILNS-DRVLVLQAGRVVE 1459
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDV-TVQaqimtLLNEL--KREFNTAIIMITHDLGVVAGIcDKVLVMYAGRTME 242
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1262-1470 |
1.30e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.39 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLAIIP--QEPFLF-SGTVR 1338
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVVRtfQHVRLFrEMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1339 ENL-DPQ----------GLHK------------DRAL-WqaLKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLAR 1394
Cdd:PRK11300 99 ENLlVAQhqqlktglfsGLLKtpafrraesealDRAAtW--LERVGLLEHANR----------QAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 1395 ALLTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIaeLRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
621-812 |
1.44e-09 |
|
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: 60.14 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH------RLRGH---------VAVRGLSKGFglatQEPWIqFA--TIRDN 683
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsvLFDGEditglppheIARLGIGRTF----QIPRL-FPelTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 684 ILFGKTFDAQLY-----------------KEVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKEL 746
Cdd:cd03219 96 VMVAAQARTGSGlllararreereareraEELLERVGL-ADLADRPAG----------ELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 747 YLLDDPLAAVDADVANHLLHRcILGM-LSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAEL-IRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1263-1470 |
1.46e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSG-----RVLLDGVDT-SQLELAQLRSQLAIIPQEPFLFSGT 1336
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1337 VREN-LDPQGLHK--DRALWQALKQCHLSEVITSMGGLDGELGEGGRsLSLGQRQLLCLARALLTDAKILCIDEATASVD 1413
Cdd:PRK14271 117 IMDNvLAGVRAHKlvPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1414 QKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
620-757 |
1.51e-09 |
|
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: 59.86 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS-----------KGFGLATQEPWIqFA--TIRDNIL- 685
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarLGIGYLPQEASI-FRklTVEENILa 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 686 ----FGKTFDAQlyKEVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:cd03218 99 vleiRGLSKKER--EEKLEE--LLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
621-802 |
1.64e-09 |
|
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: 59.47 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGeLHRL-RGHVAVRGLS------------KGFGLATQepwiQFA-----TIRD 682
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINL-LEEPdSGTIIIDGLKltddkkninelrQKVGMVFQ----QFNlfphlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 683 NILFGKTF-------DAQ-LYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:cd03262 96 NITLAPIKvkgmskaEAEeRALELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 755 AVDA-------DVANHLLHRcilGMlsytTRLLCTHRTEY-LERADAVLLMEAGRL 802
Cdd:cd03262 165 ALDPelvgevlDVMKDLAEE---GM----TMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1263-1470 |
1.69e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE------PSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSG- 1335
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1336 TVREN----LDPQGLHKDRALWQALKQChLSEViTSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATAS 1411
Cdd:PRK14246 106 SIYDNiaypLKSHGIKEKREIKKIVEEC-LRKV-GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1412 VDQKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
621-820 |
1.73e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.79 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV---------------AVRGLSKGFGLATQEPWIQF--ATIRDN 683
Cdd:PRK13645 32 LTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyaipanlkkikEVKRLRKEIGLVFQFPEYQLfqETIEKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 684 ILFGKTF----DAQLYKEVLEACalndDLSILPagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:PRK13645 112 IAFGPVNlgenKQEAYKKVPELL----KLVQLP---EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 760 VANHLLHRCILGMLSYTTR-LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEILPLVQAVPK 820
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRiIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFSNQELLTK 247
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
620-812 |
2.43e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFA-TIRDNILFG- 687
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaeLARRRAVLPQHSSLSFPfTVEEVVAMGr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 ------KTFDAQLYKEVLEACALnDDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQ------EKELYLLDDPLAA 755
Cdd:PRK13548 102 aphglsRAEDDALVAAALAQVDL-AHLA----------GRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 756 VD-------ADVANHLLHR------CILGMLSYTTRllcthrteYlerADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13548 171 LDlahqhhvLRLARQLAHErglaviVVLHDLNLAAR--------Y---ADRIVLLHQGRLVADGTPAEVL 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
621-811 |
2.88e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.63 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAG-------ELH---RLRGHV--AVRGLSKGFglatqepwiQ-FA-----TIRD 682
Cdd:PRK11650 25 LDVADGEFIVLVGPSGCGKSTLLRMVAGleritsgEIWiggRVVNELepADRDIAMVF---------QnYAlyphmSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 683 NILFG----KTFDAQLYKEVLEACALnddLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:PRK11650 96 NMAYGlkirGMPKAEIEERVAEAARI---LELEPLLDR-----KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 759 DVANHL------LHRCiLGmlsyTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11650 168 KLRVQMrleiqrLHRR-LK----TTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1213-1467 |
3.03e-09 |
|
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: 61.35 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1213 VSVERLEEYTCDLPQEPQGQPLQLGTGWLTQ-GGVEFQDVVLAYrpglPNALDGVTFCV-------QPGEKLGIVGRTGS 1284
Cdd:COG4615 294 VALRKIEELELALAAAEPAAADAAAPPAPADfQTLELRGVTYRY----PGEDGDEGFTLgpidltiRRGELVFIVGGNGS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1285 GKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFsgtvRENLDPQGLHKDRALWQALKQCHLSEV 1364
Cdd:COG4615 370 GKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLERLELDHK 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1365 IT------SmggldgelgegGRSLSLGQRQLLCLARALLTDAKILCIDEATAsvDQktD---------QLLQQTicKRfA 1429
Cdd:COG4615 446 VSvedgrfS-----------TTDLSQGQRKRLALLVALLEDRPILVFDEWAA--DQ--DpefrrvfytELLPEL--KA-R 507
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 312176403 1430 NKTVLTIAH-----RLntilnSDRVLVLQAGRVVELDSPATLR 1467
Cdd:COG4615 508 GKTVIAISHddryfDL-----ADRVLKMDYGKLVELTGPAALA 545
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
621-817 |
3.23e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.64 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS----------KGFGLATQEPWIQF--ATIRDNILFGk 688
Cdd:PRK13635 28 FSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrRQVGMVFQNPDNQFvgATVQDDVAFG- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 689 tfdaqlykevLEACALNDDLSIlPAGDQ--TEVG------EKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA-- 758
Cdd:PRK13635 107 ----------LENIGVPREEMV-ERVDQalRQVGmedflnREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrg 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176403 759 -----DVANHLLHRCILGMLSyttrllCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQA 817
Cdd:PRK13635 176 rrevlETVRQLKEQKGITVLS------ITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
621-812 |
3.45e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 59.36 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfgLATQEPW--------------IQFA-TIRDNIL 685
Cdd:COG4559 22 LTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRP----LAAWSPWelarrravlpqhssLAFPfTVEEVVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 686 FG-------KTFDAQLYKEVLEACalndDLSILPAGDQTevgekgvTLSGGQRARIALARA-------VYQEKELYLLDD 751
Cdd:COG4559 98 LGraphgssAAQDRQIVREALALV----GLAHLAGRSYQ-------TLSGGEQQRVQLARVlaqlwepVDGGPRWLFLDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 752 PLAAVD-------ADVANHLLHR-----CILGMLSYTTRLlcthrteylerADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG4559 167 PTSALDlahqhavLRLARQLARRgggvvAVLHDLNLAAQY-----------ADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
620-814 |
4.05e-09 |
|
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: 57.92 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGelHR----LRGHVAVRGLS-----------KGFGLATQEPwIQFATIRDni 684
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPkyevTEGEILFKGEDitdlppeerarLGIFLAFQYP-PEIPGVKN-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 685 lfgktfdAQLYKEVleacalnddlsilpagdqtevgekGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHL 764
Cdd:cd03217 95 -------ADFLRYV------------------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID-ALRL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312176403 765 LHRCILGMLSYTTR-LLCTHRTEYLE--RADAVLLMEAGRLIRAGPPSEILPL 814
Cdd:cd03217 143 VAEVINKLREEGKSvLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKELALEI 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1262-1462 |
4.27e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG----------VDTSQLELAQLR----SQLAIIP 1327
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhvrgADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1328 QEP-------FLFSGTVRENLD-PQGLHKDRALWQA---LKQCHLSEVITSMggldgelGEGGRSLSLGQRQLLCLARAL 1396
Cdd:PRK10261 111 QEPmtslnpvFTVGEQIAESIRlHQGASREEAMVEAkrmLDQVRIPEAQTIL-------SRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 1397 LTDAKILCIDEATASVDQKTD-QLLQQ-TICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDS 1462
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQaQILQLiKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1246-1466 |
4.36e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.82 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlELAQLRSQLAI 1325
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQ----EPFLfsgTVRENLDPQGlhkdRALWQALKQCH-LSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDA 1400
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFG----RYFGLSAAAARaLVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 1401 KILCIDEATASVDQKTDQLLQQTICKRFAN-KTVLTIAH------RLntilnSDRVLVLQAGRVVELDSPATL 1466
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHAL 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1246-1463 |
4.69e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 59.32 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQL 1323
Cdd:PRK13639 2 LETRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEP--FLFSGTVRE-------NLdpqGLHKD---RALWQALKQCHLSevitsmggldGELGEGGRSLSLGQRQLLC 1391
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEdvafgplNL---GLSKEeveKRVKEALKAVGME----------GFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1392 LARALLTDAKILCIDEATASVD----QKTDQLLQQTickrfaNKTVLTI---AHRLNTI-LNSDRVLVLQAGRVVELDSP 1463
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDpmgaSQIMKLLYDL------NKEGITIiisTHDVDLVpVYADKVYVMSDGKIIKEGTP 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1208-1460 |
5.24e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1208 TEAMLVSVERLEEYT-CDLPQ--------EPQGQPLQLGTGWLTQGG--VEFQDVVLAY--RPGLPN-------ALDGVT 1267
Cdd:PRK10261 265 TRALLAAVPQLGAMKgLDYPRrfplisleHPAKQEPPIEQDTVVDGEpiLQVRNLVTRFplRSGLLNrvtrevhAVEKVS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1268 FCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDT-SQLELAQLRSQLAIIPQEPFlfsgtvrENLDP- 1343
Cdd:PRK10261 345 FDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTlSPGKLQALRRDIQFIFQDPY-------ASLDPr 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1344 --------QGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD-- 1413
Cdd:PRK10261 418 qtvgdsimEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDvs 497
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1414 ---QKTDQLLQqtiCKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVEL 1460
Cdd:PRK10261 498 irgQIINLLLD---LQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEI 545
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1263-1422 |
5.69e-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: 57.50 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLD 1342
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1343 -PQGLHKDRALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQ 1421
Cdd:cd03231 96 fWHADHSDEQVEEALARVGLNGF----------EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
.
gi 312176403 1422 Q 1422
Cdd:cd03231 166 E 166
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1253-1463 |
5.79e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.78 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1253 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL---------RSQL 1323
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEP-------FLFSGTVRENLDPQGL-H----KDRAL-WqalkqchLSEVitsmGGLDGELGEGGRSLSLGQRQLL 1390
Cdd:PRK11701 92 GFVHQHPrdglrmqVSAGGNIGERLMAVGArHygdiRATAGdW-------LERV----EIDAARIDDLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1391 CLARALLTDAKILCIDEATA----SVDQKTDQLLQQTIckRFANKTVLTIAHRLNTI-LNSDRVLVLQAGRVVE------ 1459
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGgldvSVQARLLDLLRGLV--RELGLAVVIVTHDLAVArLLAHRLLVMKQGRVVEsgltdq 238
|
....*
gi 312176403 1460 -LDSP 1463
Cdd:PRK11701 239 vLDDP 243
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
313-750 |
5.98e-09 |
|
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: 60.58 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 313 LEEGQEPLSHGLLYALGLAGGAVLGAVL-QNQYGYEVYKVTLQARGAVLN-ILYC---KALQLGPSRpptgeALNLLGTD 387
Cdd:COG4615 40 LNATGAALARLLLLFAGLLVLLLLSRLAsQLLLTRLGQHAVARLRLRLSRrILAApleRLERIGAAR-----LLAALTED 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 388 SERLLNFAGSFHEA-WGLPLQLAITLYLLYQQVgVAFVGGLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELL 466
Cdd:COG4615 115 VRTISQAFVRLPELlQSVALVLGCLAYLAWLSP-PLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 467 SGIRVIK---------FcgwEQALGARVEACRARelgRLRVIKYLDAACVYLWAALPVVISIVIFityVLMGHQLTATKV 537
Cdd:COG4615 194 EGFKELKlnrrrrrafF---DEDLQPTAERYRDL---RIRADTIFALANNWGNLLFFALIGLILF---LLPALGWADPAV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 538 FTALALVRM-LILPLNNFPWVINGLLEAKVSLDRI-QLFLDLPNHNPQAYYSPDPPAEPS-TVLELHGALFSWDPVGTSl 614
Cdd:COG4615 265 LSGFVLVLLfLRGPLSQLVGALPTLSRANVALRKIeELELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGD- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 615 ETF----IShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlsKGFGLATQEPWIQ-FATI-RDNILF-- 686
Cdd:COG4615 344 EGFtlgpID-LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG--QPVTADNREAYRQlFSAVfSDFHLFdr 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 687 ----GKTFDAQLYKEVLEACALNDDLSIlpagdqtevgEKG----VTLSGGQRARIALARAVYQEKELYLLD 750
Cdd:COG4615 421 llglDGEADPARARELLERLELDHKVSV----------EDGrfstTDLSQGQRKRLALLVALLEDRPILVFD 482
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
611-806 |
6.53e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 611 GTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAA-------------IAGELHRLRGHV---AVRGLSKGFGLATQE-- 672
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVlnllemprsgtlnIAGNHFDFSKTPsdkAIRELRRNVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 673 PWIQFaTIRDNIL--------FGKTFDAQLYKEVLEACALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQEK 744
Cdd:PRK11124 93 LWPHL-TVQQNLIeapcrvlgLSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 745 ELYLLDDPLAAVDADVANHLLHrcILGMLSYT--TRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVS--IIRELAETgiTQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
621-818 |
7.99e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 57.73 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS-----------KGFGLATQEPWIqFA--TIRDNIL-- 685
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmhkrarLGIGYLPQEASI-FRklTVEDNILav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 686 ---FGKTFDAQlyKEVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVD----A 758
Cdd:COG1137 103 lelRKLSKKER--EERLEE--LLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiavA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 759 DVAN---HLLHRCIlGMlsyttrLLCTH--RtEYLERADAVLLMEAGRLIRAGPPSEIL--PLVQAV 818
Cdd:COG1137 174 DIQKiirHLKERGI-GV------LITDHnvR-ETLGICDRAYIISEGKVLAEGTPEEILnnPLVRKV 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1262-1462 |
9.40e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 9.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE--PS---SGRVLLDGVD--TSQLELAQLRSQLAIIPQEPFLFS 1334
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1335 GTVREN----LDPQGLHK----DRALWQALKQCHL-SEVITSMGGLDGelgeggrSLSLGQRQLLCLARALLTDAKILCI 1405
Cdd:PRK14239 100 MSIYENvvygLRLKGIKDkqvlDEAVEKSLKGASIwDEVKDRLHDSAL-------GLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1406 DEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDS 1462
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1246-1470 |
1.03e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.28 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1325
Cdd:PRK13652 4 IETRDLCYSYS-GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEP--FLFSGTVRENL--DPQGLHKDRA-----LWQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARAL 1396
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIafGPINLGLDEEtvahrVSSALHMLGLEELRDRV----------PHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1397 LTDAKILCIDEATASVD-QKTDQLLqqtickRFANK-------TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLR 1467
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDpQGVKELI------DFLNDlpetygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIF 226
|
...
gi 312176403 1468 NQP 1470
Cdd:PRK13652 227 LQP 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
621-757 |
1.07e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.87 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAA-------IAGelHRLRGHVAVRG------------LSKGFGLATQEPWIQFATIR 681
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPG--FRVEGKVTFHGknlyapdvdpveVRRRIGMVFQKPNPFPKSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 682 DNILFGKTFDA------QLYKEVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK14243 109 DNIAYGARINGykgdmdELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
..
gi 312176403 756 VD 757
Cdd:PRK14243 182 LD 183
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
621-812 |
1.08e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.93 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAI-----AGELHRLRGHVAVRGLS------------KGFGLATQEP-WIQFATIRD 682
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNiyspdvdpievrREVGMVFQYPnPFPHLTIYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 683 NILFGKTFDA---------QLYKEVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:PRK14267 105 NVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 754 AAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK14267 178 ANIDP-VGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
631-811 |
1.12e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 631 IVGKVGCGKSSLLAAI--AGELH---RLRGHVAVRG------------LSKGFGLATQEPWIQFATIRDNILFGKTFDAQ 693
Cdd:PRK14239 36 LIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGhniysprtdtvdLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 694 LYKEVLEACALNddlSILPAGDQTEVGEK----GVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCI 769
Cdd:PRK14239 116 KDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDP-ISAGKIEETL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 312176403 770 LGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK14239 192 LGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
588-764 |
1.15e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.31 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 588 PDPPAEPSTVLELHGALFSWD--PVgtsLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV-RGLSK 664
Cdd:COG0488 306 PPPERLGKKVLELEGLSKSYGdkTL---LDDL--SLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 665 GFglatqepwiqFATIRDnilfgkTFDAQlyKEVLEA-CALNDDLSILPA----------GDQ--TEVGekgvTLSGGQR 731
Cdd:COG0488 381 GY----------FDQHQE------ELDPD--KTVLDElRDGAPGGTEQEVrgylgrflfsGDDafKPVG----VLSGGEK 438
|
170 180 190
....*....|....*....|....*....|...
gi 312176403 732 ARIALARAVYQEKELYLLDDPlaavdadvANHL 764
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEP--------TNHL 463
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1263-1413 |
1.19e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.60 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLEL-AQLRSQLAIIPQEPFLFSG------ 1335
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlsvydn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1336 -----TVRENLDPQGlHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARALLTDAKILCIDEATA 1410
Cdd:PRK10895 99 lmavlQIRDDLSAEQ-REDRAN-ELMEEFHIEHLRDSM----------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
...
gi 312176403 1411 SVD 1413
Cdd:PRK10895 167 GVD 169
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
621-821 |
1.64e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 57.39 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG------------LSKGFGLATQEPWIQ-FA-TIRDNILF 686
Cdd:PRK13639 23 FKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkslleVRKTVGIVFQNPDDQlFApTVEEDVAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 G----KTFDAQLYKEVLEACAlnddlsilpagdqtEVGEKGVT------LSGGQRARIALARAVYQEKELYLLDDPLAAV 756
Cdd:PRK13639 103 GplnlGLSKEEVEKRVKEALK--------------AVGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 757 DADVANHLLHrcILGMLSY--TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEILPLVQAVPKA 821
Cdd:PRK13639 169 DPMGASQIMK--LLYDLNKegITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSDIETIRKA 234
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
622-768 |
1.67e-08 |
|
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: 59.38 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 622 EVKKGMLVGIVGKVGCGKSSLLAaIAGELHRLRGHVAVRGLSKGFGLATQEPWIQFATIRDNIL--------FGKTFDAQ 693
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIypdssedmKRRGLSDK 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 694 LYKEVLEACALNDDLsilpagdQTEVGEKGV-----TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRC 768
Cdd:TIGR00954 553 DLEQILDNVQLTHIL-------EREGGWSAVqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
621-812 |
1.67e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.21 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV------------RGLsKGFGLATQEPWI-QFATIRDNILFG 687
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplhaRAR-RGIGYLPQEASIfRRLSVYDNLMAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 KTFDAQLYKEVLE--ACALNDDLSILPAGDQTevgekGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLL 765
Cdd:PRK10895 103 LQIRDDLSAEQREdrANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP-ISVIDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 312176403 766 HRCILGMLSYTTRLLCTHRT--EYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK10895 177 KRIIEHLRDSGLGVLITDHNvrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
542-806 |
1.79e-08 |
|
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: 59.06 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 542 ALVRMLILPLNNFPWVINgllEAKVSLDRIQLFLDLPNHNPQAYYSPDPPAEPSTvlelHGAL------FSWDPVGTSLE 615
Cdd:COG5265 303 AYLIQLYIPLNFLGFVYR---EIRQALADMERMFDLLDQPPEVADAPDAPPLVVG----GGEVrfenvsFGYDPERPILK 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 616 TfIShLEVKKGMLVGIVGKVGCGKSSLLaaiagelhRL--------RGHVAVRG----------LSKGFGLATQEPwIQF 677
Cdd:COG5265 376 G-VS-FEVPAGKTVAIVGPSGAGKSTLA--------RLlfrfydvtSGRILIDGqdirdvtqasLRAAIGIVPQDT-VLF 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 678 -ATIRDNILFGKTfDAQlYKEVLEA---CALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:COG5265 445 nDTIAYNIAYGRP-DAS-EEEVEAAaraAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176403 754 AAVD-----------ADVANHllhrcilgmlsyTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 806
Cdd:COG5265 523 SALDsrteraiqaalREVARG------------RTTLVIAHRLSTIVDADEILVLEAGRIVERG 574
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
621-802 |
1.85e-08 |
|
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: 56.26 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------------LSKGFGLATQE-PWIQFATIRDNILF 686
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipyLRRKIGVVFQDfRLLPDRNVYENVAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 -------GKTFDAQLYKEVLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:cd03292 102 alevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 312176403 760 VANHLLHRCILGMLSYTTRLLCTHRTEYLERADA-VLLMEAGRL 802
Cdd:cd03292 171 TTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
621-811 |
1.88e-08 |
|
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: 56.36 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPWI----QF------ATIRDNILF---- 686
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgycpQFdalfdeLTVREHLRFyarl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 -GKtFDAQLYKEVLeacALNDDLSILPAGDqTEVGekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLL 765
Cdd:cd03263 103 kGL-PKSEIKEEVE---LLLRVLGLTDKAN-KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP-ASRRAI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 312176403 766 HRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:cd03263 173 WDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1256-1458 |
1.89e-08 |
|
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: 56.12 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1256 RPGLPNA--LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDGVDtSQLELAQLRSQLAIIPQEP 1330
Cdd:cd03233 14 GKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP-YKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1331 FLFSG-TVRENLDpqglhkdralwQALKqCHLSEVItsmggldgelgeggRSLSLGQRQLLCLARALLTDAKILCIDEAT 1409
Cdd:cd03233 93 VHFPTlTVRETLD-----------FALR-CKGNEFV--------------RGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312176403 1410 ASVDQKTD-QLLQ--QTICKRFANKTVLTIAHRLNTILNS-DRVLVLQAGRVV 1458
Cdd:cd03233 147 RGLDSSTAlEILKciRTMADVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQI 199
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1263-1470 |
1.96e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.97 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ-LAIIPQEPFLFSG-TV 1337
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREhFGFIFQRYHLLSHlTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1338 RENLD-PQ---GLHKDRALWQA---LKQCHLSEVITsmggldgelgEGGRSLSLGQRQLLCLARALLTDAKILCIDEATA 1410
Cdd:PRK10535 104 AQNVEvPAvyaGLERKQRLLRAqelLQRLGLEDRVE----------YQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1411 SVDQKTdqllqqtickrfaNKTVLTIAHRLN------TILNSDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:PRK10535 174 ALDSHS-------------GEEVMAILHQLRdrghtvIIVTHDPQVAAQAERVIEIRDGEIVRNPP 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
621-789 |
2.56e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGElhrlrghvAVRGLSKGFGLATQEPWIQFATIRDNILFGKTFDAQLykEVLE 700
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGA--------LKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAV--ELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 701 ACALNDDLSILPAGDQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS---YTT 777
Cdd:COG2401 121 AVGLSDAVLWLRRFKE---------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR--NLQKLArraGIT 189
|
170
....*....|..
gi 312176403 778 RLLCTHRTEYLE 789
Cdd:COG2401 190 LVVATHHYDVID 201
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
621-806 |
2.81e-08 |
|
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: 55.75 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlsKGFGLATQEpwiQFA------------TIRDNILFGk 688
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--KPLDIAARN---RIGylpeerglypkmKVIDQLVYL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 689 tfdAQLyKEVLEACALNDDLSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHR 767
Cdd:cd03269 95 ---AQL-KGLKKEEARRRIDEWLERLELSEYANKRVeELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 312176403 768 CILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:cd03269 170 VIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
623-812 |
2.83e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.53 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 623 VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS---------KGFGLATQ----EPwiQFaTIRDNIL-FGK 688
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvpararlarARIGVVPQfdnlDL--EF-TVRENLLvFGR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 689 TFDAQLyKEVLEACALNDDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRC 768
Cdd:PRK13536 141 YFGMST-REIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWER 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 312176403 769 ILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13536 215 LRSLLARgKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
623-806 |
2.84e-08 |
|
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: 55.84 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 623 VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------------LSKGFGLAtqePWIqfaTIRDNILF 686
Cdd:cd03266 28 VKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrrlgfVSDSTGLY---DRL---TARENLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 gktFdAQLYKevLEACALNDDLSILpaGDQTEVGE----KGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN 762
Cdd:cd03266 102 ---F-AGLYG--LKGDELTARLEEL--ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 312176403 763 HLL----HRCILGmlsyTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:cd03266 174 ALRefirQLRALG----KCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1263-1416 |
3.38e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.98 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLEL---AQLRSQ-LAIIPQEPFLFSG-TV 1337
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQFHHLLPDfTA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 1338 RENLDPQGLHKDRALWQALKQCHlsEVITSMGGLDGELGEGGRsLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 1416
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRAL--EMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
620-764 |
3.44e-08 |
|
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: 53.99 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAvrglskgfglatqepWIQFATIrdnilfgktfdaqlykevl 699
Cdd:cd03221 20 SLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------------WGSTVKI------------------- 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 700 eacalnddlSILPagdQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLaavdadvaNHL 764
Cdd:cd03221 66 ---------GYFE---Q---------LSGGEKMRLALAKLLLENPNLLLLDEPT--------NHL 101
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1262-1463 |
4.12e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 57.26 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRsQLAIIPQEPFLFSG-TVREN 1340
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENR-HVNTVFQSYALFPHmTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 ----LDPQGLHKD----RALwQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLARALLTDAKILCIDEATASV 1412
Cdd:PRK09452 107 vafgLRMQKTPAAeitpRVM-EALRMVQLEEFAQR----------KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 1413 DQKTDQLLQQTIcKRFANKTVLT---IAHRLNTILN-SDRVLVLQAGRVVELDSP 1463
Cdd:PRK09452 176 DYKLRKQMQNEL-KALQRKLGITfvfVTHDQEEALTmSDRIVVMRDGRIEQDGTP 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1261-1459 |
4.13e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.56 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1261 NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQLAIIPQEPFLFSGTV 1337
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1338 --RENLDPQGL--------HKDRALwQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDE 1407
Cdd:PRK10584 104 naLENVELPALlrgessrqSRNGAK-ALLEQLGLGKRLDHLPA----------QLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 1408 ATASVDQKT-DQL--LQQTICKRFANkTVLTIAHRLNTILNSDRVLVLQAGRVVE 1459
Cdd:PRK10584 173 PTGNLDRQTgDKIadLLFSLNREHGT-TLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1246-1470 |
4.17e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.87 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQL 1323
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 AIIPQEPFLFSG-TVREN-----LDPQGLHKDRALWQA---LKQCHLSEvitsmggldgelgeggRS------LSLGQRQ 1388
Cdd:PRK09493 80 GMVFQQFYLFPHlTALENvmfgpLRVRGASKEEAEKQArelLAKVGLAE----------------RAhhypseLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1389 LLCLARALLTDAKILCIDEATASVDQktdQLLQQ--TICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1463
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDP---ELRHEvlKVMQDLAEEgmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDP 220
|
....*..
gi 312176403 1464 ATLRNQP 1470
Cdd:PRK09493 221 QVLIKNP 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1263-1463 |
4.70e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.17 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQLAIIPQEPflfsgtvren 1340
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDP---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 lDPQGLHKD---------RALWQALKQC--HLSEVITsMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEAT 1409
Cdd:PRK13638 87 -EQQIFYTDidsdiafslRNLGVPEAEItrRVDEALT-LVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1410 ASVDQK-TDQLLqqTICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1463
Cdd:PRK13638 165 AGLDPAgRTQMI--AIIRRIVAQgnHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAP 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
620-798 |
4.95e-08 |
|
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: 54.08 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLAtQEPWIQFATIRDNIlfgktfdaqlykevl 699
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLP-QRPYLPLGTLREQL--------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 700 eacalnddlsILPAGDqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCilgmlsytTRL 779
Cdd:cd03223 85 ----------IYPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL--------KEL 137
|
170 180
....*....|....*....|....
gi 312176403 780 LCT-----HRTEYLERADAVLLME 798
Cdd:cd03223 138 GITvisvgHRPSLWKFHDRVLDLD 161
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1246-1463 |
5.29e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.18 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL-DGV---DTSQLELAQ 1318
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1319 LRSQLAIIPQ--EPFLFSGTVRENL--DPQ--GLHKDRALWQA---LKQCHLSEVITSmggldgelgeggRS---LSLGQ 1386
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDIcfGPMnfGVSEEDAKQKAremIELVGLPEELLA------------RSpfeLSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1387 RQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1463
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
631-811 |
5.31e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.81 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 631 IVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----LSKGFGLATQEPWI----QFA------TIRDNILFG-KTFDAQL 694
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPPEKRRIgyvfQDArlfphyKVRGNLRYGmAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 695 YKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS 774
Cdd:PRK11144 109 FDKIVALLGIEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP--YLERLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 312176403 775 YTTR---LLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11144 176 REINipiLYVSHSlDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
621-806 |
5.68e-08 |
|
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: 54.89 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLvGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS---------KGFGLATQEP-WIQFATIRD-----NIL 685
Cdd:cd03264 21 LTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvlkqpqklrRRIGYLPQEFgVYPNFTVREfldyiAWL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 686 FG---KTFDAQLyKEVLEACALNDdlsilpagdqtEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVdaDVAN 762
Cdd:cd03264 100 KGipsKEVKARV-DEVLELVNLGD-----------RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL--DPEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 312176403 763 HLLHRCILGMLSYT-TRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:cd03264 166 RIRFRNLLSELGEDrIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1262-1466 |
6.14e-08 |
|
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: 57.14 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSS--GRVLLDGvdtSQLELAQLRSQ----LAIIPQEPFLFSG 1335
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSG---SPLKASNIRDTeragIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1336 -TVRENL-------DPQGLHKDRALwqaLKQCHlsEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDE 1407
Cdd:TIGR02633 93 lSVAENIflgneitLPGGRMAYNAM---YLRAK--NLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 1408 ATASVDQKTDQLLQQTIcKRFANKTV--LTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 1466
Cdd:TIGR02633 168 PSSSLTEKETEILLDII-RDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTM 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1263-1464 |
6.42e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 54.80 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP---SSGRVLLDGVDTSQLElAQLRsQLAIIPQEPFLFSG-TVR 1338
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP-AEQR-RIGILFQDDLLFPHlSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1339 ENL------DPQGLHKDRALWQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASV 1412
Cdd:COG4136 95 ENLafalppTIGRAQRRARVEQALEEAGLAGFADRDPA----------TLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1413 DQK-TDQLLQQtickrfanktVLTIAHRLN--TILNS-DRVLVLQAGRVVELDSPA 1464
Cdd:COG4136 165 DAAlRAQFREF----------VFEQIRQRGipALLVThDEEDAPAAGRVLDLGNWQ 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1263-1459 |
6.82e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.14 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGV--DTS------QLELAQLRSQLAIIPQEPFLFS 1334
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItiDTArslsqqKGLIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1335 G-TVRENL--DP---QGLHKDRALwqALKQCHLSEVITSmggldGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEA 1408
Cdd:PRK11264 99 HrTVLENIieGPvivKGEPKEEAT--ARARELLAKVGLA-----GKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1409 TASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 1459
Cdd:PRK11264 172 TSALDPELVGEVLNTI-RQLAqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
621-821 |
7.34e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.40 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG------------LSKGFGLATQEP--WIQFATIRDNILF 686
Cdd:PRK13638 22 LDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpldyskrgllaLRQQVATVFQDPeqQIFYTDIDSDIAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 687 G----KTFDAQLYKEVLEACALNDDLSILPAGDQTevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN 762
Cdd:PRK13638 102 SlrnlGVPEAEITRRVDEALTLVDAQHFRHQPIQC--------LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 763 HLLH--RCILGMLSYTtrLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEILPLVQAVPKA 821
Cdd:PRK13638 174 QMIAiiRRIVAQGNHV--IISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEAMEQA 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
621-790 |
7.62e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.43 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIaGELHRLRGHVAVRGLSKGFGLATQEPWIQFATIRDNI--LFGKT--FDAQLYK 696
Cdd:PRK14258 28 MEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYERRVNLNRLRRQVsmVHPKPnlFPMSVYD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 697 EVLEACALN--------DDL--SILPAGD-----QTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 761
Cdd:PRK14258 107 NVAYGVKIVgwrpkleiDDIveSALKDADlwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAS 186
|
170 180 190
....*....|....*....|....*....|..
gi 312176403 762 ---NHLLHRciLGMLSYTTRLLCTHRTEYLER 790
Cdd:PRK14258 187 mkvESLIQS--LRLRSELTMVIVSHNLHQVSR 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
621-812 |
7.76e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.14 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAI---------------------------AGELHRLRGHVAVrgLSKGFGLATQEp 673
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirvgditidtarslsqqKGLIRQLRQHVGF--VFQNFNLFPHR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 674 wiqfaTIRDNILFGKTFDAQLYKEvlEACALNDDL--SILPAGDQTEVGEKgvtLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:PRK11264 101 -----TVLENIIEGPVIVKGEPKE--EATARARELlaKVGLAGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 752 PLAAVDADVANHLLHrCILGMLSYT-TRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK11264 171 PTSALDPELVGEVLN-TIRQLAQEKrTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
561-802 |
8.12e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.90 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 561 LLEAKVSLDRIQLFlDLpnhnpqAYYSPD---PPAEPS-TVLELHGALFSWDPVGTSLETFisHLEVKKGMLVGIVGKVG 636
Cdd:PRK10522 289 LLSAQVAFNKLNKL-AL------APYKAEfprPQAFPDwQTLELRNVTFAYQDNGFSVGPI--NLTIKRGELLFLIGGNG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 637 CGKSSLLAAIAGELHRLRGHVAVRGlsKGFGLATQEPWIQ-FATI-RDNILFGKTFDAQlyKEVLEACALNDDLSILPAG 714
Cdd:PRK10522 360 SGKSTLAMLLTGLYQPQSGEILLDG--KPVTAEQPEDYRKlFSAVfTDFHLFDQLLGPE--GKPANPALVEKWLERLKMA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 715 DQTEVGEKGVT---LSGGQRARIALARAVYQEKELYLLDDplAAVDAD-VANHLLHRCILGMLSYT--TRLLCTHRTEYL 788
Cdd:PRK10522 436 HKLELEDGRISnlkLSKGQKKRLALLLALAEERDILLLDE--WAADQDpHFRREFYQVLLPLLQEMgkTIFAISHDDHYF 513
|
250
....*....|....
gi 312176403 789 ERADAVLLMEAGRL 802
Cdd:PRK10522 514 IHADRLLEMRNGQL 527
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1261-1469 |
9.23e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.86 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1261 NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL---------RSQL-------- 1323
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFArrigvvfgqRSQLwwdlpaid 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1324 ------AI--IPQEPFlfsgtvRENLDpqglhkdrALWQALkqcHLSEVITSMggldgelgegGRSLSLGQRQLLCLARA 1395
Cdd:COG4586 116 sfrllkAIyrIPDAEY------KKRLD--------ELVELL---DLGELLDTP----------VRQLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 1396 LLTDAKILCIDEATASVD----QKTDQLLQQtICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDvvskEAIREFLKE-YNRER-GTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1258-1459 |
1.05e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.64 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1258 GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG------VDTSQLELAQLRSQLAIIPQE-- 1329
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1330 --PFLfsgTVRENL--DP---QGLHKDRALWQA---LKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTD 1399
Cdd:PRK11124 93 lwPHL---TVQQNLieAPcrvLGLSKDQALARAeklLERLRLKPYADRFPL----------HLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 1400 AKILCIDEATASVDQK-TDQL------LQQTickrfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 1459
Cdd:PRK11124 160 PQVLLFDEPTAALDPEiTAQIvsiireLAET------GITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
938-1045 |
1.07e-07 |
|
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: 55.24 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 938 LLLFSPGNLYIPVFP---LPKAAPNGS-SDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPV 1013
Cdd:cd18572 5 LVVAALSELAIPHYTgavIDAVVADGSrEAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDI 84
|
90 100 110
....*....|....*....|....*....|..
gi 312176403 1014 TFFNATPTGRILNRFSSDVACADDSLPFILNI 1045
Cdd:cd18572 85 AFFDATKTGELTSRLTSDCQKVSDPLSTNLNV 116
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
621-809 |
1.12e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.13 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFGK 688
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGrevnaenekwVRSKVGLVFQDPDDQVfsSTVWDDVAFGP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 689 TFDAQLYKEVLEAcaLNDDLSILpagDQTEVGEKG-VTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLlhR 767
Cdd:PRK13647 106 VNMGLDKDEVERR--VEEALKAV---RMWDFRDKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL--M 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 312176403 768 CILGMLSY--TTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPS 809
Cdd:PRK13647 179 EILDRLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKS 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1263-1471 |
1.15e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.66 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSS-----GRVLLDG--VDTSQLELAQLRSQLAIIPQEPFLFSG 1335
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNqnIYERRVNLNRLRRQVSMVHPKPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1336 TVRENL---------DPQgLHKDRALWQALKQCHLSEVITSMGGLDGElgeggrSLSLGQRQLLCLARALLTDAKILCID 1406
Cdd:PRK14258 103 SVYDNVaygvkivgwRPK-LEIDDIVESALKDADLWDEIKHKIHKSAL------DLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 1407 EATASVD----QKTDQLLQQTICKrfANKTVLTIAHRLNTILN-SDRVLVLQA-----GRVVELDSPATLRNQPH 1471
Cdd:PRK14258 176 EPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGLTKKIFNSPH 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
621-757 |
1.16e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.18 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----------LSKGFGLAT----QEPWIQFATIRDNI- 684
Cdd:COG1129 273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpvrirsprdaIRAGIAYVPedrkGEGLVLDLSIRENIt 352
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 685 --LFGKTFDAQLY---KEVLEACALNDDLSILPAGDQTEVGekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:COG1129 353 laSLDRLSRGGLLdrrRERALAEEYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
629-832 |
1.22e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.81 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 629 VGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFGKT---FDAQ 693
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenireVRKFVGLVFQNPDDQIfsPTVEQDIAFGPInlgLDEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 694 LYK----EVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcI 769
Cdd:PRK13652 113 TVAhrvsSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID--F 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 770 LGMLSYT---TRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEI-------------LPLVQAVPKAWAENGQESDSA 832
Cdd:PRK13652 180 LNDLPETygmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIflqpdllarvhldLPSLPKLIRSLQAQGIAIDMA 259
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
715-812 |
1.58e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.20 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 715 DQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSY--TTRLLCTHRTEYLERAD 792
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEegKTMVVVTHEMGFARHVS 219
|
90 100
....*....|....*....|.
gi 312176403 793 A-VLLMEAGRLIRAGPPSEIL 812
Cdd:PRK10619 220 ShVIFLHQGKIEEEGAPEQLF 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
621-811 |
2.52e-07 |
|
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: 55.19 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLaaiagelHRLRG-------------HVA-------VRGLSK--------GFGLATQE 672
Cdd:TIGR03269 21 FTIEEGEVLGILGRSGAGKSVLM-------HVLRGmdqyeptsgriiyHVAlcekcgyVERPSKvgepcpvcGGTLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 673 P--WIQFATIRDN------ILFGKTFdaQLYKE--VLEAC--ALND-----DLSILPAGD---QTEVGEK----GVTLSG 728
Cdd:TIGR03269 94 VdfWNLSDKLRRRirkriaIMLQRTF--ALYGDdtVLDNVleALEEigyegKEAVGRAVDlieMVQLSHRithiARDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 729 GQRARIALARAVYQEKELYLLDDPLAAVDADVANhLLHRCILGML--SYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRA 805
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLENGEIKEE 250
|
....*.
gi 312176403 806 GPPSEI 811
Cdd:TIGR03269 251 GTPDEV 256
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1273-1467 |
2.68e-07 |
|
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: 53.57 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1273 GEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSqlelaqLRSQlAIIPQepflFSGTVRENL-DPQGLHKDRA 1351
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------YKPQ-YIKAD----YEGTVRDLLsSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1352 LWQalkqchlSEVITSMgGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKtDQLLQQTICKRFA-- 1429
Cdd:cd03237 94 YFK-------TEIAKPL-QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKVIRRFAen 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 312176403 1430 -NKTVLTIAHRLNTI-LNSDRVLVL--QAGRVVELDSPATLR 1467
Cdd:cd03237 165 nEKTAFVVEHDIIMIdYLADRLIVFegEPSVNGVANPPQSLR 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
621-758 |
3.05e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH------RLRGhVAVRGLSKGFGLATQE----PWiqfATIRDNILFGKTF 690
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDG-KPVEGPGAERGVVFQNegllPW---RNVQDNVAFGLQL 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 691 dAQLYKEVLEACALnddlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:PRK11248 98 -AGVEKMQRLEIAH----QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1257-1459 |
3.17e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1257 PGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQLAIIPQEPFLfs 1334
Cdd:PRK11248 12 GGKP-ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpVEGPGAERGVVFQNEGLLPWRNVQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1335 GTVRENLDPQGLHKDRAL---WQALKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATAS 1411
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLeiaHQMLKKVGLEG----------AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312176403 1412 VDQKTDQLLQQTICKRFAN--KTVLTIAHRLNTILNSDRVLVLQA---GRVVE 1459
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQEtgKQVLLITHDIEEAVFMATELVLLSpgpGRVVE 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1262-1463 |
3.43e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.86 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL-DGVDTSQL----ELAQLRSQLAIIPQEP--FLFS 1334
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgDYAIPANLkkikEVKRLRKEIGLVFQFPeyQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1335 GTVRENL--DPQGLHKDRAlwQALKQchLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASV 1412
Cdd:PRK13645 106 ETIEKDIafGPVNLGENKQ--EAYKK--VPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1413 DQKTDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1463
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSP 235
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
623-806 |
3.87e-07 |
|
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: 52.17 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 623 VKKGMLVGIVGKVGCGKSSLLAAIAGEL--HRLRGHVAVRG-------LSKGFGLATQEPwIQFA--TIRDNILFGktfd 691
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGrpldkrsFRKIIGYVPQDD-ILHPtlTVRETLMFA---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 692 AQLykevleacalnddlsilpagdqtevgeKGvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILG 771
Cdd:cd03213 107 AKL---------------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS--LLR 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 312176403 772 MLSYTTR-LLCT-H--RTEYLERADAVLLMEAGRLIRAG 806
Cdd:cd03213 156 RLADTGRtIICSiHqpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1262-1463 |
6.06e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.32 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL------DGVDTSQLELA----------QLRSQLAI 1325
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELITNpyskkiknfkELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEP--FLFSGTVRENL--DP--QGLHKDRALWQALKqcHLSEvitsMGGLDGELGEGGRSLSLGQRQLLCLARALLTD 1399
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDImfGPvaLGVKKSEAKKLAKF--YLNK----MGLDDSYLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1400 AKILCIDEATASVDQKTDQLLQQTICKRFA-NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1463
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
621-761 |
6.13e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.71 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAG--------ELH-RLRGHVA------VRGLSKGFG----LATQEPWIQFATIR 681
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksaGSHiELLGRTVqregrlARDIRKSRAntgyIFQQFNLVNRLSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 682 DNILFGKTFDAQLYKEVLEACALNDDLSILPAgdQTEVG------EKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK09984 105 ENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
....*.
gi 312176403 756 VDADVA 761
Cdd:PRK09984 183 LDPESA 188
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
629-803 |
6.35e-07 |
|
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: 50.45 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 629 VGIVGKVGCGKSSLLAAIAGELHRLRGHVavrglskgfglatqepwiqfatirdnilfgKTFDAQLYKEVLEACALNddl 708
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGV------------------------------IYIDGEDILEEVLDQLLL--- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 709 silpagdqTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGML-----SYTTRLLCTH 783
Cdd:smart00382 52 --------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllksEKNLTVILTT 123
|
170 180
....*....|....*....|
gi 312176403 784 RTEYLERADAVLLMEAGRLI 803
Cdd:smart00382 124 NDEKDLGPALLRRRFDRRIV 143
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
621-812 |
6.68e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------------LSKGFGLATQEP-WIQFATIRDN 683
Cdd:PRK14246 31 IKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyfgkdifqidaikLRKEVGMVFQQPnPFPHLSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 684 ILF----GKTFDAQLYKEVLEACalnddlsILPAGDQTEVGEK----GVTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK14246 111 IAYplksHGIKEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 756 VDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK14246 184 IDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
608-812 |
7.03e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.50 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 608 DPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGfglATQEPWIQFATIRDNILFG 687
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIA---KISDAELREVRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 KTFDAQLYKEVLEACALNDDLSILPAGDQTE--------VGEKGVT------LSGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:PRK10070 113 QSFALMPHMTVLDNTAFGMELAGINAEERREkaldalrqVGLENYAhsypdeLSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 754 AAVDADVANHLLHRCI-LGMLSYTTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK10070 193 SALDPLIRTEMQDELVkLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1261-1462 |
7.48e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.88 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1261 NALDGVTFCVQPGEKLGIVGRTGSGKSSLllvlfrllepssGRVLLDgvdtsqLELAQLRSQLAIIPQEPFLFSGTVREN 1340
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTL------------LRLLAG------ALKGTPVAGCVDVPDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 LDPQGLHKDRAlwQALKQCHLSEVITsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLL 1420
Cdd:COG2401 106 IGRKGDFKDAV--ELLNAVGLSDAVL--------WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 312176403 1421 Q---QTICKRfANKTVLTIAHRLNTI--LNSDRVLVLQAGRVVELDS 1462
Cdd:COG2401 176 ArnlQKLARR-AGITLVVATHHYDVIddLQPDLLIFVGYGGVPEEKR 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
631-795 |
7.93e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.64 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 631 IVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----LS-----KGFGLATQEPWIQFATIRDNILfgktFDAQLYKEVLE 700
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistLKpeiyrQQVSYCAQTPTLFGDTVYDNLI----FPWQIRNQQPD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 701 ACALNDDLSI--LPagdqTEVGEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDAD---VANHLLHRcilgmls 774
Cdd:PRK10247 114 PAIFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESnkhNVNEIIHR------- 182
|
170 180
....*....|....*....|....*.
gi 312176403 775 YTTR-----LLCTHRTEYLERADAVL 795
Cdd:PRK10247 183 YVREqniavLWVTHDKDEINHADKVI 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
620-759 |
9.10e-07 |
|
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: 51.21 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGFGLATQE-PWIQFA-------TIRDNILFGKT 689
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtpLAEQRDEPHENiLYLGHLpglkpelSALENLHFWAA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176403 690 F--DAQLY-KEVLEACALNDdLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:TIGR01189 100 IhgGAQRTiEDALAAVGLTG-FEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1262-1466 |
9.24e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.10 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVqPGEKL--------------GIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIP 1327
Cdd:PRK10575 13 ALRNVSFRV-PGRTLlhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1328 QE-PFLFSGTVREnLDPQG---LHKDRALWQALKQCHLSEVITsMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKIL 1403
Cdd:PRK10575 92 QQlPAAEGMTVRE-LVAIGrypWHGALGRFGAADREKVEEAIS-LVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1404 CIDEATASVD--QKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 1466
Cdd:PRK10575 170 LLDEPTSALDiaHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEL 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1247-1469 |
9.42e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.11 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1247 EFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ-LAI 1325
Cdd:COG3845 259 EVENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLF----SGTVRENL-----DPQGLHKDRAL-WQALKQcHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARA 1395
Cdd:COG3845 338 IPEDRLGRglvpDMSVAENLilgryRRPPFSRGGFLdRKAIRA-FAEELIEEFDVRTPGPDTPARSLSGGNQQKVILARE 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 1396 LLTDAKILCIDEATASVDQK-TDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV-ELDSPATLRNQ 1469
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGaIEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEATREE 493
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
621-812 |
1.06e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH--------RLRGHVAVRG----------LSKGFGLATQEPWIQFA-TIR 681
Cdd:PRK13547 22 LRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGeplaaidaprLARLRAVLPQAAQPAFAfSAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 682 DNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQ---------EKELYLLDDP 752
Cdd:PRK13547 102 EIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 753 LAAVDadvanhllhrcilgmLSYTTRLLCTHRTEYLE-----------------RADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13547 182 TAALD---------------LAHQHRLLDTVRRLARDwnlgvlaivhdpnlaarHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1266-1457 |
1.07e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1266 VTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAIIP---QEPFLF-SGTVREN 1340
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYlDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 LDPQgLHKDRALWQALKQ--CHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 1418
Cdd:PRK15439 362 VCAL-THNRRGFWIKPARenAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 312176403 1419 LLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRV 1457
Cdd:PRK15439 441 DIYQLI-RSIAaqNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
626-758 |
1.18e-06 |
|
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: 50.95 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 626 GMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVavrgLSKGFGLATQEPWIQfatirDNILFGKTFDAqlYKEVLEA---- 701
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----LLNGGPLDFQRDSIA-----RGLLYLGHAPG--IKTTLSVlenl 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 702 ---CALNDDLSILPAGDQteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:cd03231 95 rfwHADHSDEQVEEALAR--VGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1264-1470 |
1.21e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.62 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1264 DGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP----SSGRVLLDGVdtsQLELAQLRSQL-AIIPQEP-------F 1331
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRGRKiATIMQNPrsafnplH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1332 LFSGTVRENLDPQGLHKDRA-LWQALKQCHLSEVITSMGGLDGelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATA 1410
Cdd:PRK10418 97 TMHTHARETCLALGKPADDAtLTAALEAVGLENAARVLKLYPF-------EMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312176403 1411 SVD----QKTDQLLQQTICKRfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:PRK10418 170 DLDvvaqARILDLLESIVQKR--ALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1263-1457 |
1.29e-06 |
|
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: 52.90 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS-SGRVLLDG--VDTSQLELAqLRSQLAIIPQE-------PFL 1332
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQA-IRAGIAMVPEDrkrhgivPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1333 fsgTVRENLDPQGLHKDRALWQ---ALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEAT 1409
Cdd:TIGR02633 355 ---GVGKNITLSVLKSFCFKMRidaAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 1410 ASVD--------QKTDQLLQQTIckrfankTVLTIAHRLNTILN-SDRVLVLQAGRV 1457
Cdd:TIGR02633 432 RGVDvgakyeiyKLINQLAQEGV-------AIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
594-812 |
1.33e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.77 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 594 PSTVLELHGALFSWdPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG------------ 661
Cdd:PRK13636 2 EDYILKVEELNYNY-SDGTHALKGIN-INIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 662 LSKGFGLATQEPwiqfatirDNILFgktfDAQLYKEVlEACALNDDLSilpagdQTEVGEK--------GVT-------- 725
Cdd:PRK13636 80 LRESVGMVFQDP--------DNQLF----SASVYQDV-SFGAVNLKLP------EDEVRKRvdnalkrtGIEhlkdkpth 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 726 -LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhRCILGMLSYT--TRLLCTHRTEYLE-RADAVLLMEAGR 801
Cdd:PRK13636 141 cLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM-KLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGR 219
|
250
....*....|.
gi 312176403 802 LIRAGPPSEIL 812
Cdd:PRK13636 220 VILQGNPKEVF 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
622-759 |
1.46e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.64 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 622 EVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFG--------LATQEPWIQFATIRDNILFGKTFDAQ 693
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPdvaeachyLGHRNAMKPALTVAENLEFWAAFLGG 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 694 LYKEVLEA-CALN-DDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:PRK13539 104 EELDIAAAlEAVGlAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1264-1457 |
1.57e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1264 DGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE-PSSGRVLLDG--VDTSQLELAqLRSQLAIIPQE-------PFLf 1333
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQA-IAQGIAMVPEDrkrdgivPVM- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1334 sgTVRENLDPQGLH---KDRALWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATA 1410
Cdd:PRK13549 357 --GVGKNITLAALDrftGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1411 SVD--------QKTDQLLQQTICkrfanktVLTIAHRLNTILN-SDRVLVLQAGRV 1457
Cdd:PRK13549 435 GIDvgakyeiyKLINQLVQQGVA-------IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
621-757 |
1.81e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.42 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGL----------ATQEPWIQFATIRDNILFG--- 687
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALqknlvayvpqSEEVDWSFPVLVEDVVMMGryg 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 688 --------KTFDAQLYKEVLEACALNDDlsilpagDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:PRK15056 108 hmgwlrraKKRDRQIVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
623-811 |
1.95e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.27 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 623 VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFG--- 687
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdIRHKIGMVFQNPDNQFvgATVEDDVAFGlen 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 KTFDAQLYKE-VLEACALnddlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLH 766
Cdd:PRK13650 110 KGIPHEEMKErVNEALEL--------VGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 312176403 767 -----RCILGMlsytTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13650 182 tikgiRDDYQM----TVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1262-1469 |
2.09e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.43 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLElAQLR----SQlaiipqepfLFS- 1334
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIA-TRRRvgymSQ---------AFSl 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1335 -G--TVRENLDpqgLH-------KDRA---LWQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAK 1401
Cdd:NF033858 351 yGelTVRQNLE---LHarlfhlpAAEIaarVAEMLERFDLADVADALPD----------SLPLGIRQRLSLAVAVIHKPE 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 1402 ILCIDEATASVD-QKTDQLLQQTIckRFANKTVLTI---AHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:NF033858 418 LLILDEPTSGVDpVARDMFWRLLI--ELSREDGVTIfisTHFMNEAERCDRISLMHAGRVLASDTPAALVAA 487
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
621-812 |
2.21e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 51.34 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGFGLATQEPWI--QFA------TIRDNIL-FGKT 689
Cdd:PRK13537 28 FHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepVPSRARHARQRVGVvpQFDnldpdfTVRENLLvFGRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 690 F---DAQLYKEV---LEacalnddLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANH 763
Cdd:PRK13537 108 FglsAAAARALVpplLE-------FAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 312176403 764 LLHRCILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13537 176 LMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1263-1456 |
2.65e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSS--GRVLLDGVDTSQlelaQLRSQLAIIPQEPFLFSG-TVRE 1339
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDILYPHlTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1340 NLD-------PQGLHKDRALWQAlkQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASV 1412
Cdd:PLN03211 160 TLVfcsllrlPKSLTKQEKILVA--ESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 312176403 1413 DQKTDQLLQQTICKrFAN--KTVLTIAHRLNTILNS--DRVLVLQAGR 1456
Cdd:PLN03211 238 DATAAYRLVLTLGS-LAQkgKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
620-757 |
3.32e-06 |
|
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: 50.10 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGML-----VGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFglATQEPWIQFATIRDNILFGKTFD--- 691
Cdd:cd03237 14 TLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY--KPQYIKADYEGTVRDLLSSITKDfyt 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 692 -AQLYKEVLeacalnDDLSILPAGDQtEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:cd03237 92 hPYFKTEIA------KPLQIEQILDR-EVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
621-812 |
3.46e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.37 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV----------AVRGLSKGFGLATQEPWIQF-ATIRDNILFGKT 689
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyASKEVARRIGLLAQNATTPGdITVQELVARGRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 690 FDAQLY----KEVLEACAlnddlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL 764
Cdd:PRK10253 108 PHQPLFtrwrKEDEEAVT-----KAMQATGITHLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 312176403 765 LHrcILGMLS----YTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK10253 183 LE--LLSELNrekgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1250-1461 |
3.90e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.17 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1250 DVVLAYRpGL--PNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAII 1326
Cdd:COG1129 254 EVVLEVE-GLsvGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1327 P----QEPFLFSGTVRENLDPQGLHK-------DRALWQALkqchLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARA 1395
Cdd:COG1129 333 PedrkGEGLVLDLSIRENITLASLDRlsrggllDRRRERAL----AEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1396 LLTDAKILCIDEATASVD--QKTD--QLLQQtickrFAN--KTVLTIAHRLNTIL-NSDRVLVLQAGRVV-ELD 1461
Cdd:COG1129 409 LATDPKVLILDEPTRGIDvgAKAEiyRLIRE-----LAAegKAVIVISSELPELLgLSDRILVMREGRIVgELD 477
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
621-757 |
4.06e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.04 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLL------------AAIAGELhRLRGH---------VAVRglsKGFGLATQEPwIQFA- 678
Cdd:COG1117 32 LDIPENKVTALIGPSGCGKSTLLrclnrmndlipgARVEGEI-LLDGEdiydpdvdvVELR---RRVGMVFQKP-NPFPk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 679 TIRDNILFG--------KTFDAQLYKEVLEACALNDdlsilpagdqtEV----GEKGVTLSGGQRARIALARAVYQEKEL 746
Cdd:COG1117 107 SIYDNVAYGlrlhgiksKSELDEIVEESLRKAALWD-----------EVkdrlKKSALGLSGGQQQRLCIARALAVEPEV 175
|
170
....*....|.
gi 312176403 747 YLLDDPLAAVD 757
Cdd:COG1117 176 LLMDEPTSALD 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
623-862 |
4.19e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 623 VKKGMLVGIVGKVGCGKSSLLA------------AIAGELHRLRgHVAVRGLSKGFGLATQEPWIQFATIRDNILFG--- 687
Cdd:PTZ00265 408 LTEGKTYAFVGESGCGKSTILKlierlydptegdIIINDSHNLK-DINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlys 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 -------------KTFDAQLYKEVLEACA------------------------------------------LNDDLSILP 712
Cdd:PTZ00265 487 lkdlealsnyyneDGNDSQENKNKRNSCRakcagdlndmsnttdsneliemrknyqtikdsevvdvskkvlIHDFVSALP 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 713 AGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDaDVANHLLHRCILGMLSYTTR--LLCTHRTEYLER 790
Cdd:PTZ00265 567 DKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRitIIIAHRLSTIRY 645
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 791 ADAVLLMeAGRliRAGPPSEILPLVQAVPKAWAENGQESDSATAQSVQNPEKTKEGLEE----EQSTSGRLLQEES 862
Cdd:PTZ00265 646 ANTIFVL-SNR--ERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGsyiiEQGTHDALMKNKN 718
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
625-792 |
4.22e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 625 KGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPWIQFA----------TIRDNILFGKTFDAQL 694
Cdd:PRK13540 26 AGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVghrsginpylTLRENCLYDIHFSPGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 695 YkEVLEACALN--DDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLL-----HR 767
Cdd:PRK13540 106 V-GITELCRLFslEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIItkiqeHR 174
|
170 180
....*....|....*....|....*
gi 312176403 768 CILGMLsyttrLLCTHRTEYLERAD 792
Cdd:PRK13540 175 AKGGAV-----LLTSHQDLPLNKAD 194
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
621-812 |
4.23e-06 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 49.61 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAG---------------------ELHRLRGHVavrglskgfGLATQepwiQF-- 677
Cdd:COG1126 22 LDVEKGEVVVIIGPSGSGKSTLLRCINLleepdsgtitvdgedltdskkDINKLRRKV---------GMVFQ----QFnl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 678 ---ATIRDNILFGKTFDAQLYKEVLEACALNddlsILpagDQTEVGEKG----VTLSGGQRARIALARAVYQEKELYLLD 750
Cdd:COG1126 89 fphLTVLENVTLAPIKVKKMSKAEAEERAME----LL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176403 751 DPLAAVD-------ADVANHLLHRcilGMlsytTRLLCTH-----RteylERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1126 162 EPTSALDpelvgevLDVMRDLAKE---GM----TMVVVTHemgfaR----EVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1262-1457 |
5.07e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.63 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLfrllepsSGRVLLDGVDTSQLEL----AQLRSQLA------------I 1325
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSAGSHIELlgrtVQREGRLArdirksrantgyI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSGTVRENLDPQGLHKD---RALWQALKQCHLSEVITSMGGLDGELGEGGR--SLSLGQRQLLCLARALLTDA 1400
Cdd:PRK09984 92 FQQFNLVNRLSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRvsTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176403 1401 KILCIDEATASVDQKTDQLLQQTIckRFANK----TVLTIAHRLNTILN-SDRVLVLQAGRV 1457
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTL--RDINQndgiTVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1264-1452 |
5.59e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.65 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1264 DGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLaiipqepfLFSG-------- 1335
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDL--------LYLGhqpgikte 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1336 -TVRENLD-PQGLH---KDRALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATA 1410
Cdd:PRK13538 89 lTALENLRfYQRLHgpgDDEALWEALAQVGLAGF----------EDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 312176403 1411 SVDQKTDQLLQQTICKRFANK--TVLTIAHRLNTILNSDRVLVL 1452
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGgmVILTTHQDLPVASDKVRKLRL 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1263-1463 |
6.79e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 49.29 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLldgvdTSQLELAQLRSQLAIIPQEPFLFS-GTVREN- 1340
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQDARLLPwKKVIDNv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 -LDPQGLHKDRALwQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 1419
Cdd:PRK11247 103 gLGLKGQWRDAAL-QALAAVGLADRANEWPA----------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 312176403 1420 LQQTICKRFANK--TVLTIAHRLN-TILNSDRVLVLQAGRV-----VELDSP 1463
Cdd:PRK11247 172 MQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKIgldltVDLPRP 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
621-820 |
7.50e-06 |
|
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: 50.45 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAI------AGE-------LHRLRGHvAVRGLSKGFGLATQEPwiqFA------TIR 681
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLGLALlrlipsEGEirfdgqdLDGLSRR-ALRPLRRRMQVVFQDP---FGslsprmTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 682 D------NILFGKTFDAQLYKEVLEACAlnddlsilpagdqtEVGEKGVTL-------SGGQRARIALARAVYQEKELYL 748
Cdd:COG4172 383 QiiaeglRVHGPGLSAAERRARVAEALE--------------EVGLDPAARhryphefSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 749 LDDPLAAVDADVANHLL---------HRcilgmLSYttrLLCTH-----RteYLerADAVLLMEAGRLIRAGPPSEIL-- 812
Cdd:COG4172 449 LDEPTSALDVSVQAQILdllrdlqreHG-----LAY---LFISHdlavvR--AL--AHRVMVMKDGKVVEQGPTEQVFda 516
|
250
....*....|....*
gi 312176403 813 P-------LVQAVPK 820
Cdd:COG4172 517 PqhpytraLLAAAPL 531
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
621-812 |
8.28e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.24 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWI-QFATIRDNILFGKT 689
Cdd:PRK11231 23 LSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqLARRLALLPQHHLTpEGITVRELVAYGRS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 690 FDAQLYKEVleacALNDDLSILPAGDQTEV---GEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDadvANH-- 763
Cdd:PRK11231 103 PWLSLWGRL----SAEDNARVNQAMEQTRInhlADRRLTdLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD---INHqv 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312176403 764 -LLHrcILGMLSYTTRLLCT--HRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK11231 176 eLMR--LMRELNTQGKTVVTvlHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
623-813 |
8.83e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 49.41 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 623 VKKGMLVGIVGKVGCGKSSLLAAIAGEL---HRLRGHVAVRGLSKG----------FGLATQEPWIQF--ATIRDNILFG 687
Cdd:PRK13640 30 IPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTaktvwdirekVGIVFQNPDNQFvgATVGDDVAFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 KTFDA-------QLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADV 760
Cdd:PRK13640 110 LENRAvprpemiKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 761 ANHLLHRCI-LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILP 813
Cdd:PRK13640 179 KEQILKLIRkLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1246-1456 |
1.17e-05 |
|
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: 46.67 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSlllvlfrllepssgrvLLDgvdtsqlelaqlrsqlaI 1325
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKST----------------LLK-----------------L 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEPFLFSGTVRENldpqglhkdralwQALKQCHLSEvitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKILCI 1405
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYFEQ------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1406 DEATASVDQKTDQLLQQTIcKRFaNKTVLTIAH-R--LNTIlnSDRVLVLQAGR 1456
Cdd:cd03221 95 DEPTNHLDLESIEALEEAL-KEY-PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
621-811 |
1.18e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.54 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGEL----HRLRGHVAVRGLS------KGFGLAT--QEPWIQF---ATIRDNIL 685
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPvapcalRGRKIATimQNPRSAFnplHTMHTHAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 686 -----FGKTFDAQLYKEVLEACALNDDLSILPAgdqtevgeKGVTLSGG--QRARIALarAVYQEKELYLLDDPLAAVDA 758
Cdd:PRK10418 104 etclaLGKPADDATLTAALEAVGLENAARVLKL--------YPFEMSGGmlQRMMIAL--ALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176403 759 DVANH---LLHRCI----LGMlsyttrLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK10418 174 VAQARildLLESIVqkraLGM------LLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1263-1459 |
1.76e-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: 47.14 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLF--RLLEPSSGRVLLDGVDTSQLElAQLRSQLAII--PQEPFLFSGtVR 1338
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLP-PEERARLGIFlaFQYPPEIPG-VK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1339 enldpqglhkdralwqalkqchLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 1418
Cdd:cd03217 94 ----------------------NADFLRYVNE----------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 312176403 1419 LLQQTICK-RFANKTVLTIAHRLNtILN---SDRVLVLQAGRVVE 1459
Cdd:cd03217 142 LVAEVINKlREEGKSVLIITHYQR-LLDyikPDRVHVLYDGRIVK 185
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
624-814 |
1.80e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 49.28 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 624 KKGMLVGIVGKVGCGKSSLLAAIAgelHRLRGHVAVRGLSKGFGLATQEPWIQ----FA----------TIRDNILFGKT 689
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALA---FRSPKGVKGSGSVLLNGMPIDAKEMRaisaYVqqddlfiptlTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 690 F--DAQLYKE--VLEACALNDDLSILPAGDqTEVGEKGVT--LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH 763
Cdd:TIGR00955 126 LrmPRRVTKKekRERVDEVLQALGLRKCAN-TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 764 LLhRCILGMLSYTTRLLCT-HR--TEYLERADAVLLMEAGRLIRAGPPSEILPL 814
Cdd:TIGR00955 205 VV-QVLKGLAQKGKTIICTiHQpsSELFELFDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
622-802 |
2.11e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.50 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 622 EVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGFGLATQE------PWI-QFA------TIRDNI-- 684
Cdd:PRK11629 31 SIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpMSKLSSAAKAElrnqklGFIyQFHhllpdfTALENVam 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 685 --LFGKTFDAQLYKEVLEACAlnddlsilPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN 762
Cdd:PRK11629 111 plLIGKKKPAEINSRALEMLA--------AVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 312176403 763 HLLHrcILGMLSY---TTRLLCTHRTEYLERADAVLLMEAGRL 802
Cdd:PRK11629 183 SIFQ--LLGELNRlqgTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
621-812 |
2.16e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.60 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAG--ELH---RLRGHVAVRG----------LSKGFGLATQEP-WIQFATIRDNI 684
Cdd:PRK14247 24 LEIPDNTITALMGPSGSGKSTLLRVFNRliELYpeaRVSGEVYLDGqdifkmdvieLRRRVQMVFQIPnPIPNLSIFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 685 LFGKTFD---------AQLYKEVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK14247 104 ALGLKLNrlvkskkelQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 756 VDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK14247 177 LDP-ENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVF 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1257-1461 |
2.64e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1257 PGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLfrllepS--------SGRVLLDGvdtsqlELAQLRS------- 1321
Cdd:NF040905 12 PGVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVL------SgvyphgsyEGEILFDG------EVCRFKDirdseal 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1322 QLAIIPQE----PFLfsgTVRENL------------D-PQGLHKDRALwqaLKQCHLSE----VITSmggldgelgeggr 1380
Cdd:NF040905 79 GIVIIHQElaliPYL---SIAENIflgnerakrgviDwNETNRRAREL---LAKVGLDEspdtLVTD------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1381 sLSLGQRQLLCLARALLTDAKILCIDEATASV-DQKTDQLLQqtICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGR 1456
Cdd:NF040905 140 -IGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD--LLLELKAQgiTSIIISHKLNEIRRvADSITVLRDGR 216
|
....*.
gi 312176403 1457 VVE-LD 1461
Cdd:NF040905 217 TIEtLD 222
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
961-1045 |
2.68e-05 |
|
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: 47.94 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 961 SSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLP 1040
Cdd:cd18557 32 LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVT 111
|
....*
gi 312176403 1041 FILNI 1045
Cdd:cd18557 112 DNLSQ 116
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
610-812 |
3.05e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.23 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 610 VGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAG---------------------ELHRLRGHvavrgLSKGFGL 668
Cdd:PRK03695 8 VSTRLGPL--SAEVRAGEILHLVGPNGAGKSTLLARMAGllpgsgsiqfagqpleawsaaELARHRAY-----LSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 669 ATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSilpagdqTEVGekgvTLSGGQRARIALARAVYQ------ 742
Cdd:PRK03695 81 PFAMPVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLG-------RSVN----QLSGGEWQRVRLAAVVLQvwpdin 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 743 -EKELYLLDDPLAAVD-ADVA--NHLLHR-CILGMlsytTRLLCTH---RTeyLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK03695 150 pAGQLLLLDEPMNSLDvAQQAalDRLLSElCQQGI----AVVMSSHdlnHT--LRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
974-1031 |
3.07e-05 |
|
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: 47.63 E-value: 3.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 974 IAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSD 1031
Cdd:cd18780 51 VVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSD 108
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1266-1458 |
3.40e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.23 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1266 VTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLePSSGRVLLDGVDTSQL---ELAQLRSQLAiiPQEPFLFSGTVRENLD 1342
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWsaaELARHRAYLS--QQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1343 ---PQGLHKDRAlwqalkQCHLSEViTSMGGLDGELGEGGRSLSLGQRQLLCLARALLT-------DAKILCIDEATASV 1412
Cdd:PRK03695 92 lhqPDKTRTEAV------ASALNEV-AEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 312176403 1413 D--QKT--DQLLQQtICKrfANKTVLTIAHRLN-TILNSDRVLVLQAGRVV 1458
Cdd:PRK03695 165 DvaQQAalDRLLSE-LCQ--QGIAVVMSSHDLNhTLRHADRVWLLKQGKLL 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
621-812 |
4.02e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.39 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSS-------LLAAIAGELH---------------------------RLRGHVAVRGLSKGF 666
Cdd:PRK13651 28 VEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGTIEwifkdeknkkktkekekvleklviqktRFKKIKKIKEIRRRV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 667 GLATQEPWIQF--ATIRDNILFG-------KTFDAQLYKEVLEACALndDLSILPagdqtevgEKGVTLSGGQRARIALA 737
Cdd:PRK13651 108 GVVFQFAEYQLfeQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQ--------RSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 738 RAVYQEKELYLLDDPLAAVDADVANHLLHrcILGML--SYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLnkQGKTIILVTHDLDNvLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1263-1470 |
4.58e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.41 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlrSQLAIIPQEPFLFSG-TVREN- 1340
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPHmSLGENv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 ---LDPQGLHKD---RALWQALKQCHLSevitsmggldGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQ 1414
Cdd:PRK11432 100 gygLKMLGVPKEerkQRVKEALELVDLA----------GFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1415 KTDQLLQQTI---CKRFaNKTVLTIAH-RLNTILNSDRVLVLQAGRVVELDSPATLRNQP 1470
Cdd:PRK11432 170 NLRRSMREKIrelQQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
622-811 |
4.64e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 622 EVKKGMLVGIVGKVGCGKSSL---LAAI----AGELhRLRG-------HVAVRGLSKGFGLATQEPwiqFATI--Rdnil 685
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLarlLTMIetptGGEL-YYQGqdllkadPEAQKLLRQKIQIVFQNP---YGSLnpR---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 686 fgKTFDAQLYkevlEACALNDDLSILPAGDQTEVGEKGVTL------------SGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:PRK11308 109 --KKVGQILE----EPLLINTSLSAAERREKALAMMAKVGLrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 754 AAVDADVANHLLHrciLGM-------LSYttrLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11308 183 SALDVSVQAQVLN---LMMdlqqelgLSY---VFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
629-764 |
4.64e-05 |
|
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: 48.01 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 629 VGIVGKVGCGKSSLLAAIAGELHRLRGHVAvrgLSKGF--GLATQEPWI-QFATIRDNILFG--------KTFDA----- 692
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKDFNGEAR---PQPGIkvGYLPQEPQLdPTKTVRENVEEGvaeikdalDRFNEisaky 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 693 --------QLYKE------VLEACA---LNDDLSI------LPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLL 749
Cdd:TIGR03719 111 aepdadfdKLAAEqaelqeIIDAADawdLDSQLEIamdalrCPPWDA-----DVTKLSGGERRRVALCRLLLSKPDMLLL 185
|
170
....*....|....*....
gi 312176403 750 DDPLAAVDAD-VA---NHL 764
Cdd:TIGR03719 186 DEPTNHLDAEsVAwleRHL 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1246-1461 |
5.01e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.75 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYrPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLdGVDTsqlelaqlrsQLAI 1325
Cdd:COG0488 316 LELEGLSKSY-GDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPQEpflfsgtvRENLDPqglhkDRALWQALKQC-------HLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLT 1398
Cdd:COG0488 383 FDQH--------QEELDP-----DKTVLDELRDGapggteqEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1399 DAKILCIDEATASVDQKTDQLLQQTIcKRFANkTVLTIAH-R--LNTIlnSDRVLVLQAGRVVELD 1461
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEAL-DDFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1263-1452 |
5.19e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.65 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsQLELAQLRSQLAIIPQEPFLFSGTVRenLD 1342
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQKLYLDTTLPLTVNRFLR--LR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1343 PqGLHKDRALwQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQ 1422
Cdd:PRK09544 94 P-GTKKEDIL-PALKRVQAGHLIDA----------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190
....*....|....*....|....*....|...
gi 312176403 1423 TI--CKRFANKTVLTIAHRLNTIL-NSDRVLVL 1452
Cdd:PRK09544 162 LIdqLRRELDCAVLMVSHDLHLVMaKTDEVLCL 194
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1241-1443 |
5.22e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.80 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1241 LTQGGVEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlelAQLR 1320
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1321 SQLAIIPQ-EPFLFSGTVR-ENLDPQGLHKDRAlWQALKQCHLSEVITSMGGLDGELGEGGRS---LSLGQRQLLCLARA 1395
Cdd:PRK15056 78 NLVAYVPQsEEVDWSFPVLvEDVVMMGRYGHMG-WLRRAKKRDRQIVTAALARVDMVEFRHRQigeLSGGQKKRVFLARA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 312176403 1396 LLTDAKILCIDEATASVDQKTD----QLLQQTickRFANKTVLTIAHRLNTI 1443
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEariiSLLREL---RDEGKTMLVSTHNLGSV 205
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1278-1458 |
5.83e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.18 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1278 IVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG---VDTSQ-LELAQLRSQLAIIPQEPFLFSG-TVRENLDPQGLHKDRAL 1352
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1353 WQAlkqchlsevITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD-QKTDQLLQ--QTICKRFa 1429
Cdd:PRK11144 109 FDK---------IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLPylERLAREI- 178
|
170 180 190
....*....|....*....|....*....|
gi 312176403 1430 NKTVLTIAHRLNTILN-SDRVLVLQAGRVV 1458
Cdd:PRK11144 179 NIPILYVSHSLDEILRlADRVVVLEQGKVK 208
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
620-768 |
6.38e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.57 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfgLATQEPwiQFAtirdnilfgktfDAQLY---- 695
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP----IRRQRD--EYH------------QDLLYlghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 696 ---KEVLEA-------CALNDDLS---ILPAGDQteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAV 756
Cdd:PRK13538 83 pgiKTELTAlenlrfyQRLHGPGDdeaLWEALAQ--VGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170
....*....|....*.
gi 312176403 757 D----ADVANHLLHRC 768
Cdd:PRK13538 161 DkqgvARLEALLAQHA 176
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
620-811 |
7.34e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 46.31 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------------KGFGLATQEPWIQF--ATIRDN 683
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyirpvrKRIGMVFQFPESQLfeDTVERE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 684 ILFG-KTFDAQL-------YKEVLEACALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK13646 107 IIFGpKNFKMNLdevknyaHRLLMDLGFSRDVMSQSP-----------FQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 756 VDADvANHLLHRCI--LGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13646 176 LDPQ-SKRQVMRLLksLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
286-571 |
7.48e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 46.35 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 286 LALGLLKLVGTMLGFSGPLLLSLLV-GFLEEGQEPLSHGLL--YALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNI 362
Cdd:cd18563 2 ILGFLLMLLGTALGLVPPYLTKILIdDVLIQLGPGGNTSLLllLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 363 LYCKALQLGPS---RPPTGEALNLLGTDSERLLNFAgsfheAWGLPlqlaitlYLLYQQVGVAFVGGLI------LALL- 432
Cdd:cd18563 82 LYEHLQRLSLSffdKRQTGSLMSRVTSDTDRLQDFL-----SDGLP-------DFLTNILMIIGIGVVLfslnwkLALLv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 433 LVPVNKVIAT-----RIMASNQEMLQHKDARVK-LVTELLSGIRVIKFCGWEQalgarveacraRELGRLRVI--KYLDA 504
Cdd:cd18563 150 LIPVPLVVWGsyffwKKIRRLFHRQWRRWSRLNsVLNDTLPGIRVVKAFGQEK-----------REIKRFDEAnqELLDA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176403 505 --ACVYLWAALPVVISIVIFITYVLM----GHQLTATK----VFTA-LALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18563 219 niRAEKLWATFFPLLTFLTSLGTLIVwyfgGRQVLSGTmtlgTLVAfLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1262-1469 |
7.92e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 46.26 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtSQLELAQlRSQLAIIPQEPFLFSG-TVREn 1340
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPED-RRRIGYLPEERGLYPKmKVGE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 ldpQ--------GLHKDRAL-----WqaLKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLARALLTDAKILCIDE 1407
Cdd:COG4152 91 ---QlvylarlkGLSKAEAKrradeW--LERLGLGDRANK----------KVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1408 ATASVDQKTDQLLQQTIcKRFANK--TVLTIAHRLNTI--LnSDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:COG4152 156 PFSGLDPVNVELLKDVI-RELAAKgtTVIFSSHQMELVeeL-CDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
626-818 |
8.12e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 626 GMLVGIVGKVGCGKSSLLAAIAGELH--RLRGHVAVRG------LSKGFGLATQEPWI-QFATIRDNILF------GKTF 690
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNrkptkqILKRTGFVTQDDILyPHLTVRETLVFcsllrlPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 691 DAQlyKEVLEACALNDDLSILPAGDqTEVGEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcI 769
Cdd:PLN03211 174 TKQ--EKILVAESVISELGLTKCEN-TIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL--T 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312176403 770 LGMLSYTTRLLCTHRTEYLERA----DAVLLMEAGRLIRAGPPSEILPLVQAV 818
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQPSSRVyqmfDSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
621-820 |
9.82e-05 |
|
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: 46.20 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGeLHRLRGHVA--------------------VRGlsKGFGLATQEPwiqFA-- 678
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGITSgeilfdgedllklsekelrkIRG--REIQMIFQDP---MTsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 679 ----TIRDNI-----LFGKTFDAQLYK---EVLEACALNDDLSIL---PagdqtevGEkgvtLSGGQRARIALARAVYQE 743
Cdd:COG0444 100 npvmTVGDQIaeplrIHGGLSKAEAREraiELLERVGLPDPERRLdryP-------HE----LSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 744 KELYLLDDPLAAVD----ADVANHL--LHRcILGMlSYttrLLCTH-----RteylERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG0444 169 PKLLIADEPTTALDvtiqAQILNLLkdLQR-ELGL-AI---LFITHdlgvvA----EIADRVAVMYAGRIVEEGPVEELF 239
|
250
....*....|....*..
gi 312176403 813 -----P----LVQAVPK 820
Cdd:COG0444 240 enprhPytraLLSSIPR 256
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
725-788 |
1.50e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312176403 725 TLSGGQRARIALARAVYQEKELYLLDDPlaavdadvANHLLHRCILGMLSYTTR-----LLCTHRTEYL 788
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEP--------TNHLDLHAVLWLETYLLKwpktfIVVSHAREFL 404
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1262-1443 |
2.55e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIpqepflfsgtvrENL 1341
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1342 DPQGlhkdraLWQALKQCHLSEVITSMGGLD---GELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQK-TD 1417
Cdd:PRK13545 107 ELKG------LMMGLTKEKIKEIIPEIIEFAdigKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTfTK 180
|
170 180
....*....|....*....|....*.
gi 312176403 1418 QLLQQTICKRFANKTVLTIAHRLNTI 1443
Cdd:PRK13545 181 KCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1278-1460 |
3.12e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.06 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1278 IVGRTGSGKSSLLLVLFRLLEPS-----SGRVLLDGVD--TSQLELAQLRSQLAIIPQEPFLFSG-TVREN--------- 1340
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNiySPDVDPIEVRREVGMVFQYPNPFPHlTIYDNvaigvklng 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1341 -LDPQGLHKDRALWqALKQCHLSEVITSMGGLDGElgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 1419
Cdd:PRK14267 115 lVKSKKELDERVEW-ALKKAALWDEVKDRLNDYPS------NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAK 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 312176403 1420 LQQTICKRFANKTVLTIAHR-LNTILNSDRVLVLQAGRVVEL 1460
Cdd:PRK14267 188 IEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEV 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
621-811 |
3.58e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.41 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGeLHR-LRGHVAVRG-----LS-KGFGLATQEPWIQFA--------TIRDNIL 685
Cdd:PRK11153 26 LHIPAGEIFGVIGASGAGKSTLIRCINL-LERpTSGRVLVDGqdltaLSeKELRKARRQIGMIFQhfnllssrTVFDNVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 686 F----GKTFDAQLYK---EVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:PRK11153 105 LplelAGTPKAEIKArvtELLELVGLSDKADRYPA-----------QLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 759 DVAnhllhRCILGMLSYTTR------LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11153 174 ATT-----RSILELLKDINRelgltiVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEV 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
601-821 |
5.08e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 43.52 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 601 HGALFSWDPVGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSK--GFGLATQEPWIQ 676
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNV--SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGepLAKlnRAQRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 677 FA------------TIRDNI------LFGKTFDAQLYK--EVLEACALND-DLSILPAgdqtevgekgvTLSGGQRARIA 735
Cdd:PRK10419 93 MVfqdsisavnprkTVREIIreplrhLLSLDKAERLARasEMLRAVDLDDsVLDKRPP-----------QLSGGQLQRVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 736 LARAVYQEKELYLLDDPLAAVDAdvanhLLHRCILGML------SYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPP 808
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDL-----VLQAGVIRLLkklqqqFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPV 236
|
250
....*....|...
gi 312176403 809 SEILPLVQAVPKA 821
Cdd:PRK10419 237 GDKLTFSSPAGRV 249
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
628-812 |
5.17e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.55 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 628 LVGIVGKVGCGKSSLLAA-------IAGelHRLRGHVAVRGLS-----------KGFGLATQEPWIQFATIRDNILFG-- 687
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTlnrmndkVSG--YRYSGDVLLGGRSifnyrdvlefrRRVGMLFQRPNPFPMSIMDNVLAGvr 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 688 --KTFDAQLYKEVLEAC--------ALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:PRK14271 127 ahKLVPRKEFRGVAQARltevglwdAVKDRLSDSP-----------FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 758 ADVANHlLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK14271 196 PTTTEK-IEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1272-1463 |
6.04e-04 |
|
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: 41.98 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1272 PGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGtvrenldpqglhkdra 1351
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1352 lwqalkqchlsevitsmggldgelgeggrslsLGQRQLlcLARALLTDAKILCIDEATASVDQKTDQLLQQTIC------ 1425
Cdd:smart00382 65 --------------------------------LRLRLA--LALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 312176403 1426 -KRFANKTVLTIAHRLNTILnsDRVLVLQAGRVVELDSP 1463
Cdd:smart00382 111 lKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLI 147
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
623-811 |
8.42e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.82 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 623 VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV----------AVRGLSKGFGLATQEPWIQF--ATIRDNILFGKTF 690
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddNFEKLRKHIGIVFQNPDNQFvgSIVKYDVAFGLEN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 691 DAQLYKEVLE--ACALNDDLSILPAGDQTEvgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLL--- 765
Cdd:PRK13648 112 HAVPYDEMHRrvSEALKQVDMLERADYEPN------ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLdlv 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 312176403 766 HRciLGMLSYTTRLLCTHR-TEYLErADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13648 186 RK--VKSEHNITIISITHDlSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
957-1039 |
9.79e-04 |
|
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: 42.89 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 957 APNGSSDIRFYLTVyATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACAD 1036
Cdd:cd18573 34 EIFGLSLKTFALAL-LGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVG 112
|
...
gi 312176403 1037 DSL 1039
Cdd:cd18573 113 KSL 115
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1246-1459 |
9.88e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1246 VEFQDVVLAYRpglpnALDGVTFCVQPGEKLGIVGRTGSGKS-SLLLVLFRLLEPssGRVL-----LDGVDTSQLELAQL 1319
Cdd:PRK11022 11 VHFGDESAPFR-----AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaekleFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1320 R----SQLAIIPQEPFlfsgtvrENLDP---------------QG----LHKDRALwQALKQCHLSEVITSMggldgelG 1376
Cdd:PRK11022 84 RnlvgAEVAMIFQDPM-------TSLNPcytvgfqimeaikvhQGgnkkTRRQRAI-DLLNQVGIPDPASRL-------D 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1377 EGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD-----QKTDQLLQqtiCKRFANKTVLTIAHRLNTILNS-DRVL 1450
Cdd:PRK11022 149 VYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqaQIIELLLE---LQQKENMALVLITHDLALVAEAaHKII 225
|
....*....
gi 312176403 1451 VLQAGRVVE 1459
Cdd:PRK11022 226 VMYAGQVVE 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
628-808 |
1.28e-03 |
|
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: 43.46 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 628 LVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG---------LSKGFGLATQEPWI-QFATIRDNILFGKTFDAQLYKE 697
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldaVRQSLGMCPQHNILfHHLTVAEHILFYAQLKGRSWEE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 698 V-LEACALNDDlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYT 776
Cdd:TIGR01257 1038 AqLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP-YSRRSIWDLLLKYRSGR 1111
|
170 180 190
....*....|....*....|....*....|...
gi 312176403 777 TRLLCTHRTEYLE-RADAVLLMEAGRLIRAGPP 808
Cdd:TIGR01257 1112 TIIMSTHHMDEADlLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1273-1463 |
1.32e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 42.28 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1273 GEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRAL 1352
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARGRYPHQPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1353 WQALKQCHLSEVITSMGGL--DGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD--QKTDQLLQQTICKRF 1428
Cdd:PRK10253 113 FTRWRKEDEEAVTKAMQATgiTHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDisHQIDLLELLSELNRE 192
|
170 180 190
....*....|....*....|....*....|....*.
gi 312176403 1429 ANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 1463
Cdd:PRK10253 193 KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAP 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
621-765 |
1.38e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.08 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG---------LSKGFGLAT--QE----PWIqfaTIRDNIL 685
Cdd:COG1129 25 LELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvrfrsprDAQAAGIAIihQElnlvPNL---SVAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 686 FGK------TFD-AQLYKEVLEACA-LndDLSILPAgdqTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:COG1129 102 LGReprrggLIDwRAMRRRARELLArL--GLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
....*...
gi 312176403 758 ADVANHLL 765
Cdd:COG1129 173 EREVERLF 180
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
621-757 |
1.41e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 42.80 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 621 LEVKKGMLVGIVGKVGCGKSS-------LLAAIAGELH-------RLRGHvAVRGLSKGFGLATQEPwiqFA------TI 680
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTlgrlllrLEEPTSGEILfdgqditGLSGR-ELRPLRRRMQMVFQDP---YAslnprmTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 681 RDNI-----LFGKTFDAQLYKEV---LEACALN-DDLSILPagdqtevGEkgvtLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:COG4608 115 GDIIaeplrIHGLASKAERRERVaelLELVGLRpEHADRYP-------HE----FSGGQRQRIGIARALALNPKLIVCDE 183
|
....*.
gi 312176403 752 PLAAVD 757
Cdd:COG4608 184 PVSALD 189
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
427-571 |
1.43e-03 |
|
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: 42.40 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 427 LILALLLVPVNKVIATRIMASnQEMLQHKDARVKlvtELLSGIRVIKFCGWEQALGARVEAcRARELGR--LRVIKylda 504
Cdd:cd18541 151 PLLALLVYRLGKKIHKRFRKV-QEAFSDLSDRVQ---ESFSGIRVIKAFVQEEAEIERFDK-LNEEYVEknLRLAR---- 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 505 acvyLWAALPVVISIVIFITYVL---MGHQLTATKVFTALALV------RMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18541 222 ----VDALFFPLIGLLIGLSFLIvlwYGGRLVIRGTITLGDLVafnsylGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1257-1458 |
1.68e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1257 PGLpNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAqLRSQLAIIPQEPFLF- 1333
Cdd:PRK10982 9 PGV-KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKEA-LENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1334 SGTVRENL-----DPQGLHKDRAlwqalKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEA 1408
Cdd:PRK10982 87 QRSVMDNMwlgryPTKGMFVDQD-----KMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312176403 1409 TASVDQK-TDQLLqqTICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVV 1458
Cdd:PRK10982 162 TSSLTEKeVNHLF--TIIRKLKERgcGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
727-765 |
2.41e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 2.41e-03
10 20 30
....*....|....*....|....*....|....*....
gi 312176403 727 SGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLL 765
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL 465
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1257-1458 |
2.47e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1257 PGLPNAldgVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELA---------QLRSQLAI 1325
Cdd:PRK11288 266 PGLREP---ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAiragimlcpEDRKAEGI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1326 IPqepflfSGTVRENLD--------PQGLHKDRALWQALKQCHlsevITSMGGLDGELGEGGRSLSLGQRQLLCLARALL 1397
Cdd:PRK11288 343 IP------VHSVADNINisarrhhlRAGCLINNRWEAENADRF----IRSLNIKTPSREQLIMNLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1398 TDAKILCIDEATASVD--QKTD------QLLQQTIckrfankTVLTIAHRLNTILN-SDRVLVLQAGRVV 1458
Cdd:PRK11288 413 EDMKVILLDEPTRGIDvgAKHEiynviyELAAQGV-------AVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
589-812 |
3.22e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 41.31 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 589 DPPAEPSTVLELHGALFSWdPVGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL------ 662
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRV-PGRTLLHPL--SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplesws 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 663 SKGFG-----LATQEPWIQFATIRDNILFGK--------TFDAQLYKEVLEACALnddlsilpagdqteVGEKGV----- 724
Cdd:PRK10575 80 SKAFArkvayLPQQLPAAEGMTVRELVAIGRypwhgalgRFGAADREKVEEAISL--------------VGLKPLahrlv 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 725 -TLSGGQRARIALARAVYQEKELYLLDDPLAAVD----ADVANhLLHRciLGMLSYTTRLLCTHRTEYLER-ADAVLLME 798
Cdd:PRK10575 146 dSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLA-LVHR--LSQERGLTVIAVLHDINMAARyCDYLVALR 222
|
250
....*....|....
gi 312176403 799 AGRLIRAGPPSEIL 812
Cdd:PRK10575 223 GGEMIAQGTPAELM 236
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1262-1471 |
3.98e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1262 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP----SSGRVLLDGVDTSQLELAQLRS----QLAIIPQEPflf 1333
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKlvghNVSMIFQEP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1334 sgtvRENLDP---------QGL----HKDRaLWQALKQCHLSEVITSMGGLDGELGEGGRS----LSLGQRQLLCLARAL 1396
Cdd:PRK15093 99 ----QSCLDPservgrqlmQNIpgwtYKGR-WWQRFGWRKRRAIELLHRVGIKDHKDAMRSfpyeLTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1397 LTDAKILCIDEATASVDQKTdqllQQTICKRFA------NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 1469
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTT----QAQIFRLLTrlnqnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVTT 249
|
..
gi 312176403 1470 PH 1471
Cdd:PRK15093 250 PH 251
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
967-1033 |
4.20e-03 |
|
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: 41.00 E-value: 4.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176403 967 YLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVA 1033
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVD 107
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| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1263-1464 |
7.66e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.20 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1263 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS--------SGRVLLDGVDTSQLE---LAQLRSQLAIIPQEPF 1331
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDaprLARLRAVLPQAAQPAF 96
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 1332 LFSgtVRE----------NLDPQGLHKDRAL-WQALkqchlsevitSMGGLDGELGEGGRSLSLGQRQLLCLARAL---- 1396
Cdd:PRK13547 97 AFS--AREivllgryphaRRAGALTHRDGEIaWQAL----------ALAGATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176403 1397 -----LTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLN-TILNSDRVLVLQAGRVVELDSPA 1464
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVrrLARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPA 240
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| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
631-751 |
8.94e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176403 631 IVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGfglATQEPWIQF----------ATIRDNILFGKTF--DAQLYKEV 698
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN---NIAKPYCTYighnlglkleMTVFENLKFWSEIynSAETLYAA 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 312176403 699 LEACALNDDLSilpagdqtevgEKGVTLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:PRK13541 108 IHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
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