|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
324-1453 |
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: 692.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 324 LWRALYGAFGRCYLALGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVT 403
Cdd:TIGR00957 307 LFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSG 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 404 LQARGAVLNILYCKALQLGPS--RPPT-GEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLIL 480
Cdd:TIGR00957 387 MRIKTAVMGAVYRKALVITNSarKSSTvGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAV 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 481 ALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYL 560
Cdd:TIGR00957 467 MVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFT 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 561 WAALPVVISIVIFITYVLMGHQ--LTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLFLDLPNHNPQAYYS 638
Cdd:TIGR00957 547 WVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIER 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 639 PDPPAEPSTVLELHGALFSW---DPVGTSLETFishlEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlsk 715
Cdd:TIGR00957 627 RTIKPGEGNSITVHNATFTWardLPPTLNGITF----SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--- 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 716 GFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEK 795
Cdd:TIGR00957 700 SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 796 ELYLLDDPLAAVDADVANHLLHRCI--LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPK-- 871
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEfl 859
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 872 ---AWAENGQESDSATAQSVQNPEKTKEGLE----------------------------------------EEQSTSGRL 908
Cdd:TIGR00957 860 rtyAPDEQQGHLEDSWTALVSGEGKEAKLIEngmlvtdvvgkqlqrqlsasssdsgdqsrhhgssaelqkaEAKEETWKL 939
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 909 LQEESKKEGAVALHVYQAYWKAVGQGLALAILFSLLLMQATRNAADWWLSHWISQLKAeNSSQEaqpstspasmglfspq 988
Cdd:TIGR00957 940 MEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMV-NGTQN---------------- 1002
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 989 lllfspgnlyipvfplpkaapngssDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFN 1068
Cdd:TIGR00957 1003 -------------------------NTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE 1057
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1069 ATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGS 1148
Cdd:TIGR00957 1058 RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLES 1137
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1149 LTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQg 1228
Cdd:TIGR00957 1138 VSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHS- 1216
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1229 lANPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTCDLPQEP-QGQPLQLGTGWLTQGGVEFQDVVLAYR 1307
Cdd:TIGR00957 1217 -LSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQETAPPSGWPPRGRVEFRNYCLRYR 1295
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1308 PGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGT 1387
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGS 1375
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 1388 VRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGEL-GEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:TIGR00957 1376 LRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEcAEGGENLSVGQRQLVCLARALLRKTKI 1442
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
266-1453 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 633.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 266 EDGESWLSRFSYAWLAPLLARGacgeLRQP---QDICRLPHRLQPTYLARVFQAHWQEGAR-----LWRALYGAFGRCYL 337
Cdd:PLN03232 229 ERYASIFSRIYFSWMTPLMQLG----YRKPiteKDVWQLDQWDQTETLIKRFQRCWTEESRrpkpwLLRALNNSLGGRFW 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 338 ALGLLKLVGTMLGFSGPLLLSLLVGFLEEGqEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCK 417
Cdd:PLN03232 305 LGGIFKIGHDLSQFVGPVILSHLLQSMQEG-DPAWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 418 ALQL---GPSRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATR 494
Cdd:PLN03232 384 SLRLtheARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRK 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 495 IMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFI 574
Cdd:PLN03232 464 MRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 575 TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI-QLFLdlpnhNPQAYYSPDPPAEPST-VLELH 652
Cdd:PLN03232 544 VFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIeELLL-----SEERILAQNPPLQPGApAISIK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 653 GALFSWDPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGEL-HRLRGHVAVRGlskGFGLATQEPWIQFATI 731
Cdd:PLN03232 619 NGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELsHAETSSVVIRG---SVAYVPQVSWIFNATV 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 732 RDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADV 811
Cdd:PLN03232 696 RENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 812 ANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEiLPLVQAVPKAWAENGQESDSATAQSVQNP 891
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAGKMDATQEVNTNDE 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 892 EKTKEGLEEEQSTSGR--------------LLQEESKKEGAVALHVYQAYWKAVGQGLALAILFS-LLLMQATRNAADWW 956
Cdd:PLN03232 855 NILKLGPTVTIDVSERnlgstkqgkrgrsvLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVcYLTTEVLRVSSSTW 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 957 LSHWISQLKAENssqeaqpstspasmglfspqlllFSPGnlyipvfplpkaapngssdirFYLTVYATIAGVNSLCTLLR 1036
Cdd:PLN03232 935 LSIWTDQSTPKS-----------------------YSPG---------------------FYIVVYALLGFGQVAVTFTN 970
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1037 AVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLP 1116
Cdd:PLN03232 971 SFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVST 1050
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1117 WLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATS 1196
Cdd:PLN03232 1051 ISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANT 1130
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1197 ATMQWLDIRLQLMGAAVVSAIAGIALVQH-----QQGLANpgLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEE 1271
Cdd:PLN03232 1131 SSNRWLTIRLETLGGVMIWLTATFAVLRNgnaenQAGFAS--TMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGN 1208
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1272 YTcDLPQEP-----QGQPLqlgTGWLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFR 1346
Cdd:PLN03232 1209 YI-DLPSEAtaiieNNRPV---SGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFR 1284
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1347 LLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVIT-SMGGLDGE 1425
Cdd:PLN03232 1285 IVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDrNPFGLDAE 1364
|
1210 1220
....*....|....*....|....*...
gi 2462611208 1426 LGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PLN03232 1365 VSEGGENFSVGQRQLLSLARALLRRSKI 1392
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
254-1453 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 621.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 254 PLLPEDQEPEVAED---GE--------SWLSRFSYAWLAPLLARGACGELRQPqDICRLPHRLQPTYLARVFQAHWQEGA 322
Cdd:PLN03130 206 PIGSESVDDYEYEElpgGEqicperhaNIFSRIFFGWMTPLMQLGYKRPLTEK-DVWKLDTWDQTETLYRSFQKCWDEEL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 323 R-----LWRALYGAFGRCYLALGLLKLVGTMLGFSGPLLLSLLVGFLEEGqEPLSHGLLYALGLAGGAVLGAVLQNQYGY 397
Cdd:PLN03130 285 KkpkpwLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNG-EPAWIGYIYAFSIFVGVVLGVLCEAQYFQ 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 398 EVYKVTLQARGAVLNILYCKALQL---GPSRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAF 474
Cdd:PLN03130 364 NVMRVGFRLRSTLVAAVFRKSLRLtheGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVAS 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 475 VGGLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLD 554
Cdd:PLN03130 444 LIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLS 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 555 AACVYLWAALPVVISIVIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQ-LFLdlpnhNP 633
Cdd:PLN03130 524 AFNSFILNSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEeLLL-----AE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 634 QAYYSPDPPAEPST-VLELHGALFSWDPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGEL-HRLRGHVAVR 711
Cdd:PLN03130 599 ERVLLPNPPLEPGLpAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 712 GlskGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAV 791
Cdd:PLN03130 679 G---TVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAV 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 792 YQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL---PLVQ- 867
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSnngPLFQk 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 868 ----------AVPKAWAENGQESDSATAQSVQNPEKTKEGLEEEQSTSGR--LLQEESKKEGAVALHVYQAYWKAVGQGL 935
Cdd:PLN03130 836 lmenagkmeeYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKsvLIKQEERETGVVSWKVLERYKNALGGAW 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 936 ALAILF-SLLLMQATRNAADWWLSHWISQlkaenssqeaqpsTSPASMGlfspqlllfsPGnlyipvfplpkaapngssd 1014
Cdd:PLN03130 916 VVMILFlCYVLTEVFRVSSSTWLSEWTDQ-------------GTPKTHG----------PL------------------- 953
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1015 irFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFIL 1094
Cdd:PLN03130 954 --FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFV 1031
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1095 NILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGAT 1174
Cdd:PLN03130 1032 NMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAY 1111
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1175 YRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQH-----QQGLANpgLVGLSLSYALSLTGLL 1249
Cdd:PLN03130 1112 DRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNgraenQAAFAS--TMGLLLSYALNITSLL 1189
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1250 SGLVSSFTQTEAMLVSVERLEEYTcDLPQEpqgQPLQLGT-----GWLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPG 1324
Cdd:PLN03130 1190 TAVLRLASLAENSLNAVERVGTYI-DLPSE---APLVIENnrpppGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPS 1265
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1325 EKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALW 1404
Cdd:PLN03130 1266 EKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLW 1345
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1405 QALKQCHLSEVI-TSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PLN03130 1346 ESLERAHLKDVIrRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
324-1448 |
1.45e-148 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 493.14 E-value: 1.45e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 324 LWRALYGAFGRCYLALGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVT 403
Cdd:PTZ00243 234 LLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 404 LQARGAVLNILYCKALQLGP---SRPP--TGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGL 478
Cdd:PTZ00243 314 LQYRSALNALIFEKCFTISSkslAQPDmnTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 479 ILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACV 558
Cdd:PTZ00243 394 AVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 559 YLWAALPVVISIVIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLFLDLPN-------- 630
Cdd:PTZ00243 474 FVNNATPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNatcstvqd 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 631 ----------HNP-------------QAYYSPDPPAEPSTVLELHGALFSW----------------------------- 658
Cdd:PTZ00243 554 meeywreqreHSTacqlaavlenvdvTAFVPVKLPRAPKVKTSLLSRALRMlcceqcrptkrhpspsvvvedtdygspss 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 659 -----DPVGTS-------------------LETFIS----------HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRL 704
Cdd:PTZ00243 634 asrhiVEGGTGggheatptsersaktpkmkTDDFFElepkvllrdvSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 705 RGHVAVrglSKGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRAR 784
Cdd:PTZ00243 714 EGRVWA---ERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKAR 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 785 IALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL- 863
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMr 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 864 -PLVQAVPKAWAEN--GQESDS-----------ATAQSVQNPEKTKEGLEEEQ------STSGRLLQEESKKEGAVALHV 923
Cdd:PTZ00243 871 tSLYATLAAELKENkdSKEGDAdaevaevdaapGGAVDHEPPVAKQEGNAEGGdgaaldAAAGRLMTREEKASGSVPWST 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 924 YQAYWKAVGQGL-ALAILFSLLLMQATRNAADWWLSHWisqlkaenssqeaqpstSPASMGLfspqlllfspgnlyipvf 1002
Cdd:PTZ00243 951 YVAYLRFCGGLHaAGFVLATFAVTELVTVSSGVWLSMW-----------------STRSFKL------------------ 995
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1003 plpkaapngSSDIrfYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSD 1082
Cdd:PTZ00243 996 ---------SAAT--YLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRD 1064
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1083 VACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTL 1162
Cdd:PTZ00243 1065 IDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEAL 1144
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1163 AGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLA--NPGLVGLSLS 1240
Cdd:PTZ00243 1145 QGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATsqEIGLVSLSLT 1224
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1241 YALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTCDLPQE--PQ--------------------------GQPLQLGTGWL 1292
Cdd:PTZ00243 1225 MAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEdmPEldeevdalerrtgmaadvtgtvviepASPTSAAPHPV 1304
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1293 TQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRS 1372
Cdd:PTZ00243 1305 QAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 1373 QLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALL 1448
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSnYSVGQRQLMCMARALL 1461
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
339-622 |
1.41e-134 |
|
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: 416.57 E-value: 1.41e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 339 LGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKA 418
Cdd:cd18598 2 LGLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 419 LQLGPSR---PPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRI 495
Cdd:cd18598 82 LRVRSSSlskFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 496 MASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFIT 575
Cdd:cd18598 162 GALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462611208 576 YVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 622
Cdd:cd18598 242 YVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
338-622 |
2.32e-127 |
|
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: 396.97 E-value: 2.32e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 338 ALGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCK 417
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 418 ALQLGPS---RPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATR 494
Cdd:cd18559 81 ALRSPISffeRTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 495 IMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFI 574
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462611208 575 TYVLMGH--QLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 622
Cdd:cd18559 241 AYVSRHSlaGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
936-1273 |
1.42e-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: 332.19 E-value: 1.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 936 ALAILFSLLLMQATRNAADWWLSHWISQLKAENSSQeaqpstspasmglfspqlllfspgnlyipvfplpkaapnGSSDI 1015
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNF---------------------------------------INDSF 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1016 RFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILN 1095
Cdd:cd18605 42 NFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1096 ILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATY 1175
Cdd:cd18605 122 ILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1176 RFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGL-ANPGLVGLSLSYALSLTGLLSGLVS 1254
Cdd:cd18605 202 RFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAVVQHFFGLsIDAGLIGLALSYALPITGLLSGLLN 281
|
330
....*....|....*....
gi 2462611208 1255 SFTQTEAMLVSVERLEEYT 1273
Cdd:cd18605 282 SFTETEKEMVSVERVRQYF 300
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
270-1453 |
3.78e-103 |
|
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: 362.31 E-value: 3.78e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 270 SWLSRFSYAWLAPLLARGACGELrQPQDICRLPHRLQPTYLARVFQAHW-------QEGARLWRALYGAFGRCYLALGLL 342
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKL-ELSDIYQIPSFDSADNLSERLEREWdrelasaKKNPKLLNALRRCFFWRFVFYGIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 343 KLVGTMLGFSGPLLLSLLVG-FLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKALQL 421
Cdd:TIGR01271 89 LYFGEATKAVQPLLLGRIIAsYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 422 GP---SRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRIMAS 498
Cdd:TIGR01271 169 SSrvlDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 499 NQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVI---KYLDAACVYLWAALPVVISIVifiT 575
Cdd:TIGR01271 249 RDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIaylRYFYSSAFFFSGFFVVFLSVV---P 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 576 YVLMgHQLTATKVFTALALVRMLILPLN-NFPWVINGLLEAKVSLDRIQLFLDLPNHNPQAYyspdppAEPSTVLELHGA 654
Cdd:TIGR01271 326 YALI-KGIILRRIFTTISYCIVLRMTVTrQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEY------NLTTTEVEMVNV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 655 LFSWDP-VGTSLET-----------------FISHLE-------------VKKGMLVGIVGKVGCGKSSLLAAIAGELHR 703
Cdd:TIGR01271 399 TASWDEgIGELFEKikqnnkarkqpngddglFFSNFSlyvtpvlknisfkLEKGQLLAVAGSTGSGKSSLLMMIMGELEP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 704 LRGHVAVRGLskgFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRA 783
Cdd:TIGR01271 479 SEGKIKHSGR---ISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 784 RIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI- 862
Cdd:TIGR01271 556 RISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELq 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 863 ---------LPLVQAVPKAWAENGQ------------ESDSATA-------QSVQNP-----EKTK-------------- 895
Cdd:TIGR01271 636 akrpdfsslLLGLEAFDNFSAERRNsiltetlrrvsiDGDSTVFsgpetikQSFKQPppefaEKRKqsiilnpiasarkf 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 896 ----------EGLEEEQSTSGRL-----------LQEESKKEGAVALH--VYQAYWK----------AVGQGL--ALAIL 940
Cdd:TIGR01271 716 sfvqmgpqkaQATTIEDAVREPSerkfslvpedeQGEESLPRGNQYHHglQHQAQRRqsvlqlmthsNRGENRreQLQTS 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 941 FSLLLMQATRNAADWWLSHWISQLKAENS------------------SQEAQPSTSPASMGL---FSPQLLLF------- 992
Cdd:TIGR01271 796 FRKKSSITQQNELASELDIYSRRLSKDSVyeiseeineedlkecfadERENVFETTTWNTYLryiTTNRNLVFvlifclv 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 993 --------SPGNLYI----PVFPL----------------PKAAPNGSSdirfYLTVYATIAGVNSLCTL--LRAVLFAA 1042
Cdd:TIGR01271 876 iflaevaaSLLGLWLitdnPSAPNyvdqqhanasspdvqkPVIITPTSA----YYIFYIYVGTADSVLALgfFRGLPLVH 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1043 GTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLL 1122
Cdd:TIGR01271 952 TLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAA 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1123 PPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWL 1202
Cdd:TIGR01271 1032 IPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWF 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1203 DIRLQLMGAAVVSAIAGIALVQHQQGlanPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTcDLPQEP-- 1280
Cdd:TIGR01271 1112 QMRIDIIFVFFFIAVTFIAIGTNQDG---EGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFI-DLPQEEpr 1187
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1281 ---QGQPLQLGTG-----------WLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFR 1346
Cdd:TIGR01271 1188 psgGGGKYQLSTVlvienphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR 1267
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1347 LLEpSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGEL 1426
Cdd:TIGR01271 1268 LLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFV 1346
|
1370 1380
....*....|....*....|....*...
gi 2462611208 1427 GEGGRS-LSLGQRQLLCLARALLTDAKV 1453
Cdd:TIGR01271 1347 LVDGGYvLSNGHKQLMCLARSILSKAKI 1374
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
649-852 |
6.48e-101 |
|
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: 320.96 E-value: 6.48e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 649 LELHGALFSWDPVGTSLETFIS--HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlskGFGLATQEPWI 726
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKdiNLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG---SIAYVSQEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 727 QFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 806
Cdd:cd03250 78 QNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462611208 807 VDADVANHLLHRCILGMLSYT-TRLLCTHRTEYLERADAVLLMEAGR 852
Cdd:cd03250 158 VDAHVGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
339-622 |
6.41e-90 |
|
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: 293.62 E-value: 6.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 339 LGLLKLVGTMLGFSGPLLLSLLVGFLEE-GQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCK 417
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 418 ALQLGPS---RPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATR 494
Cdd:cd18579 82 ALRLSSSarqETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 495 IMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFI 574
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462611208 575 TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 622
Cdd:cd18579 242 TYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
340-622 |
6.44e-79 |
|
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: 262.41 E-value: 6.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 340 GLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKAL 419
Cdd:cd18595 3 ALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 420 QLGP-SRP--PTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRIM 496
Cdd:cd18595 83 RLSNsARKksTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 497 ASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITY 576
Cdd:cd18595 163 KLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462611208 577 VLMG--HQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 622
Cdd:cd18595 243 VLSDpdNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
338-622 |
5.34e-67 |
|
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: 228.92 E-value: 5.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 338 ALGLLKLVGTMLGFSGPLLLSLLVGFLEE-GQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYC 416
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLEDpGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 417 KALQL----GPSRPP------------------TGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGV-A 473
Cdd:cd18596 81 KALRRrdksGSSKSSeskkkdkeededekssasVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWsA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 474 FVGGLILALLLvPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYL 553
Cdd:cd18596 161 LVGLAVMVLLL-PLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 554 DAACVYLWAALPVVISIVIFITYVL-MGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 622
Cdd:cd18596 240 DLLLSLLWFLIPILVTVVTFATYTLvMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
937-1273 |
3.75e-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: 220.07 E-value: 3.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 937 LAILFSLLLMQATRNAADWWLSHWISQlkaenssqeaqpstspasmglfspqlllfspgnlyipvfplpkAAPNGSSDIR 1016
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSD-------------------------------------------WSSSPNSSSG 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1017 FYLTVYATIAGVNS-LCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILN 1095
Cdd:cd18580 39 YYLGVYAALLVLASvLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1096 ILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATY 1175
Cdd:cd18580 119 DFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1176 RFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQglANPGLVGLSLSYALSLTGLLSGLVSS 1255
Cdd:cd18580 199 RFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALLAVLLRSS--ISAGLVGLALTYALSLTGSLQWLVRQ 276
|
330
....*....|....*...
gi 2462611208 1256 FTQTEAMLVSVERLEEYT 1273
Cdd:cd18580 277 WTELETSMVSVERILEYT 294
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1295-1453 |
6.47e-64 |
|
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: 216.59 E-value: 6.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1295 GGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1374
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1375 AIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGEnLSVGQRQLLCLARALLRKSKI 160
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
340-622 |
6.96e-61 |
|
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: 210.77 E-value: 6.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 340 GLLKLVGTMLGFSGPLLLSLLVGFLEEGQE-----PLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNIL 414
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLINFVEDAYLggpppSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 415 YCKALQL-GPSR--PPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVI 491
Cdd:cd18597 83 YRKSLRLsGKSRheFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 492 ATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIV 571
Cdd:cd18597 163 MKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASML 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 572 IFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 622
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, ... |
1005-1273 |
1.55e-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: 1.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1005 PKAAPNGSSDIR-FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDV 1083
Cdd:cd18603 29 PALNGTQDTEQRdYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1084 ACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLA 1163
Cdd:cd18603 109 DTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1164 GLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlaNPGLVGLSLSYAL 1243
Cdd:cd18603 189 GASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLFAALFAVLSRDSL--SPGLVGLSISYAL 266
|
250 260 270
....*....|....*....|....*....|
gi 2462611208 1244 SLTGLLSGLVSSFTQTEAMLVSVERLEEYT 1273
Cdd:cd18603 267 QITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
323-863 |
2.02e-55 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 203.86 E-value: 2.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 323 RLWRALYGAFGRCYLALgLLKLVGTMLGFSGPLLLSLLVGFLEEGQePLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKV 402
Cdd:COG1132 11 RLLRYLRPYRGLLILAL-LLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLLLLLLGLALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 403 TLQARGAVLNILYCKALQLGPS---RPPTGEALNLLGTDSERLLNFAG-SFHEAWGLPLQLAITL-YLLYQQVGVAFVGG 477
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSffdRRRTGDLLSRLTNDVDAVEQFLAhGLPQLVRSVVTLIGALvVLFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 478 LILALLLVPVnKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEAcRARELGR--LRVIKYLDA 555
Cdd:COG1132 169 LVLPLLLLVL-RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE-ANEELRRanLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 556 --ACVYLWAALPVVISIVIFITYVLMGhQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLFLDLPNHNP 633
Cdd:COG1132 247 ffPLMELLGNLGLALVLLVGGLLVLSG-SLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 634 QAYySPDPPAEPSTVLELHGALFSWDPVGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAG-------------- 699
Cdd:COG1132 326 DPP-GAVPLPPVRGEIEFENVSFSYPGDRPVLKDI--SLTIPPGETVALVGPSGSGKSTLVNLLLRfydptsgrilidgv 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 700 -----ELHRLRGHVAVrglskgfglATQEPWIQFATIRDNILFGK---TfDAQLyKEVLEACALNDDLSILPAGDQTEVG 771
Cdd:COG1132 403 dirdlTLESLRRQIGV---------VPQDTFLFSGTIRENIRYGRpdaT-DEEV-EEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 772 EKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAG 851
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETE-ALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
570
....*....|..
gi 2462611208 852 RLIRAGPPSEIL 863
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; ... |
937-1273 |
1.12e-54 |
|
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: 193.07 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 937 LAILFSLLLMQATRNAADWWLSHWisqlkaenSSQEAQPSTSPASmglfspqlllfspgnlyipvfplpkaapngSSDIR 1016
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIW--------ASAYETSSALPPS------------------------------EVSVL 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1017 FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNI 1096
Cdd:cd18604 44 YYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1097 LLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYR 1176
Cdd:cd18604 124 LLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEER 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1177 FEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQqglANPGLVGLSLSYALSLTGLLSGLVSSF 1256
Cdd:cd18604 204 FIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSFATAALLVYGPG---IDAGLAGFSLSFALGFSSAILWLVRSY 280
|
330
....*....|....*..
gi 2462611208 1257 TQTEAMLVSVERLEEYT 1273
Cdd:cd18604 281 NELELDMNSVERIQEYL 297
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
649-851 |
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 2462611208 649 LELHGALFSWDPVGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV-------------AVRGLSK 715
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNI--NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 716 G-FGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQE 794
Cdd:cd03290 79 YsVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 795 KELYLLDDPLAAVDADVANHLLHRCILGMLSYTTR--LLCTHRTEYLERADAVLLMEAG 851
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 ... |
936-1273 |
1.63e-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: 187.04 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 936 ALAILFSLLLMQATRNAADWWLSHWisqlkaenssQEAQPSTSPASMGLFSPQLLlfspgnlyipvfplpkaapngSSDI 1015
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADW----------TEANHDVASVVFNITSSSLE---------------------DDEV 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1016 RFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILN 1095
Cdd:cd18602 50 SYYISVYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1096 ILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATY 1175
Cdd:cd18602 130 RLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1176 RFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYALSLTGLLSGLVSS 1255
Cdd:cd18602 210 RFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRN 289
|
330
....*....|....*...
gi 2462611208 1256 FTQTEAMLVSVERLEEYT 1273
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 ... |
937-1273 |
2.82e-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: 185.76 E-value: 2.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 937 LAILFSLLLMQATRNAADWWLSHWISQLkaenssqeaqpstspasmglfspqlllfspgnlyipvFPLPKAapngssdir 1016
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTEDF-------------------------------------FGLSQG--------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1017 FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLP----- 1091
Cdd:cd18606 36 FYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPdslrm 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1092 -----------FILNIllanaagllgllavlgSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLAD 1160
Cdd:cd18606 116 flytlssiigtFILII----------------IYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1161 TLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVV--SAIAGIALVQHqqglANPGLVGLS 1238
Cdd:cd18606 180 SLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVliVALLCVTRRFS----ISPSSTGLV 255
|
330 340 350
....*....|....*....|....*....|....*
gi 2462611208 1239 LSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEYT 1273
Cdd:cd18606 256 LSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1013-1453 |
3.62e-52 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 194.23 E-value: 3.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1013 SDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVA----CADD 1088
Cdd:COG1132 58 SALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDaveqFLAH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1089 SLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRlgslTLSPLYSHLADTLAGLSVL 1168
Cdd:COG1132 138 GLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQE----ALAELNGRLQESLSGIRVV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1169 RATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYALSLTGL 1248
Cdd:COG1132 214 KAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1249 LSGLVSSFTQTEAMLVSVERLEEY---TCDLPQEPQGQPLQLgtgwlTQGGVEFQDVVLAYRPGLPnALDGVTFCVQPGE 1325
Cdd:COG1132 294 LRQLANVLNQLQRALASAERIFELldePPEIPDPPGAVPLPP-----VRGEIEFENVSFSYPGDRP-VLKDISLTIPPGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1326 KLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLdpqGLHKDRA--- 1402
Cdd:COG1132 368 TVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENI---RYGRPDAtde 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 1403 -LWQALKQCHLSEVITSMggldge-lgeggRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:COG1132 445 eVEEAAKAAQAHEFIEALpdgydtvvgergVNLSGGQRQRIAIARALLKDPPI 497
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
932-1273 |
1.46e-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: 1.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 932 GQGLALAILFSLLLMQATRNAADWWLSHWISQLKAENSSQEAQPSTSPASMglfspqlllfspgnlyipvfplpkaapNG 1011
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNI---------------------------SD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1012 SSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLP 1091
Cdd:cd18599 54 NPDLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1092 FILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRAT 1171
Cdd:cd18599 134 FTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1172 GATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHqqGLANPGLVGLSLSYALSLTGLLSG 1251
Cdd:cd18599 214 NKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITALLVVLLK--GSISPAFAGLALSYALQLSGLFQF 291
|
330 340
....*....|....*....|..
gi 2462611208 1252 LVSSFTQTEAMLVSVERLEEYT 1273
Cdd:cd18599 292 TVRLASETEARFTSVERILEYI 313
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
367-863 |
3.04e-48 |
|
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: 182.27 E-value: 3.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 367 GQEPLSHGLLYALGLAGGAVLGAVL---QNQYGYEV-YKVTLQARGAVLNilycKALQLGP---SRPPTGEALNLLGTDS 439
Cdd:COG4988 50 GGAPLSALLPLLGLLLAVLLLRALLawlRERAAFRAaARVKRRLRRRLLE----KLLALGPawlRGKSTGELATLLTEGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 440 ERLLNFAGSFheawgLP-------LQLAITLYLLYQQVGVAFVggLILALLLVPVNKVIATRIMASNQEmlQHKDARVKL 512
Cdd:COG4988 126 EALDGYFARY-----LPqlflaalVPLLILVAVFPLDWLSGLI--LLVTAPLIPLFMILVGKGAAKASR--RQWRALARL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 513 ---VTELLSGIRVIKFCGWEQALGARV----EACRARELGRLRV----IKYLDAAcVYLWAALpvvisIVIFITYVLMGH 581
Cdd:COG4988 197 sghFLDRLRGLTTLKLFGRAKAEAERIaeasEDFRKRTMKVLRVaflsSAVLEFF-ASLSIAL-----VAVYIGFRLLGG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 582 QLTATKVFTALALVRMLILPLNNFpwvinGL-----LEAKVSLDRIQLFLDLPNHNPQAYYSPDPPAEPSTvLELHGALF 656
Cdd:COG4988 271 SLTLFAALFVLLLAPEFFLPLRDL-----GSfyharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPS-IELEDVSF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 657 SWDPVGTSLEtFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWI 726
Cdd:COG4988 345 SYPGGRPALD-GLS-LTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpasWRRQIAWVPQNPYL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 727 QFATIRDNILFGKTF--DAQLyKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPL 804
Cdd:COG4988 423 FAGTIRENLRLGRPDasDEEL-EAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 805 AAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG4988 502 AHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
465-863 |
4.24e-48 |
|
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: 184.65 E-value: 4.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 465 LLYQQVGVAFVGgLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCG--------WEQALGARV 536
Cdd:COG2274 290 LFFYSPPLALVV-LLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGaesrfrrrWENLLAKYL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 537 EAcrarelgRLRVIKYLDAAcvYLWA-ALPVVISIVIFI--TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLL 613
Cdd:COG2274 369 NA-------RFKLRRLSNLL--STLSgLLQQLATVALLWlgAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 614 EAKVSLDRIQLFLDLPNHNPQAYYSPDPPAEPSTVlELHGALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSL 693
Cdd:COG2274 440 DAKIALERLDDILDLPPEREEGRSKLSLPRLKGDI-ELENVSFRYPGDSPPVLDNIS-LTIKPGERVAIVGRSGSGKSTL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 694 LAAIAGELHRLRGHVAV----------RGLSKGFGLATQEPWIQFATIRDNILFGKTF--DAQLYkEVLEACALNDDLSI 761
Cdd:COG2274 518 LKLLLGLYEPTSGRILIdgidlrqidpASLRRQIGVVLQDVFLFSGTIRENITLGDPDatDEEII-EAARLAGLHDFIEA 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 762 LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLER 841
Cdd:COG2274 597 LPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRL 675
|
410 420
....*....|....*....|..
gi 2462611208 842 ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG2274 676 ADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
340-622 |
4.19e-47 |
|
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: 171.65 E-value: 4.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 340 GLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALG--------------LAGGAVLGAVLQNQYGYEVYKVT-- 403
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVsyvtveeffsngyvLAVILFLALLLQATFSQASYHIVir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 404 --LQARGAVLNILYCKALQLGPSRPP-----TGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVG 476
Cdd:cd18591 83 egIRLKTALQAMIYEKALRLSSWNLSsgsmtIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 477 GLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELgrlrviKYLDAA 556
Cdd:cd18591 163 GAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKEL------KLLLKD 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 557 CVY------LWAALPVVISIVIFITYVLMGHQ-LTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 622
Cdd:cd18591 237 AVYwslmtfLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1291-1453 |
7.38e-47 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 167.20 E-value: 7.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1291 WLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL 1370
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1371 RSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKqchLSEvitsmggldgelgeGGRSLSLGQRQLLCLARALLTD 1450
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR---VSE--------------GGLNLSQGQRQLLCLARALLKR 143
|
...
gi 2462611208 1451 AKV 1453
Cdd:cd03369 144 PRV 146
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
363-623 |
2.12e-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: 168.97 E-value: 2.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 363 FLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKALQLGP---SRPPTGEALNLLGTDS 439
Cdd:cd18594 27 FVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSsalSKITTGHIVNLLSNDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 440 ERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSG 519
Cdd:cd18594 107 QKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 520 IRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITYVLMGHQLTATKVFTALAL---VR 596
Cdd:cd18594 187 MRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTARKVFTVISLlnaLR 266
|
250 260
....*....|....*....|....*..
gi 2462611208 597 MLIlpLNNFPWVINGLLEAKVSLDRIQ 623
Cdd:cd18594 267 MTI--TRFFPESIQTLSESRVSLKRIQ 291
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
428-863 |
3.01e-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: 176.50 E-value: 3.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 428 TGEALNLLGTDSERLLNF-------AGSfheAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVnkvIATRIM-ASN 499
Cdd:COG4987 111 SGDLLNRLVADVDALDNLylrvllpLLV---ALLVILAAVAFLAFFSPALALVLALGLLLAGLLLPL---LAARLGrRAG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 500 QEMLQHKDARVKLVTELLSGIRVIKFCG-WEQALGA--RVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITY 576
Cdd:COG4987 185 RRLAAARAALRARLTDLLQGAAELAAYGaLDRALARldAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 577 VLMGHQ---LTATKVFTALALVRMLiLPLnnfPWVINGLLEAKVSLDRIQlflDLPNHNPQAYYSPDPPAEPSTV-LELH 652
Cdd:COG4987 265 VAAGALsgpLLALLVLAALALFEAL-APL---PAAAQHLGRVRAAARRLN---ELLDAPPAVTEPAEPAPAPGGPsLELE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 653 GALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQ 722
Cdd:COG4987 338 DVSFRYPGAGRPVLDGLS-LTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddLRRRIAVVPQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 723 EPWIQFATIRDNILFGK---TfDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYL 799
Cdd:COG4987 417 RPHLFDTTLRENLRLARpdaT-DEELW-AALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILL 494
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 800 LDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG4987 495 LDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
672-862 |
4.77e-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: 4.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLskgFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLE 751
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR---ISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 752 ACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLL 831
Cdd:cd03291 135 ACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRIL 214
|
170 180 190
....*....|....*....|....*....|.
gi 2462611208 832 CTHRTEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:cd03291 215 VTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
934-1273 |
1.28e-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: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 934 GLALAILFSLLlMQATRNAADWWLSHWisqlkaeNSSQEAQPSTSPASMGLFSpqlllfspGNLYIPVfplpkaapngsS 1013
Cdd:cd18601 4 VFILLVLLNIA-AQVLYVLSDWWLSYW-------ANLEEKLNDTTDRVQGENS--------TNVDIED-----------L 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1014 DIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFI 1093
Cdd:cd18601 57 DRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1094 LNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGA 1173
Cdd:cd18601 137 FLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1174 TYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVqhqqgLA---NPGLVGLSLSYALSLTGLLS 1250
Cdd:cd18601 217 QERFQEEFDAHQDLHSEAWFLFLATSRWLAVRLDALCALFVTVVAFGSLF-----LAeslDAGLVGLSLSYALTLMGTFQ 291
|
330 340
....*....|....*....|...
gi 2462611208 1251 GLVSSFTQTEAMLVSVERLEEYT 1273
Cdd:cd18601 292 WCVRQSAEVENLMTSVERVLEYS 314
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1006-1453 |
1.45e-42 |
|
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: 167.70 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1006 KAAPNGSSDIRFYLTVYATIAGV-NSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVA 1084
Cdd:COG2274 185 RVLPNQDLSTLWVLAIGLLLALLfEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVES 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1085 CAD-----------DSLPFILNILLanaagllgllavlgsglpwlllllpplsIMYYH--------------------VQ 1133
Cdd:COG2274 265 IREfltgslltallDLLFVLIFLIV----------------------------LFFYSpplalvvllliplyvllgllFQ 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1134 RHYRASSRELRRLGSLtlspLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAV 1213
Cdd:COG2274 317 PRLRRLSREESEASAK----RQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLA 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1214 VSAI--AGIALVQHQQ-------------GLANPGLVGLslsyalsltgllsglVSSFTQTEAMLVSVERLEEYTcDLPQ 1278
Cdd:COG2274 393 TVALlwLGAYLVIDGQltlgqliafnilsGRFLAPVAQL---------------IGLLQRFQDAKIALERLDDIL-DLPP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1279 EPQGQPLQLGTGWLtQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLD 1358
Cdd:COG2274 457 EREEGRSKLSLPRL-KGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1359 GVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQglHKDRALWQALKQCHLSEVITSMGG-LDGELGEGGRSLS 1434
Cdd:COG2274 536 GIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDPD--ATDEEIIEAARLAGLHDFIEALPMgYDTVVGEGGSNLS 613
|
490
....*....|....*....
gi 2462611208 1435 LGQRQLLCLARALLTDAKV 1453
Cdd:COG2274 614 GGQRQRLAIARALLRNPRI 632
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
370-622 |
3.10e-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: 153.92 E-value: 3.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 370 PLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKALQLGPS---RPPTGEALNLLGTDSERLLNFA 446
Cdd:cd18593 35 SLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAalgKTTVGQIVNLLSNDVNRFDQAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 447 GSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIAtRIMASN-QEMLQHKDARVKLVTELLSGIRVIKF 525
Cdd:cd18593 115 LFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG-KLFSKLrRKTAARTDKRIRIMNEIINGIRVIKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 526 CGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITYVLMGHQLTATKVFTALALVRMLILPLNN- 604
Cdd:cd18593 194 YAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILTAERVFVTMALYNAVRLTMTLf 273
|
250
....*....|....*...
gi 2462611208 605 FPWVINGLLEAKVSLDRI 622
Cdd:cd18593 274 FPFAIQFGSELSVSIRRI 291
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1297-1453 |
1.57e-37 |
|
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: 139.06 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1376
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 1377 IPQEPFLFSGTVRENLdpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03228 81 VPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
341-622 |
1.79e-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: 137.31 E-value: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 341 LLKLVGTMLGFSGPLLL-SLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKAL 419
Cdd:cd18592 4 LLLLISLIFGFIGPTILiRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 420 QL-GPSRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQL----AITLYLLyqqvG-VAFVGGLILaLLLVPVNKVIAT 493
Cdd:cd18592 84 RLrSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLilgiVYSTYLL----GpWALLGMLVF-LLFYPLQAFIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 494 RIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIF 573
Cdd:cd18592 159 LTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTF 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462611208 574 ITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 622
Cdd:cd18592 239 LAHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1295-1453 |
3.59e-35 |
|
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: 134.28 E-value: 3.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1295 GGVEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1374
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1375 AIIPQEPFLFSGTVRENLDPQGLHKDRALWQ-ALKQCHLSEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARALLTDAK 1452
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNgYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
.
gi 2462611208 1453 V 1453
Cdd:cd03254 160 I 160
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
649-857 |
1.01e-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: 132.71 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 649 LELHGALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFG 718
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVS-LTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 719 LATQEPWIQFATIRDNILFGKTF-DAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKEL 797
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 798 YLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 857
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
374-848 |
3.82e-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: 139.34 E-value: 3.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 374 GLLYALGLAGGAVLG-AVLQNQYGYEVYKVTLQARGAVLNILYCKALQLGP---SRPPTGEALNLLGTDSERLLNFAGSF 449
Cdd:TIGR02857 42 ELLPALGALALVLLLrALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPrwlQGRPSGELATLALEGVEALDGYFARY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 450 heawgLP-LQLA--ITLYLLYQQVGVAFVGGLIL--ALLLVPVNKV-IATRIMASNQEMLQHKDARVKLVTELLSGIRVI 523
Cdd:TIGR02857 122 -----LPqLVLAviVPLAILAAVFPQDWISGLILllTAPLIPIFMIlIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 524 KFCGWEQALGARV----EACRARELGRLRvIKYLDAACVYLWAALPVVIsIVIFITYVLMGHQLTATKVFTALALVRMLI 599
Cdd:TIGR02857 197 KLFGRAKAQAAAIrrssEEYRERTMRVLR-IAFLSSAVLELFATLSVAL-VAVYIGFRLLAGDLDLATGLFVLLLAPEFY 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 600 LPLNNFPWVINGLLEAKVSLDRIQLFLDlpnHNPQAYYSPDP-PAEPSTVLELHGALFSW---DPVGTSLEtfishLEVK 675
Cdd:TIGR02857 275 LPLRQLGAQYHARADGVAAAEALFAVLD---AAPRPLAGKAPvTAAPASSLEFSGVSVAYpgrRPALRPVS-----FTVP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 676 KGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGKTF-DAQ 744
Cdd:TIGR02857 347 PGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadsWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 745 LYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGML 824
Cdd:TIGR02857 427 EIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA-LRALA 505
|
490 500
....*....|....*....|....
gi 2462611208 825 SYTTRLLCTHRTEYLERADAVLLM 848
Cdd:TIGR02857 506 QGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1297-1453 |
9.88e-32 |
|
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: 124.65 E-value: 9.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1376
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1377 IPQEPFLFSGTVRENL---DPQGLHKDraLWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAK 1452
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGATREE--VEEAARAANAHEFIMELPEGYDTVIGERGVkLSGGQRQRIAIARALLKDPP 158
|
.
gi 2462611208 1453 V 1453
Cdd:cd03251 159 I 159
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1295-1448 |
2.52e-31 |
|
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: 124.25 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1295 GGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1374
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 1375 AIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLD-GELGEGGRSLSLGQRQLLCLARALL 1448
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdAVVTEGGENFSVGQRQLFCLARAFV 172
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1278-1453 |
2.84e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 131.03 E-value: 2.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1278 QEPQGQPLQLGTGWLTQGGVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL 1357
Cdd:COG4988 318 PEPAAPAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1358 DGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGG-LDGELGEGGRSL 1433
Cdd:COG4988 397 NGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRPDA--SDEELEAALEAAGLDEFVAALPDgLDTPLGEGGRGL 474
|
170 180
....*....|....*....|
gi 2462611208 1434 SLGQRQLLCLARALLTDAKV 1453
Cdd:COG4988 475 SGGQAQRLALARALLRDAPL 494
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1295-1450 |
4.20e-31 |
|
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: 122.31 E-value: 4.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1295 GGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1374
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1375 AIIPQEPFLFSGTVRENL---DPqgLHKDRALWQALKQCHLSEVI-TSMGGLDGELGEGGRSLSLGQRQLLCLARALLTD 1450
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAP--LADDERILRAAELAGVTDFVnKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1025-1453 |
6.96e-31 |
|
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: 129.84 E-value: 6.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1025 IAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDV----ACADDSLPFILNILLAN 1100
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSeqvaSAATDAFIVLVRETLTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1101 AAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRL-GSLTLSplyshLADTLAGLSVLRATGA----TY 1175
Cdd:TIGR02203 143 IGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSmGQVTTV-----AEETLQGYRVVKLFGGqayeTR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1176 RFEEENLRLLELNQRCQFATSAtmqwLDIRLQLMGAAVVSAIAGIALVQHQQGLANPG-LVGLSLSYALSLTGLLSGL-V 1253
Cdd:TIGR02203 218 RFDAVSNRNRRLAMKMTSAGSI----SSPITQLIASLALAVVLFIALFQAQAGSLTAGdFTAFITAMIALIRPLKSLTnV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1254 SSFTQTeaMLVSVERLEEYTcDLPQEPQGQPLQLGTgwlTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRT 1333
Cdd:TIGR02203 294 NAPMQR--GLAAAESLFTLL-DSPPEKDTGTRAIER---ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1334 GSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQGLHKDRALwQALKQC 1410
Cdd:TIGR02203 368 GSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTEQADRAEIE-RALAAA 446
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462611208 1411 HLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKV 1453
Cdd:TIGR02203 447 YAQDFVDKLPLGLDTPIGENGVlLSGGQRQRLAIARALLKDAPI 490
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
672-852 |
1.13e-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: 116.33 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILfgktf 741
Cdd:cd03228 23 LTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldlesLRKNIAYVPQDPFLFSGTIRENIL----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 742 daqlykevleacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCIL 821
Cdd:cd03228 98 ------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPE-TEALILEALR 140
|
170 180 190
....*....|....*....|....*....|.
gi 2462611208 822 GMLSYTTRLLCTHRTEYLERADAVLLMEAGR 852
Cdd:cd03228 141 ALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
406-835 |
2.76e-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: 124.40 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 406 ARGAVLNILYCKALqLGPSRPPTGEALNLLGTDSERLLNFagsfHEAWGLPLQLAITLYL--------LYQQVGVAFVGG 477
Cdd:TIGR02868 88 LRVRVYERLARQAL-AGRRRLRRGDLLGRLGADVDALQDL----YVRVIVPAGVALVVGAaavaaiavLSVPAALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 478 LILALLLVPVnkvIATRIMASNQEMLQHKDARV-KLVTELLSGIRVIKFCGWEQALGARVEAcRARELGRLR----VIKY 552
Cdd:TIGR02868 163 LLLAGFVAPL---VSLRAARAAEQALARLRGELaAQLTDALDGAAELVASGALPAALAQVEE-ADRELTRAErraaAATA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 553 LDAACVYLWAALPVVISIVIFITYVlMGHQLT----ATKVFTALALVRmlilPLNNFPWVINGLLEAKVSLDRIqlfLDL 628
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAV-ADGRLApvtlAVLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERI---VEV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 629 PNHNPQAYYSPDPPAEPSTV----LELHGALFSWDPvGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRL 704
Cdd:TIGR02868 311 LDAAGPVAEGSAPAAGAVGLgkptLELRDLSAGYPG-APPVLDGVS-LDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 705 RGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGK--TFDAQLYkEVLEACALNDDLSILPAGDQTEVGE 772
Cdd:TIGR02868 389 QGEVTLDGvpvssldqdeVRRRVSVCAQDAHLFDTTVRENLRLARpdATDEELW-AALERVGLADWLRALPDGLDTVLGE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 773 KGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHR 835
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHH 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
672-863 |
6.27e-29 |
|
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: 116.87 E-value: 6.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAI-------AGELHrLRGH----VAVRGLSKGFGLATQEPWIQFATIRDNILFGKt 740
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEIL-LDGVdirdLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 741 FDAQLyKEVLEAC--ALNDDLSI-LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD---VANH 814
Cdd:cd03249 102 PDATD-EEVEEAAkkANIHDFIMsLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEsekLVQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462611208 815 LLHRCILGMlsytTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:cd03249 181 ALDRAMKGR----TTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1297-1453 |
2.18e-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: 114.94 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAY--RPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1374
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1375 AIIPQEPFLFSGTVRENL---DPQGLHKDRAlwQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTD 1450
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygKPDATDEEVE--EAAKKANIHDFIMSLPDGYDTLVGERGSqLSGGQKQRIAIARALLRN 157
|
...
gi 2462611208 1451 AKV 1453
Cdd:cd03249 158 PKI 160
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
671-863 |
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 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGK- 739
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrksLRSMIGVVLQDTFLFSGTIMENIRLGRp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 740 TFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANhLLHRC 819
Cdd:cd03254 103 NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK-LIQEA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462611208 820 ILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:cd03254 182 LEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
672-863 |
3.05e-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: 108.86 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAI-------AGELhRLRGH----VAVRGLSKGFGLATQEPWIQFATIRDNILFGKt 740
Cdd:cd03251 23 LDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRI-LIDGHdvrdYTLASLRRQIGLVSQDVFLFNDTVAENIAYGR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 741 FDAQLyKEVLEA---CALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDaDVANHLLH 817
Cdd:cd03251 101 PGATR-EEVEEAaraANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD-TESERLVQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462611208 818 RCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:cd03251 179 AALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
671-857 |
3.74e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 115.33 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAG-------------ELHRL-----RGHVAVRGlskgfglatQEPWIQFATIR 732
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingiELRELdpeswRKHLSWVG---------QNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 733 DNILFGKTF--DAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 810
Cdd:PRK11174 441 DNVLLGNPDasDEQLQ-QALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462611208 811 VANHLLHRCILGMLSYTTrLLCTHRTEYLERADAVLLMEAGRLIRAG 857
Cdd:PRK11174 520 SEQLVMQALNAASRRQTT-LMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1314-1453 |
5.10e-26 |
|
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: 105.42 E-value: 5.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSG-TVRENL 1392
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 1393 -------DPQGLHKDRALWQALKQCHLSEVITSmggldgELGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDLADR------PVGERPGTLSGGQRQRVAIARALLTKPKL 142
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
649-863 |
7.18e-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: 107.96 E-value: 7.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 649 LELHGALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFG 718
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNIS-LRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 719 LATQEPWIQFATIRDNILFGKTfdAQLYKEVLEACAL---NDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEK 795
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADP--GMSMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 796 ELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:cd03252 158 RILIFDEATSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1297-1453 |
1.20e-25 |
|
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: 107.19 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1376
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1377 IPQEPFLFSGTVRENL---DPqGLHKDRALWQA-LKQCHlsEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARALLTDA 1451
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP-GMSMERVIEAAkLAGAH--DFISELPEgYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
..
gi 2462611208 1452 KV 1453
Cdd:cd03252 158 RI 159
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1295-1453 |
2.57e-24 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 104.55 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1295 GGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEpSSGRVLLDGVDTSQLELAQLRSQL 1374
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1375 AIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCvLSHGHKQLMCLARSVLSKAKI 159
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
672-859 |
3.34e-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: 102.57 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNI-LFGKT 740
Cdd:cd03244 25 FSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdLRSRISIIPQDPVLFSGTIRSNLdPFGEY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 741 FDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLLHRCI 820
Cdd:cd03244 105 SDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETD-ALIQKTI 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462611208 821 LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPP 859
Cdd:cd03244 183 REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1267-1453 |
4.57e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 109.43 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1267 ERLEEYTCDLPQEPQgqPLQLGTGWLtQGGVEFQDVVLAY--RPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVL 1344
Cdd:TIGR00958 452 EKVFEYLDRKPNIPL--TGTLAPLNL-EGLIEFQDVSFSYpnRPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1345 FRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLdPQGLHK--DRALWQALKQCHLSEVITSMGGL 1422
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENI-AYGLTDtpDEEIMAAAKAANAHDFIMEFPNG 606
|
170 180 190
....*....|....*....|....*....|..
gi 2462611208 1423 DGELGEGGRS-LSLGQRQLLCLARALLTDAKV 1453
Cdd:TIGR00958 607 YDTEVGEKGSqLSGGQKQRIAIARALVRKPRV 638
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1297-1453 |
2.27e-23 |
|
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: 100.38 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1376
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1377 IPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMgGLDGELGEGGRSLSL--GQRQLLCLARALLTDA 1451
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPDA--TDEEVIEAAKAAQIHDKIMRF-PDGYDTIVGERGLKLsgGEKQRVAIARAILKNP 156
|
..
gi 2462611208 1452 KV 1453
Cdd:cd03253 157 PI 158
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1137-1453 |
3.59e-23 |
|
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: 105.52 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1137 RASSRELRRLgsltLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQL-MGAAVVS 1215
Cdd:TIGR02868 179 RAAEQALARL----RGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLaAGLAVLG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1216 AI--AGIALVQHQQG---LANPGLVGLSLSYALSLTGLlsglvsSFTQTEAMLVSVERLEEYTCDLPQEPQGQPLQLGTG 1290
Cdd:TIGR02868 255 ALwaGGPAVADGRLApvtLAVLVLLPLAAFEAFAALPA------AAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1291 WLTQGGVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL 1370
Cdd:TIGR02868 329 GLGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1371 RSQLAIIPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARA 1446
Cdd:TIGR02868 408 RRRVSVCAQDAHLFDTTVRENLrlaRPDA--TDEELWAALERVGLADWLRALPDgLDTVLGEGGARLSGGERQRLALARA 485
|
....*..
gi 2462611208 1447 LLTDAKV 1453
Cdd:TIGR02868 486 LLADAPI 492
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1297-1453 |
1.53e-22 |
|
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: 96.23 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLAI 1376
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 1377 IPQEPFLFSGTVRENLdpqglhkdralwqalkqchlsevitsmggldgelgegGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03247 80 LNQRPYLFDTTLRNNL-------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1292-1451 |
2.43e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 103.37 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1292 LTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLR 1371
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1372 SQLAIIPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALL 1448
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALL 491
|
...
gi 2462611208 1449 TDA 1451
Cdd:PRK11160 492 HDA 494
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
672-853 |
2.61e-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: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFG-KT 740
Cdd:cd03248 35 FTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkyLHSKVSLVGQEPVLFARSLQDNIAYGlQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 741 FDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCI 820
Cdd:cd03248 115 CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQVQQAL 193
|
170 180 190
....*....|....*....|....*....|...
gi 2462611208 821 LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRL 853
Cdd:cd03248 194 YDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1279-1453 |
3.96e-22 |
|
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: 102.36 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1279 EPQGQPL--QLGTGWLTQGGVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVL 1356
Cdd:TIGR02857 302 DAAPRPLagKAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1357 LDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGGLDGELG-EGGRS 1432
Cdd:TIGR02857 381 VNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--SDAEIREALERAGLDEFVAALPQGLDTPIgEGGAG 458
|
170 180
....*....|....*....|.
gi 2462611208 1433 LSLGQRQLLCLARALLTDAKV 1453
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPL 479
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
672-855 |
4.05e-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: 96.39 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV-----AVRGLSKGFGLATQE----PWiqfATIRDNILFGKTF- 741
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgePVTGPGPDRGYVFQQdallPW---LTVLDNVALGLELq 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 742 ---DAQLYKEVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 812
Cdd:cd03293 102 gvpKAEARERAEELLEL--------------VGLSGFenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462611208 813 NHlLHRCILGMLSYT--TRLLCTHRTE---YLerADAVLLMEA--GRLIR 855
Cdd:cd03293 168 EQ-LQEELLDIWRETgkTVLLVTHDIDeavFL--ADRVVVLSArpGRIVA 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
671-872 |
2.30e-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: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEpwIQF--ATIRDNI-LF 737
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreeLGRHIGYLPQD--VELfdGTIAENIaRF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 GKTfDAQlykEVLEACALND--DLsI--LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN 813
Cdd:COG4618 430 GDA-DPE---KVVAAAKLAGvhEM-IlrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEA 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 814 HLLhRCILGM-LSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPKA 872
Cdd:COG4618 505 ALA-AAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
671-805 |
2.83e-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: 91.56 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQ-FATIRDNILFG- 738
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderksLRKEIGYVFQDPQLFpRLTVRENLRLGl 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 739 -------KTFDAQLYkEVLEACALNDDLSilpagdqTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLA 805
Cdd:pfam00005 85 llkglskREKDARAE-EALEKLGLGDLAD-------RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
479-862 |
3.42e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.18 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 479 ILALLLVP----VNKVIATRIMASNQEmLQHKDARV-KLVTELLSGIRVIKFCGWEQalgarVEACRARE-------LGR 546
Cdd:TIGR00958 305 MVTLINLPlvflAEKVFGKRYQLLSEE-LQEAVAKAnQVAEEALSGMRTVRSFAAEE-----GEASRFKEaleetlqLNK 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 547 LRVIKYLdaacVYLWAAlpVVISIVIFITYVLMGHQLTATKVFTALALVRMLILP------LNNFPWVINGLLEAKVSLD 620
Cdd:TIGR00958 379 RKALAYA----GYLWTT--SVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQeqlgeaVRVLSYVYSGMMQAVGASE 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 621 RIQLFLDL-PNHNPQAYYSPDPPaepSTVLELHGALFSW-----DPVGTSLeTFishlEVKKGMLVGIVGKVGCGKSSLL 694
Cdd:TIGR00958 453 KVFEYLDRkPNIPLTGTLAPLNL---EGLIEFQDVSFSYpnrpdVPVLKGL-TF----TLHPGEVVALVGPSGSGKSTVA 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 695 AAI-------AGEL------------HRLRGHVAVRGlskgfglatQEPWIQFATIRDNILFGKTF--DAQLYKEVLEAC 753
Cdd:TIGR00958 525 ALLqnlyqptGGQVlldgvplvqydhHYLHRQVALVG---------QEPVLFSGSVRENIAYGLTDtpDEEIMAAAKAAN 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 754 AlNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVaNHLLH--RCILGMlsytTRLL 831
Cdd:TIGR00958 596 A-HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-EQLLQesRSRASR----TVLL 669
|
410 420 430
....*....|....*....|....*....|.
gi 2462611208 832 CTHRTEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:TIGR00958 670 IAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
671-858 |
3.72e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 99.40 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAI-------AGE------------LHRLRGHVAVrglskgfglATQEPWIQFATI 731
Cdd:PRK10789 335 NFTLKPGQMLGICGPTGSGKSTLLSLIqrhfdvsEGDirfhdipltklqLDSWRSRLAV---------VSQTPFLFSDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 732 RDNILFGKTfDA--QLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 809
Cdd:PRK10789 406 ANNIALGRP-DAtqQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 810 DVANHLLHRcilgmLS----YTTRLLCTHRTEYLERADAVLLMEAGRLIRAGP 858
Cdd:PRK10789 485 RTEHQILHN-----LRqwgeGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
672-862 |
3.82e-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: 94.33 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGfGLATQEPWIQFA----------TIRDNILFG--- 738
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT-DVPVQERNVGFVfqhyalfrhmTVFDNVAFGlrv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 --------KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 810
Cdd:cd03296 102 kprserppEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 811 VANHL------LHRCIlgmlsYTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:cd03296 171 VRKELrrwlrrLHDEL-----HVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1294-1451 |
4.31e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 99.65 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1294 QGGVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ 1373
Cdd:PRK13657 332 KGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1374 LAIIPQEPFLFSGTVRENL---DPQGLHKDraLWQALKQCHLSEVI-TSMGGLDGELGEGGRSLSLGQRQLLCLARALLT 1449
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIrvgRPDATDEE--MRAAAERAQAHDFIeRKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
..
gi 2462611208 1450 DA 1451
Cdd:PRK13657 489 DP 490
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
656-863 |
5.69e-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: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 656 FSWDPVGTSLETfIShLEVKKGMLVGIVGKVGCGKSSLLAAiageLHRL----RGHVAVRG----------LSKGFGLAT 721
Cdd:cd03253 8 FAYDPGRPVLKD-VS-FTIPAGKKVAIVGPSGSGKSTILRL----LFRFydvsSGSILIDGqdirevtldsLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 722 QEPWIQFATIRDNILFGK--TFDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYL 799
Cdd:cd03253 82 QDTVLFNDTIGYNIRYGRpdATDEEVI-EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 800 LDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:cd03253 161 LDEATSALDT-HTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
672-857 |
7.50e-21 |
|
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: 91.61 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG---------LSKGFGLATQEPWIQFATIRDNIlfgktfd 742
Cdd:cd03247 23 LELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekaLSSLISVLNQRPYLFDTTLRNNL------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 743 aqlykevleacalnddlsilpagdqtevgekGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhRCILG 822
Cdd:cd03247 96 -------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL-SLIFE 143
|
170 180 190
....*....|....*....|....*....|....*
gi 2462611208 823 MLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 857
Cdd:cd03247 144 VLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1294-1453 |
1.18e-20 |
|
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: 92.53 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1294 QGGVEFQDVVLAY--RPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLR 1371
Cdd:cd03248 9 KGIVKFQNVTFAYptRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1372 SQLAIIPQEPFLFSGTVRENLdPQGLHK--DRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALL 1448
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNI-AYGLQScsFECVKEAAQKAHAHSFISELASGYDTEVGEKGSqLSGGQKQRVAIARALI 166
|
....*
gi 2462611208 1449 TDAKV 1453
Cdd:cd03248 167 RNPQV 171
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
672-857 |
1.39e-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: 91.81 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------KGFGLATQE----PWIqfaTIRDNILFG- 738
Cdd:cd03259 21 LTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperRNIGMVFQDyalfPHL---TVAENIAFGl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 ---KTFDAQLYKEVLEACALNDDLSILpagdqtevGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL 815
Cdd:cd03259 98 klrGVPKAEIRARVRELLELVGLEGLL--------NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462611208 816 LH--RCILGMLSYTTrLLCTH-RTEYLERADAVLLMEAGRLIRAG 857
Cdd:cd03259 170 REelKELQRELGITT-IYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1295-1453 |
1.40e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 98.27 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1295 GGVEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1374
Cdd:TIGR01193 472 GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1375 AIIPQEPFLFSGTVRENL---DPQGLHKDRaLWQALKQCHLSEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARALLTD 1450
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLllgAKENVSQDE-IWAACEIAEIKDDIENMPLgYQTELSEEGSSISGGQKQRIALARALLTD 629
|
...
gi 2462611208 1451 AKV 1453
Cdd:TIGR01193 630 SKV 632
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
672-852 |
1.49e-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: 91.76 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFG- 738
Cdd:cd03225 22 LTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkeLRRKVGLVFQNPDDQFfgPTVEEEVAFGl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 ------KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD---- 808
Cdd:cd03225 102 enlglpEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDpagr 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462611208 809 ADVANHLLHRCILGMlsytTRLLCTHRTEYLER-ADAVLLMEAGR 852
Cdd:cd03225 171 RELLELLKKLKAEGK----TIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1298-1447 |
3.22e-20 |
|
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: 89.58 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1298 EFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAII 1377
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1378 PQEPFLFSGTVRENLdpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARAL 1447
Cdd:cd03246 82 PQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARAL 111
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
672-855 |
3.57e-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: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV-----AVRGLSKGFGLATQE----PWiqfATIRDNILFG---- 738
Cdd:COG1116 32 LTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVlvdgkPVTGPGPDRGVVFQEpallPW---LTVLDNVALGlelr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 ---KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHl 815
Cdd:COG1116 109 gvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRER- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462611208 816 LHRCILGMLSYT--TRLLCTHRTE---YLerADAVLLMEA--GRLIR 855
Cdd:COG1116 177 LQDELLRLWQETgkTVLFVTHDVDeavFL--ADRVVVLSArpGRIVE 221
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1013-1269 |
3.79e-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: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1013 SDIRFYLTVYATIAGVNSLCTL--LRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSL 1090
Cdd:cd18600 65 TFTSSYYVFYIYVGVADSLLAMgfFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1091 PFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRA 1170
Cdd:cd18600 145 PLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1171 TGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlanPGLVGLSLSYALSLTGLLS 1250
Cdd:cd18600 225 FGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDG---EGRVGIILTLAMNIMSTLQ 301
|
250
....*....|....*....
gi 2462611208 1251 GLVSSFTQTEAMLVSVERL 1269
Cdd:cd18600 302 WAVNTSIDVDSLMRSVSRI 320
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
561-901 |
4.64e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.18 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 561 WAALPVV-------ISIV-IFI--TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVsldRIQLFLDLPN 630
Cdd:PRK13657 238 WWALASVlnraastITMLaILVlgAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAP---KLEEFFEVED 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 631 HNPQAYYSPD--PPAEPSTVLELHGALFSWDPVGTSLE--TFishlEVKKGMLVGIVGKVGCGKSSLLAAiageLHRL-- 704
Cdd:PRK13657 315 AVPDVRDPPGaiDLGRVKGAVEFDDVSFSYDNSRQGVEdvSF----EAKPGQTVAIVGPTGAGKSTLINL----LQRVfd 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 705 --RGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGKT--FDAQLYkEVLEACALNDDLSILPAGDQTEV 770
Cdd:PRK13657 387 pqSGRILIDGtdirtvtrasLRRNIAVVFQDAGLFNRSIEDNIRVGRPdaTDEEMR-AAAERAQAHDFIERKPDGYDTVV 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 771 GEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEA 850
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV-ETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDN 544
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 851 GRLIRAGPPSEILplvqavpkawAENGQESDSATAQSVQNPEKTKEGLEEE 901
Cdd:PRK13657 545 GRVVESGSFDELV----------ARGGRFAALLRAQGMLQEDERRKQPAAE 585
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1298-1453 |
5.19e-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: 90.22 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1298 EFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAII 1377
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1378 PQEPF--LFSGTVRE----NLDPQGLHKD---RALWQALKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLARALL 1448
Cdd:cd03225 81 FQNPDdqFFGPTVEEevafGLENLGLPEEeieERVEEALELVGLEG----------LRDRSPFTLSGGQKQRVAIAGVLA 150
|
....*
gi 2462611208 1449 TDAKV 1453
Cdd:cd03225 151 MDPDI 155
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1275-1418 |
1.09e-19 |
|
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: 95.27 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1275 DLPQE----PQGQPLQLgtgwlTQGGVEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP 1350
Cdd:COG5265 337 DQPPEvadaPDAPPLVV-----GGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV 410
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 1351 SSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQGLHKDraLWQALKQCHLSEVITS 1418
Cdd:COG5265 411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPDASEEE--VEAAARAAQIHDFIES 479
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
672-863 |
1.67e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 91.75 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH------RLRGHVAVRGLS---KGFGLATQepwiQFA-----TIRDNILF 737
Cdd:COG1118 23 LEIASGELVALLGPSGSGKTTLLRIIAGLETpdsgriVLNGRDLFTNLPpreRRVGFVFQ----HYAlfphmTVAENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 GktfdaqlykevleacalnddLSILPAGDQtEVGEKgVT------------------LSGGQRARIALARAVYQEKELYL 799
Cdd:COG1118 99 G--------------------LRVRPPSKA-EIRAR-VEellelvqlegladrypsqLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 800 LDDPLAAVDADVANHL------LHRCILGmlsytTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG1118 157 LDEPFGALDAKVRKELrrwlrrLHDELGG-----TTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1297-1453 |
1.99e-19 |
|
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: 93.81 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPN---ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQL 1370
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1371 RSQLAIIPQEPF--LFSG-TVRENL-DPQGLH--------KDRALwQALKQCHLSEvitsmggldGELGEGGRSLSLGQR 1438
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIaEPLRLHgllsraerRERVA-ELLERVGLPP---------DLADRYPHELSGGQR 410
|
170
....*....|....*
gi 2462611208 1439 QLLCLARALLTDAKV 1453
Cdd:COG1123 411 QRVAIARALALEPKL 425
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
672-863 |
2.61e-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: 88.54 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFG- 738
Cdd:COG1122 22 LSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlreLRRKVGLVFQNPDDQLfaPTVEEDVAFGp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 -------KTFDAQLyKEVLEACALND--DLSILpagdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 809
Cdd:COG1122 102 enlglprEEIRERV-EEALELVGLEHlaDRPPH-------------ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 810 DVANHLLHrcILGML--SYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG1122 168 RGRRELLE--LLKRLnkEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
672-853 |
6.37e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 86.79 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS----------KGFGLATQEPWIQFATIRDNILF---- 737
Cdd:COG4619 21 LTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrRQVAYVPQEPALWGGTVRDNLPFpfql 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 -GKTFDAQLYKEVLEACALNDDlsILpagdQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLL 816
Cdd:COG4619 101 rERKFDRERALELLERLGLPPD--IL----DKPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT-RRV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462611208 817 HRCILGMLSY--TTRLLCTHRTEYLER-ADAVLLMEAGRL 853
Cdd:COG4619 170 EELLREYLAEegRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1297-1453 |
7.64e-19 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 86.77 E-value: 7.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 1371
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1372 -SQLAIIPQE----PFLfsgTVRENL--------DPQGLHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQR 1438
Cdd:cd03255 81 rRHIGFVFQSfnllPDL---TALENVelplllagVPKKERRERAE-ELLERVGLGDRLNHY----------PSELSGGQQ 146
|
170
....*....|....*
gi 2462611208 1439 QLLCLARALLTDAKV 1453
Cdd:cd03255 147 QRVAIARALANDPKI 161
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
672-863 |
8.00e-19 |
|
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: 87.79 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFA-TIRDNILFGKT 740
Cdd:COG1120 22 LSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrreLARRIAYVPQEPPAPFGlTVRELVALGRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 741 --------FDAQLYKEVLEACAlnddlsilpagdQTEVG---EKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVD 808
Cdd:COG1120 102 phlglfgrPSAEDREAVEEALE------------RTGLEhlaDRPVdELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 809 advANHLLHrcILGMLSYTTR------LLCTH------RTeylerADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG1120 170 ---LAHQLE--VLELLRRLARergrtvVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGPPEEVL 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
672-863 |
1.06e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 87.04 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS---------KGFGLATQEPWI-QFATIRDNILF---- 737
Cdd:COG1131 21 LTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvardpaevrRRIGYVPQEPALyPDLTVRENLRFfarl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 ---GKTFDAQLYKEVLEACALNDDLsilpagdqtevGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANH 814
Cdd:COG1131 101 yglPRKEARERIDELLELFGLTDAA-----------DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP-EARR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 815 LLHRCILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG1131 169 ELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
671-857 |
1.14e-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: 86.19 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVK---KGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL-----SKGFGLATQEPWIQFA----------TIR 732
Cdd:cd03297 14 TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVfqqyalfphlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 733 DNILFGKTF-----DAQLYKEVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAA 806
Cdd:cd03297 94 ENLAFGLKRkrnreDRISVDELLDLLGL------------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 807 VDADVANHLLH--RCILGMLSYTTrLLCTHRTEYLER-ADAVLLMEAGRLIRAG 857
Cdd:cd03297 162 LDRALRLQLLPelKQIKKNLNIPV-IFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
672-852 |
1.91e-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: 83.83 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFglatqepwIQFATIRDNIlfgktfdaqlykevle 751
Cdd:cd00267 20 LTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--------LPLEELRRRI---------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 752 acalnddlSILPagdQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLLHRCILGML-SYTTRL 830
Cdd:cd00267 76 --------GYVP---Q---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAeEGRTVI 134
|
170 180
....*....|....*....|...
gi 2462611208 831 LCTHRTEYLERA-DAVLLMEAGR 852
Cdd:cd00267 135 IVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
671-862 |
1.91e-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: 86.08 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAG-----ELHRLRGHVAVRG------------LSKGFGLATQEPWIQFATIRD 733
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGkdiydldvdvleLRRRVGMVFQKPNPFPGSIYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 734 NILFG--------KTFDAQLYKEVLEACALNDDLSilpagDQTevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLA 805
Cdd:cd03260 100 NVAYGlrlhgiklKEELDERVEEALRKAALWDEVK-----DRL----HALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 806 AVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 862
Cdd:cd03260 171 ALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
673-859 |
2.19e-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: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 673 EVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNI-LFGKTF 741
Cdd:cd03369 30 KVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledLRSSLTIIPQDPTLFSGTIRSNLdPFDEYS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 742 DAQLYKevleacALnddlsilpagdqtEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCIL 821
Cdd:cd03369 110 DEEIYG------AL-------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA-TDALIQKTIR 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462611208 822 GMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPP 859
Cdd:cd03369 170 EEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
618-863 |
2.70e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.58 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 618 SLDRIQLFLDLPNHNPQAYYSPDPPAE-PST--------VLELHGALfswDPVGTSLETFISHLEVkkgmlVGIVGKVGC 688
Cdd:PLN03232 1202 SVERVGNYIDLPSEATAIIENNRPVSGwPSRgsikfedvHLRYRPGL---PPVLHGLSFFVSPSEK-----VGVVGRTGA 1273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 689 GKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYkEVLEACALND 757
Cdd:PLN03232 1274 GKSSMLNALFRIVELEKGRIMIDDcdvakfgltdLRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDADLW-EALERAHIKD 1352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 758 DLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVaNHLLHRCILGMLSYTTRLLCTHRTE 837
Cdd:PLN03232 1353 VIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-DSLIQRTIREEFKSCTMLVIAHRLN 1431
|
250 260
....*....|....*....|....*.
gi 2462611208 838 YLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PLN03232 1432 TIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
671-863 |
3.85e-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: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGF---------GLATQEPWI-QFATIRDNILFgkt 740
Cdd:COG4555 21 SFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKeprearrqiGVLPDERGLyDRLTVRENIRY--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 741 FdAQLYKEVLEACALNDDlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRC 819
Cdd:COG4555 98 F-AELYGLFDEELKKRIE-ELIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM-ARRLLREI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462611208 820 ILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG4555 175 LRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1297-1453 |
5.49e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 84.71 E-value: 5.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 1371
Cdd:COG1136 5 LELRNLTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1372 SQ-LAIIPQEPFLFSG-TVREN----LDPQGLHK----DRALwQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLL 1441
Cdd:COG1136 85 RRhIGFVFQFFNLLPElTALENvalpLLLAGVSRkerrERAR-ELLERVGLGDRLDHRP----------SQLSGGQQQRV 153
|
170
....*....|..
gi 2462611208 1442 CLARALLTDAKV 1453
Cdd:COG1136 154 AIARALVNRPKL 165
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
672-867 |
5.69e-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: 84.86 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------------LSKGFGLATQepwiQFA-----TIRD 733
Cdd:cd03261 21 LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrLRRRMGMLFQ----SGAlfdslTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 734 NILF--------GKTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLA 805
Cdd:cd03261 97 NVAFplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 806 AVD---ADVANHLLHRC--ILGMlsytTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL----PLVQ 867
Cdd:cd03261 166 GLDpiaSGVIDDLIRSLkkELGL----TSIMVTHDlDTAFAIADRIAVLYDGKIVAEGTPEELRasddPLVR 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1297-1450 |
6.17e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 84.33 E-value: 6.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ 1373
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1374 LAIIPQE-PFLFSGTVREN----LDPQGLHKD---RALWQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLAR 1445
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENvalpLRVTGKSRKeirRRVREVLDLVGLSDKAKAL----------PHELSGGEQQRVAIAR 150
|
....*
gi 2462611208 1446 ALLTD 1450
Cdd:COG2884 151 ALVNR 155
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1297-1453 |
6.17e-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: 84.54 E-value: 6.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGlpNALDGVTFCVQPGEKLGIVGRTGSGKSSL-----LLVLFRLLEPSSGRVLLDGVD--TSQLELAQ 1369
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLlrllnRLNDLIPGAPDEGEVLLDGKDiyDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1370 LRSQLAIIPQEPFLFSGTVRENLD----PQGLHKDRAL----WQALKQCHLSEvitsmgglDGELGEGGRSLSLGQRQLL 1441
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEELdervEEALRKAALWD--------EVKDRLHALGLSGGQQQRL 150
|
170
....*....|..
gi 2462611208 1442 CLARALLTDAKV 1453
Cdd:cd03260 151 CLARALANEPEV 162
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
671-853 |
1.16e-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: 82.26 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILfgkt 740
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpneLGDHVGYLPQDDELFSGSIAENIL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 741 fdaqlykevleacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCI 820
Cdd:cd03246 98 -------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVE-GERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....
gi 2462611208 821 LGM-LSYTTRLLCTHRTEYLERADAVLLMEAGRL 853
Cdd:cd03246 140 AALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1294-1453 |
1.42e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.15 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1294 QGGVEFQDVVLAYrPGLPN-ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRS 1372
Cdd:PRK11176 339 KGDIEFRNVTFTY-PGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1373 QLAIIPQEPFLFSGTVRENL--DPQGLHKDRALWQALKQCHLSEVITSMGGLD-GELGEGGRSLSLGQRQLLCLARALLT 1449
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLdTVIGENGVLLSGGQRQRIAIARALLR 497
|
....
gi 2462611208 1450 DAKV 1453
Cdd:PRK11176 498 DSPI 501
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
337-622 |
1.54e-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: 84.91 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 337 LALGLLkLVGTMLGFSGPLLLSLLVGFLEeGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYC 416
Cdd:cd07346 3 LALLLL-LLATALGLALPLLTKLLIDDVI-PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 417 KALQLGPS---RPPTGEALNLLGTDSERLLNFAGS-FHEAWGLPLQLAITL-YLLYQQVGVAFVGgLILALLLVPVNKVI 491
Cdd:cd07346 81 HLQRLSLSffdRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALvILFYLNWKLTLVA-LLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 492 ATRIMASNQEmLQHKDARV-KLVTELLSGIRVIKFCGWEQALGARVEAcRARELGRLRV-IKYLDAACVYLWAALPVVIS 569
Cdd:cd07346 160 RRRIRKASRE-VRESLAELsAFLQESLSGIRVVKAFAAEEREIERFRE-ANRDLRDANLrAARLSALFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 570 IVIFI--TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 622
Cdd:cd07346 238 ALVLLygGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
337-602 |
1.57e-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: 84.62 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 337 LALGLLKLVGTMLGFSGPLLLSLLVG-FLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILY 415
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDvLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 416 CKALQLGPS---RPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLL--YQQVGVAFVGgLILALLLVPVNKV 490
Cdd:pfam00664 82 KKILRQPMSffdTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVmfYYGWKLTLVL-LAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 491 IATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGR-LRVIKYLDAACVYLWAALPVVIS 569
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAgIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 2462611208 570 IVIFI-TYVLMGHQLTATKVFTALALVRMLILPL 602
Cdd:pfam00664 241 LALWFgAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
672-888 |
1.81e-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: 87.65 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGEL---HRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNIL 736
Cdd:COG1123 27 LTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGrdllelsealRGRRIGMVFQDPMTQLnpVTVGDQIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 737 FG----KTFDAQLYKEVLEACALnddlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 812
Cdd:COG1123 107 EAlenlGLSRAEARARVLELLEA--------VGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 813 NHLLHrcILGML---SYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEILPLVQ---AVPKAWAENGQESDSATA 885
Cdd:COG1123 179 AEILD--LLRELqreRGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQalaAVPRLGAARGRAAPAAAA 256
|
...
gi 2462611208 886 QSV 888
Cdd:COG1123 257 AEP 259
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
672-863 |
1.96e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 83.60 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfgLATQEPWI-----------QF-ATIRDNILFG- 738
Cdd:COG1121 27 LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP----PRRARRRIgyvpqraevdwDFpITVRDVVLMGr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 -------KTFDAQLYKEVLEACALnddLSILPAGDQTeVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADV 811
Cdd:COG1121 103 ygrrglfRRPSRADREAVDEALER---VGLEDLADRP-IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 812 ANHLLHrcILGMLS--YTTRLLCTHRTEYLER-ADAVLLMeAGRLIRAGPPSEIL 863
Cdd:COG1121 175 EEALYE--LLRELRreGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVL 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
672-857 |
4.09e-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: 81.81 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL-----SKGFGLATQEPWIQF---ATIRDNIL------- 736
Cdd:cd03235 20 FEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekeRKRIGYVPQRRSIDRdfpISVRDVVLmglyghk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 737 -FGKTFDAQLYKEVLEAcalnddlsiLPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVD----AD 810
Cdd:cd03235 100 gLFRRLSKADKAKVDEA---------LERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDpktqED 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462611208 811 VANHLLHRCILGMlsytTRLLCTH-RTEYLERADAVLLMeAGRLIRAG 857
Cdd:cd03235 171 IYELLRELRREGM----TILVVTHdLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
672-863 |
4.95e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.42 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLA-------AIAGELhRLRGH----VAVRGLSKGFGLATQEPWIQFATIRDNILFGK- 739
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQlltrawdPQQGEI-LLNGQpiadYSEAALRQAISVVSQRVHLFSATLRDNLLLAAp 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 740 -TFDAQLyKEVLEACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhR 818
Cdd:PRK11160 440 nASDEAL-IEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIL-E 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462611208 819 CILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK11160 517 LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
672-853 |
6.60e-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: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlskgfglatQEPWIQFATIRDNILFgktfdaqlykeVLE 751
Cdd:cd03230 21 LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG---------KDIKKEPEEVKRRIGY-----------LPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 752 ACALNDDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS--YTTR 829
Cdd:cd03230 81 EPSLYENLT----------VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE--LLRELKkeGKTI 148
|
170 180
....*....|....*....|....*
gi 2462611208 830 LLCTHRTEYLER-ADAVLLMEAGRL 853
Cdd:cd03230 149 LLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
989-1272 |
7.27e-17 |
|
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: 83.03 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 989 LLLFS-PGNLYIPV-FPLPKAAPngSSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTF 1066
Cdd:cd18559 11 NHVFSgPSNLWLLLwFDDPVNGP--QEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1067 FNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYhVQRHYRASSRELRRL 1146
Cdd:cd18559 89 FERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVP-VNRVYAASSRQLKRL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1147 GSLTLSPLYSHLADTLAGLSVLRATGATYRFeEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQ 1226
Cdd:cd18559 168 ESVSKDPRYKLFNETLLGISVIKAFEWEEAF-IRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRH 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462611208 1227 QglaNPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEY 1272
Cdd:cd18559 247 S---LAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1297-1453 |
1.81e-16 |
|
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: 80.24 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRP--GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL---R 1371
Cdd:cd03257 2 LEVKNLSVSFPTggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1372 SQLAIIPQEPFL---FSGTVRENL-DPQGLHKD--------RALWQALKQCHLSEVITSMggldgelgeGGRSLSLGQRQ 1439
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGEQIaEPLRIHGKlskkearkEAVLLLLVGVGLPEEVLNR---------YPHELSGGQRQ 152
|
170
....*....|....
gi 2462611208 1440 LLCLARALLTDAKV 1453
Cdd:cd03257 153 RVAIARALALNPKL 166
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1267-1447 |
1.88e-16 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 84.41 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1267 ERLEEYTCDLPQEPQGQPLQLgtgwlTQGGVEFQDVVLAYrPGLPNA-LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLF 1345
Cdd:COG4618 306 RRLNELLAAVPAEPERMPLPR-----PKGRLSVENLTVVP-PGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLV 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1346 RLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVREN------LDPQglhkdrALWQALKQCHLSEVI--- 1416
Cdd:COG4618 380 GVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENiarfgdADPE------KVVAAAKLAGVHEMIlrl 453
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462611208 1417 -----TsmggldgELGEGGRSLSLGQRQLLCLARAL 1447
Cdd:COG4618 454 pdgydT-------RIGEGGARLSGGQRQRIGLARAL 482
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
672-862 |
3.16e-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: 82.07 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------KGFGLATQEpwiqFA-----TIRDNILFG 738
Cdd:COG3842 26 LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtglppekRNVGMVFQD----YAlfphlTVAENVAFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 ----KTFDAQLYKEVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVD 808
Cdd:COG3842 102 lrmrGVPKAEIRARVAELLEL--------------VGLEGLadryphQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 809 ADVANHL------LHRcILGmlsyTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:COG3842 168 AKLREEMreelrrLQR-ELG----ITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
671-857 |
3.35e-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: 78.25 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVavrglskgfglatqepwiqfatirdnILFGKTFDAQLYKEVL 750
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI--------------------------LLDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 751 EACAlnddlsILP-AGDQTEVG---EKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS 825
Cdd:cd03214 73 RKIA------YVPqALELLGLAhlaDRPFnELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE--LLRRLA 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462611208 826 Y---TTRLLCTHrteYLERA----DAVLLMEAGRLIRAG 857
Cdd:cd03214 145 RergKTVVMVLH---DLNLAaryaDRVILLKDGRIVAQG 180
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
618-864 |
3.61e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 84.79 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 618 SLDRIQLFLDLPNHNPQAYYS--PdPPAEPST--------VLELHGALfswDPVGTSLETFISHLEVkkgmlVGIVGKVG 687
Cdd:PLN03130 1205 AVERVGTYIDLPSEAPLVIENnrP-PPGWPSSgsikfedvVLRYRPEL---PPVLHGLSFEISPSEK-----VGIVGRTG 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 688 CGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYkEVLEACALN 756
Cdd:PLN03130 1276 AGKSSMLNALFRIVELERGRILIDGcdiskfglmdLRKVLGIIPQAPVLFSGTVRFNLdPFNEHNDADLW-ESLERAHLK 1354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 757 DDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRT 836
Cdd:PLN03130 1355 DVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR-TDALIQKTIREEFKSCTMLIIAHRL 1433
|
250 260
....*....|....*....|....*...
gi 2462611208 837 EYLERADAVLLMEAGRLIRAGPPSEILP 864
Cdd:PLN03130 1434 NTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
619-872 |
4.13e-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: 83.41 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 619 LDRIQLFLDLPNHNPQAYYSPDPPAEPSTVLELHGALFSWDPVGTslETF-----IShLEVKKGMLVGIVGKVGCGKSSL 693
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGK--GGVravddVS-LTLRRGETLGLVGESGSGKSTL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 694 LAAIAGELHRLRGHVAVRG-------------LSKGFGLATQEPWIQF---ATIRDNI-----LFGKTFDAQLYK---EV 749
Cdd:COG1123 308 ARLLLGLLRPTSGSILFDGkdltklsrrslreLRRRVQMVFQDPYSSLnprMTVGDIIaeplrLHGLLSRAERRErvaEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 750 LEACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD----ADVANHLLH-RCILGm 823
Cdd:COG1123 388 LERVGLPPDlADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDvsvqAQILNLLRDlQRELG- 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 824 LSYttrLLCTH---RTEYLerADAVLLMEAGRLIRAGPPSEIL--P-------LVQAVPKA 872
Cdd:COG1123 456 LTY---LFISHdlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFanPqhpytraLLAAVPSL 511
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
681-863 |
5.12e-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: 81.30 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 681 GIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL-----SKGFGLAT---------QEPWIqFA--TIRDNILFG-----K 739
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsARGIFLPPhrrrigyvfQEARL-FPhlSVRGNLLYGrkrapR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 740 TFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrc 819
Cdd:COG4148 108 AERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462611208 820 ILGMLSYTTR---LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG4148 175 YLERLRDELDipiLYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1297-1456 |
6.47e-16 |
|
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: 78.78 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDV--VLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 1371
Cdd:cd03258 2 IELKNVskVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1372 SQLAIIPQEPFLFSG-TVREN----LDPQGLHKDRALWQA---LKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCL 1443
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENvalpLEIAGVPKAEIEERVlelLELVGLEDKADA----------YPAQLSGGQKQRVGI 151
|
170
....*....|...
gi 2462611208 1444 ARALLTDAKVRSC 1456
Cdd:cd03258 152 ARALANNPKVLLC 164
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
557-863 |
9.35e-16 |
|
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: 83.46 E-value: 9.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 557 CVYLWAALPVVISivifityvlmGHQLTATKVFTALALVRMLILPLNnfpWVINGLLEAK---VSLDRIQLFLDLPNHNP 633
Cdd:TIGR00957 1201 CIVLFAALFAVIS----------RHSLSAGLVGLSVSYSLQVTFYLN---WLVRMSSEMEtniVAVERLKEYSETEKEAP 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 634 QAYYSPDPPAE--PSTVLELHGALFSWDPvgtSLETFISHLEV--KKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVA 709
Cdd:TIGR00957 1268 WQIQETAPPSGwpPRGRVEFRNYCLRYRE---DLDLVLRHINVtiHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 710 VRGLS-KGFGLAT---------QEPWIQFATIRDNI-LFGKTFDAQLYKeVLEACALNDDLSILPAGDQTEVGEKGVTLS 778
Cdd:TIGR00957 1345 IDGLNiAKIGLHDlrfkitiipQDPVLFSGSLRMNLdPFSQYSDEEVWW-ALELAHLKTFVSALPDKLDHECAEGGENLS 1423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 779 GGQRARIALARAVYQEKELYLLDDPLAAVDADVANhLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGP 858
Cdd:TIGR00957 1424 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDN-LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGA 1502
|
....*
gi 2462611208 859 PSEIL 863
Cdd:TIGR00957 1503 PSNLL 1507
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
672-857 |
1.32e-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: 77.30 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL--------SKGFGLATQepwiQFA-----TIRDNILFG 738
Cdd:cd03301 21 LDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkDRDIAMVFQ----NYAlyphmTVYDNIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 ----KTFDAQLYKEVLEACALnddLSIlpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH 814
Cdd:cd03301 97 lklrKVPKDEIDERVREVAEL---LQI-----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462611208 815 L------LHRcilgMLSYTTrLLCTH-RTEYLERADAVLLMEAGRLIRAG 857
Cdd:cd03301 169 MraelkrLQQ----RLGTTT-IYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1317-1453 |
1.41e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.81 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1317 VTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLePSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---D 1393
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgN 447
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 1394 PQGlhKDRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK11174 448 PDA--SDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAgLSVGQAQRLALARALLQPCQL 506
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
672-852 |
2.06e-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: 75.69 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLskgfGLATQEPWIQfaTIRDNIlfGKTF-DAQLY--KE 748
Cdd:cd03229 21 LNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE----DLTDLEDELP--PLRRRI--GMVFqDFALFphLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 749 VLEACALnddlsilpagdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL--LHRCILGMLSY 826
Cdd:cd03229 93 VLENIAL--------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVraLLKSLQAQLGI 152
|
170 180
....*....|....*....|....*..
gi 2462611208 827 TTrLLCTHRTEYLER-ADAVLLMEAGR 852
Cdd:cd03229 153 TV-VLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1257-1448 |
2.32e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.30 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1257 TQTEAML----VSVERLEEYTcDLPQEPQGQPLQLgtgwLTQGGVEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGR 1332
Cdd:PRK10790 302 TTQQSMLqqavVAGERVFELM-DGPRQQYGNDDRP----LQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1333 TGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDpqgLHKD---RALWQALKQ 1409
Cdd:PRK10790 376 TGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVT---LGRDiseEQVWQALET 452
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462611208 1410 CHLSEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARALL 1448
Cdd:PRK10790 453 VQLAELARSLPDgLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
671-863 |
2.46e-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: 77.54 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGFGLAT--------QEPwiqFA------TIRDN 734
Cdd:COG1124 25 SLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpVTRRRRKAFrrrvqmvfQDP---YAslhprhTVDRI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 735 I-----LFGKTFDAQLYKEVLEACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 808
Cdd:COG1124 102 LaeplrIHGLPDREERIAELLEQVGLPPSfLDRYPH-----------QLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 809 ADVANHLLHrcILGML---SYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG1124 171 VSVQAEILN--LLKDLreeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1298-1453 |
2.71e-15 |
|
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: 74.97 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1298 EFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAII 1377
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 1378 PQepflfsgtvrenldpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd00267 79 PQ-----------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
672-862 |
5.22e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.19 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGeLHRL-RGHVAV------------RGLSKGFglatQepwiQFA-----TIRD 733
Cdd:COG3839 24 LDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPtSGEILIggrdvtdlppkdRNIAMVF----Q----SYAlyphmTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 734 NILFG----KTFDAQLYKEVLEACALnddLSI------LPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDP 803
Cdd:COG3839 95 NIAFPlklrKVPKAEIDRRVREAAEL---LGLedlldrKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 804 LAAVDADVANHL------LHRcilgMLSYTTrLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:COG3839 161 LSNLDAKLRVEMraeikrLHR----RLGTTT-IYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1297-1453 |
6.91e-15 |
|
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: 75.20 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVdtsqlELAQLRSQL 1374
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1375 AIIPQEPFLFS-GTVREN----LDPQGLHK----DRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLAR 1445
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvalgLELQGVPKaearERAE-ELLELVGLSGFENAY----------PHQLSGGMRQRVALAR 144
|
....*...
gi 2462611208 1446 ALLTDAKV 1453
Cdd:cd03293 145 ALAVDPDV 152
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
660-863 |
7.71e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.56 E-value: 7.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 660 PVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKG-----------FGLATQEPWIQF 728
Cdd:PRK13644 12 PDGTPALENIN-LVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfsklqgirklVGIVFQNPETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 729 A--TIRDNILFGKTF----DAQLYKEVleacalndDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDD 802
Cdd:PRK13644 91 VgrTVEEDLAFGPENlclpPIEIRKRV--------DRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 803 PLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
672-862 |
9.15e-15 |
|
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: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------KGFGLATQepwiQFA-----TIRDNILFG 738
Cdd:cd03300 21 LDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpphkRPVNTVFQ----NYAlfphlTVFENIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 ----KTFDAQLYKEVLEACalndDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH 814
Cdd:cd03300 97 lrlkKLPKAEIKERVAEAL----DLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 815 L------LHRcILGMlsytTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 862
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 ... |
671-853 |
1.01e-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: 74.83 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV-----AVRGLSKG----------------FGLatqepwIQFA 729
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtDISKLSEKelaafrrrhigfvfqsFNL------LPDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 730 TIRDNILFGKTF-------DAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDD 802
Cdd:cd03255 98 TALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 803 PLAAVDADVAnhllhRCILGML------SYTTRLLCTHRTEYLERADAVLLMEAGRL 853
Cdd:cd03255 167 PTGNLDSETG-----KEVMELLrelnkeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
671-853 |
1.16e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.48 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLL-------AAIAGELhrLRGHVAVRGLSKGFGLATQE----PWiqfATIRDNI---L 736
Cdd:PRK11247 32 DLHIPAGQFVAVVGRSGCGKSTLLrllagleTPSAGEL--LAGTAPLAEAREDTRLMFQDarllPW---KKVIDNVglgL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 737 FGKTFDAQLykEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdvanhlL 816
Cdd:PRK11247 107 KGQWRDAAL--QALAAVGLADRANEWPA-----------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDA------L 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462611208 817 HRCILGMLSYT-------TRLLCTHR-TEYLERADAVLLMEAGRL 853
Cdd:PRK11247 168 TRIEMQDLIESlwqqhgfTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1297-1453 |
1.32e-14 |
|
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: 78.41 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDGVDTSQLELAQLRSQ 1373
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1374 LAIIPQEPF--LFSGTVRENLD--------PQGLHKDRALWqALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCL 1443
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAealenlglSRAEARARVLE-LLEAVGLERRLDRYPH----------QLSGGQRQRVAI 153
|
170
....*....|
gi 2462611208 1444 ARALLTDAKV 1453
Cdd:COG1123 154 AMALALDPDL 163
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
672-863 |
1.34e-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: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------KGFGLATQEpWIQFA--TIRDNILFG--- 738
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDitnlppekRDISYVPQN-YALFPhmTVYKNIAYGlkk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 -KTFDAQLYKEVLEacaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdvanhLLH 817
Cdd:cd03299 99 rKVDKKEIERKVLE---IAEMLGIDHLLNR-----KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV-----RTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 818 RCILGMLSY------TTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:cd03299 166 EKLREELKKirkefgVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1297-1453 |
1.35e-14 |
|
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: 75.22 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 1374
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1375 AIIPQEPFLfS----GTVRENLD-PQGLHK----DRALWQALKQCHLSEvitsmggldGELGEGGRSLSLGQRQLLCLAR 1445
Cdd:COG1124 82 QMVFQDPYA-SlhprHTVDRILAePLRIHGlpdrEERIAELLEQVGLPP---------SFLDRYPHQLSGGQRQRVAIAR 151
|
....*...
gi 2462611208 1446 ALLTDAKV 1453
Cdd:COG1124 152 ALILEPEL 159
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
561-849 |
1.96e-14 |
|
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: 79.18 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 561 WAALPVVISIVIF---ITYVLMG-HQLTATKVFTALALVrMLILplNNFPWVIN------GLLEakvSLDRIQLFLDLPN 630
Cdd:TIGR01271 1110 WFQMRIDIIFVFFfiaVTFIAIGtNQDGEGEVGIILTLA-MNIL--STLQWAVNssidvdGLMR---SVSRVFKFIDLPQ 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 631 HNPQAYYSPDPpAEPSTVL-----------------ELHGALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSL 693
Cdd:TIGR01271 1184 EEPRPSGGGGK-YQLSTVLvienphaqkcwpsggqmDVQGLTAKYTEAGRAVLQDLS-FSVEGGQRVGLLGRTGSGKSTL 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 694 LAAIAgELHRLRGHVAVRGLS----------KGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYKeVLEACALNDDLSIL 762
Cdd:TIGR01271 1262 LSALL-RLLSTEGEIQIDGVSwnsvtlqtwrKAFGVIPQKVFIFSGTFRKNLdPYEQWSDEEIWK-VAEEVGLKSVIEQF 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 763 PAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLERA 842
Cdd:TIGR01271 1340 PDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLEC 1418
|
....*..
gi 2462611208 843 DAVLLME 849
Cdd:TIGR01271 1419 QQFLVIE 1425
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1314-1453 |
2.21e-14 |
|
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: 73.67 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLAIIPQEPFLFSG-TVRENL 1392
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPElTVRENL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 1393 D----PQGLHKDRA-LWQALKQCHLSEVITsmggldgelgEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:COG4133 97 RfwaaLYGLRADREaIDEALEAVGLAGLAD----------LPVRQLSAGQKRRVALARLLLSPAPL 152
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
1010-1242 |
2.53e-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: 74.99 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1010 NGSSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDS 1089
Cdd:pfam00664 35 PETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1090 LPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLR 1169
Cdd:pfam00664 115 LGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 1170 ATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYA 1242
Cdd:pfam00664 195 AFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
672-854 |
2.75e-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: 73.69 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------------LSKGFGLATQEPwiqFA------TIR 732
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkiRRKEIQMVFQDP---MSslnprmTIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 733 DNI-----LFGKTFDAQLYKEV--LEACALNDDLSIL---PAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDD 802
Cdd:cd03257 103 EQIaeplrIHGKLSKKEARKEAvlLLLVGVGLPEEVLnryPH-----------ELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 803 PLAAVDADVANHLLH--RCI---LGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLI 854
Cdd:cd03257 172 PTSALDVSVQAQILDllKKLqeeLGL----TLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
672-857 |
2.89e-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: 73.84 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH---RLRGHVAVRG--LSKG-----FGLATQ-EPWIQFATIRDNILFGKT 740
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGqpRKPDqfqkcVAYVRQdDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 741 F-----DAQLYKEVLEACALNDDLSILPAGDQTEVGekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL 815
Cdd:cd03234 108 LrlprkSSDAIRKKRVEDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462611208 816 LHrcILGMLSYTTRL-LCT-H--RTEYLERADAVLLMEAGRLIRAG 857
Cdd:cd03234 183 VS--TLSQLARRNRIvILTiHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1297-1453 |
4.80e-14 |
|
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: 73.49 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1376
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1377 IPQEPFLFSG-TVREN--LDPQGLH------KDRALwQALKQCHLSEvitsmgglDGELGEGGRSLSLGQRQLLCLARAL 1447
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPKLLKwpkekiRERAD-ELLALVGLDP--------AEFADRYPHELSGGQQQRVGVARAL 150
|
....*.
gi 2462611208 1448 LTDAKV 1453
Cdd:cd03295 151 AADPPL 156
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1313-1453 |
6.25e-14 |
|
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: 72.40 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlELAQLRSQLAIIPQEPFLFSG-TVREN 1391
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 1392 LDP-QGLH--KDRALWQALkqchlsEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03266 99 LEYfAGLYglKGDELTARL------EELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
672-863 |
7.37e-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: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----LSKGFGLATQepwiqfATIRDNILFGktfdAQLY 746
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsalLELGAGFHPE------LTGRENIYLN----GRLL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 747 -------KEVLEACAlnddlsilpagDQTEVGE------KgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdvan 813
Cdd:COG1134 117 glsrkeiDEKFDEIV-----------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA---- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 814 HLLHRCILGMLSY----TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG1134 180 AFQKKCLARIRELresgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1297-1453 |
7.44e-14 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 73.15 E-value: 7.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGlpNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1376
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1377 IPQEPFL-FSGTVRE----------NLDPQGLHKDRAL-WQALKQCHLSEvitsmggldgelgEGGR---SLSLGQRQLL 1441
Cdd:COG1120 80 VPQEPPApFGLTVRElvalgryphlGLFGRPSAEDREAvEEALERTGLEH-------------LADRpvdELSGGERQRV 146
|
170
....*....|..
gi 2462611208 1442 CLARALLTDAKV 1453
Cdd:COG1120 147 LIARALAQEPPL 158
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1313-1453 |
9.55e-14 |
|
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: 72.47 E-value: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLAI-----IPQepfLFSG- 1386
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIgrtfqIPR---LFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1387 TVRENL------------------DPQGLHKDRAlWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALL 1448
Cdd:cd03219 91 TVLENVmvaaqartgsglllararREEREARERA-EELLERVGLADL----------ADRPAGELSYGQQRRLEIARALA 159
|
....*
gi 2462611208 1449 TDAKV 1453
Cdd:cd03219 160 TDPKL 164
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
672-862 |
1.13e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.35 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGfGLATQEPWIQFA----------TIRDNILFGKTF 741
Cdd:PRK10851 23 LDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-RLHARDRKVGFVfqhyalfrhmTVFDNIAFGLTV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 742 --------DAQLYKEV---LEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 810
Cdd:PRK10851 102 lprrerpnAAAIKAKVtqlLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 811 VANHL------LHRcilgMLSYTTrLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK10851 171 VRKELrrwlrqLHE----ELKFTS-VFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
612-863 |
1.16e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 612 LLEAKVSLDRIQLFLDlpnhNPQAYYSPDPPAEPSTVLELHGALFSWDPvGTSLETFIShLEVKKGMLVGIVGKVGCGKS 691
Cdd:PRK10790 308 LQQAVVAGERVFELMD----GPRQQYGNDDRPLQSGRIDIDNVSFAYRD-DNLVLQNIN-LSVPSRGFVALVGHTGSGKS 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 692 SLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSI 761
Cdd:PRK10790 382 TLASLLMGYYPLTEGEIRLDGrplsslshsvLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARS 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 762 LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRTEYLER 841
Cdd:PRK10790 462 LPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG-TEQAIQQALAAVREHTTLVVIAHRLSTIVE 540
|
250 260
....*....|....*....|..
gi 2462611208 842 ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK10790 541 ADTILVLHRGQAVEQGTHQQLL 562
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
671-863 |
1.20e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.88 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFA-TIRDNILFGK 739
Cdd:PRK09536 23 DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraASRRVASVPQDTSLSFEfDVRQVVEMGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 740 TFDAQLYKEVLEAcalnDDLSILPAGDQTEV---GEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDadvANHL 815
Cdd:PRK09536 103 TPHRSRFDTWTET----DRAAVERAMERTGVaqfADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLD---INHQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 816 LHrcilgMLSYTTRLLCTHRTEY-----LERA----DAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK09536 176 VR-----TLELVRRLVDDGKTAVaaihdLDLAarycDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1297-1453 |
1.22e-13 |
|
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: 71.67 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ 1373
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1374 LAIIPQEPFLFSG-TVREN--LDPQGLHKDRALWQ-----ALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLAR 1445
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENvaFALEVTGVPPREIRkrvpaALELVGLSHKHRALPA----------ELSGGEQQRVAIAR 149
|
....*...
gi 2462611208 1446 ALLTDAKV 1453
Cdd:cd03292 150 AIVNSPTI 157
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
663-863 |
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 2462611208 663 TSLETFISHLE--VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFAT 730
Cdd:cd03288 31 NNLKPVLKHVKayIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtLRSRLSIILQDPILFSGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 731 IRDNI-LFGKTFDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 809
Cdd:cd03288 111 IRFNLdPECKCTDDRLW-EALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 810 DVANhLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:cd03288 190 ATEN-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
672-863 |
1.67e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.06 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSllaaIAGELHR----------LRGH----VAVRGLSKGFGLATQEPWIQFATIRDNILF 737
Cdd:PRK11176 364 FKIPAGKTVALVGRSGSGKST----IANLLTRfydidegeilLDGHdlrdYTLASLRNQVALVSQNVHLFNDTIANNIAY 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 ---GKTFDAQLYKEVLEACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANH 814
Cdd:PRK11176 440 artEQYSREQIEEAARMAYAM-DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE-SER 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462611208 815 LLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK11176 518 AIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1314-1452 |
1.72e-13 |
|
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: 71.42 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlRSQLAII--PQEPFLFSG-TVRE 1390
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlTVEE 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 1391 NLDP--QGLHKDRALWQA-----LKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAK 1452
Cdd:cd03218 95 NILAvlEIRGLSKKEREEkleelLEEFHITHLRKSKAS----------SLSGGERRRVEIARALATNPK 153
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
672-862 |
1.88e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 73.72 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEP----WIQFA-----TIRDNILFGKTFD 742
Cdd:PRK11607 40 LTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPinmmFQSYAlfphmTVEQNIAFGLKQD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 743 AQLYKEVleACALNDDLSILPAgdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRC--I 820
Cdd:PRK11607 120 KLPKAEI--ASRVNEMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVvdI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462611208 821 LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK11607 196 LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
710-875 |
1.93e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.84 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 710 VRGLSKGFGLATQEPWIQFATIRDNILFGKTfDAQLyKEVLEAC---ALNDDLSILPAGDQTEVGEKGVTLSGGQRARIA 786
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATR-EDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 787 LARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCT--HRTEYLERADAVLLM----EAGRLIRA-GPP 859
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITiaHRIASIKRSDKIVVFnnpdRTGSFVQAhGTH 1447
|
170
....*....|....*.
gi 2462611208 860 SEILPLVQAVPKAWAE 875
Cdd:PTZ00265 1448 EELLSVQDGVYKKYVK 1463
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
672-863 |
1.93e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 71.32 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfgLATQEPW-------IQ----FA--TIRDNILFG 738
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD----LTALPPAerpvsmlFQennlFPhlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 -------KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD--- 808
Cdd:COG3840 96 lrpglklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpal 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 809 ----ADVANHLLHRciLGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG3840 165 rqemLDLVDELCRE--RGL----TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
672-868 |
2.88e-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: 71.16 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------------LSKGFGLATQEPwiqfA-----TIRD 733
Cdd:COG1127 26 LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyeLRRRIGMLFQGG----AlfdslTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 734 NILFG----KTFD----AQLYKEVLEACALNDDLSILPAgdqtevgEkgvtLSGGQRARIALARAVYQEKELYLLDDPLA 805
Cdd:COG1127 102 NVAFPlrehTDLSeaeiRELVLEKLELVGLPGAADKMPS-------E----LSGGMRKRVALARALALDPEILLYDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 806 AVD---ADVANHLLHRC--ILGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL----PLVQA 868
Cdd:COG1127 171 GLDpitSAVIDELIRELrdELGL----TSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLasddPWVRQ 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1304-1453 |
3.10e-13 |
|
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: 69.39 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1304 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQepfl 1383
Cdd:cd03214 5 LSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ---- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 1384 fsgtvrenldpqglhkdralwqALKQC---HLSEvitsmggldgelgEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03214 81 ----------------------ALELLglaHLAD-------------RPFNELSGGERQRVLLARALAQEPPI 118
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
642-862 |
3.20e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 642 PAEPSTVLELHGALFSWDpvGTsleTFISH--LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGL 719
Cdd:PRK09452 8 PSSLSPLVELRGISKSFD--GK---EVISNldLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 720 ATQEP----WIQFA-----TIRDNILFG----KTFDAQLYKEVLEACALN--DDLSilpagdqtevGEKGVTLSGGQRAR 784
Cdd:PRK09452 83 AENRHvntvFQSYAlfphmTVFENVAFGlrmqKTPAAEITPRVMEALRMVqlEEFA----------QRKPHQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 785 IALARAVYQEKELYLLDDPLAAVDA----DVANHL--LHRcILGMlsytTRLLCTH-RTEYLERADAVLLMEAGRLIRAG 857
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYklrkQMQNELkaLQR-KLGI----TFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
....*
gi 2462611208 858 PPSEI 862
Cdd:PRK09452 228 TPREI 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1297-1453 |
4.00e-13 |
|
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: 70.24 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLpnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRsqLAI 1376
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1377 IPQEPFLFSG-TVRENL--------DPQGLHKDRALWqALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARAL 1447
Cdd:cd03259 77 VFQDYALFPHlTVAENIafglklrgVPKAEIRARVRE-LLELVGLEGLLNRY----------PHELSGGQQQRVALARAL 145
|
....*.
gi 2462611208 1448 LTDAKV 1453
Cdd:cd03259 146 AREPSL 151
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
672-862 |
4.02e-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: 70.67 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAG----------------------ELHRLRGHVAVrgLSKGFGLatqepwIQFA 729
Cdd:cd03256 22 LSINPGEFVALIGPSGAGKSTLLRCLNGlveptsgsvlidgtdinklkgkALRQLRRQIGM--IFQQFNL------IERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 730 TIRDNILFG--------KTFDAQLYK-EVLEACALNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLL 800
Cdd:cd03256 94 SVLENVLSGrlgrrstwRSLFGLFPKeEKQRALAALERVGLLDKAYQ-----RADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 801 DDPLAAVDADVAN---HLLHRciLGMLSYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEI 862
Cdd:cd03256 169 DEPVASLDPASSRqvmDLLKR--INREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1297-1453 |
4.36e-13 |
|
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: 69.81 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPG---LPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVlldgvdtsqlelaQLRSQ 1373
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1374 LAIIPQEPFLFSGTVREN------LDPQglhkdRaLWQALKQCHL------------SEV----ITsmggldgelgeggr 1431
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENilfgkpFDEE-----R-YEKVIKACALepdleilpdgdlTEIgekgIN-------------- 127
|
170 180
....*....|....*....|..
gi 2462611208 1432 sLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03250 128 -LSGGQKQRISLARAVYSDADI 148
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
672-872 |
5.87e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.30 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV--------------RGLSKGFGLATQEPWIQF--ATIRDNI 735
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkeiKPVRKKVGVVFQFPESQLfeETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 736 LFGKTfDAQLYKEVLEACALnDDLSILpaGDQTEVGEKG-VTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH 814
Cdd:PRK13643 107 AFGPQ-NFGIPKEKAEKIAA-EKLEMV--GLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 815 LLHRCILGMLSYTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEILPLVQ-------AVPKA 872
Cdd:PRK13643 183 MMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDflkahelGVPKA 248
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1298-1453 |
7.75e-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: 69.90 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1298 EFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQL 1374
Cdd:cd03256 2 EVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1375 AIIPQEPFLFSG-TVREN------------------LDPQglHKDRALwQALKQCHLSEVITSMGGLdgelgeggrsLSL 1435
Cdd:cd03256 81 GMIFQQFNLIERlSVLENvlsgrlgrrstwrslfglFPKE--EKQRAL-AALERVGLLDKAYQRADQ----------LSG 147
|
170
....*....|....*...
gi 2462611208 1436 GQRQLLCLARALLTDAKV 1453
Cdd:cd03256 148 GQQQRVAIARALMQQPKL 165
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
677-853 |
7.88e-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: 70.65 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 677 GMLVGIVGKVGCGKSSLLAAIAgELHRLRGHVAVRGLS----------KGFGLATQEPWIQFATIRDNI-LFGKTFDAQL 745
Cdd:cd03289 30 GQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSwnsvplqkwrKAFGVIPQKVFIFSGTFRKNLdPYGKWSDEEI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 746 YKeVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLS 825
Cdd:cd03289 109 WK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFA 186
|
170 180
....*....|....*....|....*...
gi 2462611208 826 YTTRLLCTHRTEYLERADAVLLMEAGRL 853
Cdd:cd03289 187 DCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
672-857 |
9.55e-13 |
|
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: 69.06 E-value: 9.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPwiQFATIRDNILFgktfdAQLYKEVLE 751
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENNLF-----AHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 752 ACALNDDLSiLPAGDQTEV----GEKGV---------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhR 818
Cdd:cd03298 92 GLGLSPGLK-LTAEDRQAIevalARVGLaglekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML-D 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462611208 819 CILGMLSYT--TRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 857
Cdd:cd03298 170 LVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
671-810 |
9.82e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.05 E-value: 9.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELH---RLRGHVAVRG--------LSKGFGLATQEPWIqFA--TIRDNILF 737
Cdd:COG4136 21 SLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGrrltalpaEQRRIGILFQDDLL-FPhlSVGENLAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 G--KTFDAQLYKEVLEAcALnddlsilpagdqTEVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 809
Cdd:COG4136 100 AlpPTIGRAQRRARVEQ-AL------------EEAGLAGFadrdpaTLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
.
gi 2462611208 810 D 810
Cdd:COG4136 167 A 167
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
672-857 |
1.09e-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: 69.10 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------LSKGFGLAtqepwiqfATIRDNILFG------ 738
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvssllgLGGGFNPE--------LTGRENIYLNgrllgl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 -KTFDAQLYKEVLEACALNDDLSiLPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdvanHLLH 817
Cdd:cd03220 115 sRKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDA----AFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462611208 818 RC---ILGMLS-YTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 857
Cdd:cd03220 180 KCqrrLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
672-847 |
1.91e-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: 67.89 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPWIQFA----------TIRDNILF---- 737
Cdd:COG4133 23 FTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLghadglkpelTVRENLRFwaal 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 -GKTFDAQLYKEVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLL 816
Cdd:COG4133 103 yGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-GVALL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462611208 817 HRCIL------GMLsyttrLLCTHRTEYLERADAVLL 847
Cdd:COG4133 171 AELIAahlargGAV-----LLTTHQPLELAAARVLDL 202
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
671-863 |
3.22e-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: 67.99 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAG--------------ELHRLRGHvAVRGLSKGFGLATQepwiQF-----ATI 731
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCINGlerptsgsvlvdgtDLTLLSGK-ELRKARRRIGMIFQ----HFnllssRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 732 RDNILF-------GKTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPL 804
Cdd:cd03258 100 FENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 805 AAVDADVAnhllhRCILGMLSYTTR------LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:cd03258 169 SALDPETT-----QSILALLRDINRelgltiVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1297-1453 |
3.41e-12 |
|
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: 67.17 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQL 1374
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1375 AIIPQEPFLFSG-TVREN--LDP---QGLHKD----RALwQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLLCLA 1444
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENitLAPikvKGMSKAeaeeRAL-ELLEKVGLADKADAYP----------AQLSGGQQQRVAIA 147
|
....*....
gi 2462611208 1445 RALLTDAKV 1453
Cdd:cd03262 148 RALAMNPKV 156
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
672-863 |
4.44e-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: 67.80 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH-----------RLRGHVAVRGLSKGFGLAT---QEPWIQFATIRDNILF 737
Cdd:COG1119 24 WTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygndvrlfgERRGGEDVWELRKRIGLVSpalQLRFPRDETVLDVVLS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 GKtFDA-QLYKEVLE-----ACALNDDLSILPAGDQTeVGekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDaDV 811
Cdd:COG1119 104 GF-FDSiGLYREPTDeqrerARELLELLGLAHLADRP-FG----TLSQGEQRRVLIARALVKDPELLILDEPTAGLD-LG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 812 ANHLLHRCI--LGMLSYTTRLLCTHRTEYLERA-DAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG1119 177 ARELLLALLdkLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1297-1453 |
4.89e-12 |
|
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: 67.53 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ 1373
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1374 LAIIPQEPFLFSG-TVRENL---------DPQGLHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCL 1443
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVafplrehtrLSEEEIREIVL-EKLEAVGLRGAEDLY----------PAELSGGMKKRVAL 147
|
170
....*....|
gi 2462611208 1444 ARALLTDAKV 1453
Cdd:cd03261 148 ARALALDPEL 157
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1297-1391 |
6.37e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.57 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 1371
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAAR 81
|
90 100
....*....|....*....|.
gi 2462611208 1372 SQLAIIPQEPFLFSG-TVREN 1391
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAEN 102
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1297-1381 |
7.90e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.32 E-value: 7.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1376
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
....*
gi 2462611208 1377 IPQEP 1381
Cdd:PRK13632 88 IFQNP 92
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1313-1453 |
8.17e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.74 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL 1392
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 1393 -----DPQGLHKDRALWQA--------LKQCHLSEVitsmggldgelgeGGRS--LSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK10789 410 algrpDATQQEIEHVARLAsvhddilrLPQGYDTEV-------------GERGvmLSGGQKQRISIARALLLNAEI 472
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
648-863 |
9.41e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 9.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 648 VLELHGALFSWDPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGF 717
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 718 GLATQEPWIQF--ATIRDNILFGKTFDAQLYKEVLEACalndDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEK 795
Cdd:PRK13642 84 GMVFQNPDNQFvgATVEDDVAFGMENQGIPREEMIKRV----DEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 796 ELYLLDDPLAAVDADVANHLLhRCILGMLS--YTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIM-RVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1298-1453 |
9.94e-12 |
|
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: 66.30 E-value: 9.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1298 EFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAI 1376
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1377 IPQEPFLFSG-TVRENLD--PQGLHKDRALWQ---------ALKQchlsevitsmggldgELGEGGRSLSLGQRQLLCLA 1444
Cdd:cd03224 80 VPEGRRIFPElTVEENLLlgAYARRRAKRKARlervyelfpRLKE---------------RRKQLAGTLSGGEQQMLAIA 144
|
....*....
gi 2462611208 1445 RALLTDAKV 1453
Cdd:cd03224 145 RALMSRPKL 153
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
672-855 |
1.23e-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: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSK-----------GFGLatqepwIQFAT 730
Cdd:COG1136 29 LSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslsereLARlrrrhigfvfqFFNL------LPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 731 IRDNILF-------GKTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDP 803
Cdd:COG1136 103 ALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 804 LAAVDADVANH---LLHRCI--LGmlsyTTRLLCTHRTEYLERADAVLLMEAGRLIR 855
Cdd:COG1136 172 TGNLDSKTGEEvleLLRELNreLG----TTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
672-863 |
1.68e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.88 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAI-------AGEL-----HRLRGHVAVRGLSKGFGLATQepwiQF-----ATIRDN 734
Cdd:PRK09493 22 LNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLivdglKVNDPKVDERLIRQEAGMVFQ----QFylfphLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 735 ILFG-------KTFDA-QLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAA 806
Cdd:PRK09493 98 VMFGplrvrgaSKEEAeKQARELLAKVGLAERAHHYPS-----------ELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 807 VDADvanhLLHRCILGMLSYT----TRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK09493 167 LDPE----LRHEVLKVMQDLAeegmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
672-861 |
1.79e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.46 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----LSKG--------FGLATQEpwiqFA-----TIRD 733
Cdd:COG2884 23 LEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrLKRReipylrrrIGVVFQD----FRllpdrTVYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 734 NILF-----GKTfDAQLYKEVLEACALnddlsilpagdqteVG--EKG----VTLSGGQRARIALARAVYQEKELYLLDD 802
Cdd:COG2884 99 NVALplrvtGKS-RKEIRRRVREVLDL--------------VGlsDKAkalpHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 803 PLAAVDADVAN---HLLHR-CILGmlsyTTRLLCTHRTEYLERADA-VLLMEAGRLIRAGPPSE 861
Cdd:COG2884 164 PTGNLDPETSWeimELLEEiNRRG----TTVLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
672-815 |
2.05e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVR-GLSKGFgLAtQEPwiQF---ATIRDNILFGKTFDAQLYK 747
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGY-LP-QEP--PLdddLTVLDTVLDGDAELRALEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 748 EVLEACALNDDLSILP---AGDQTEVGEKGV--------------------------TLSGGQRARIALARAVYQEKELY 798
Cdd:COG0488 95 ELEELEAKLAEPDEDLerlAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEPDLL 174
|
170
....*....|....*..
gi 2462611208 799 LLDDPlaavdadvANHL 815
Cdd:COG0488 175 LLDEP--------TNHL 183
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1313-1453 |
2.06e-11 |
|
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: 64.13 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLE--LAQLRSQLAIIPQEPFLFSG-TVR 1389
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 1390 ENLdpqglhkdrALwqalkqchlsevitsmggldgelgeggrSLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03229 95 ENI---------AL----------------------------GLSGGQQQRVALARALAMDPDV 121
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
672-863 |
2.56e-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: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL--------------SKGFGLATQepwiQFA-----TIR 732
Cdd:cd03294 45 LDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelrelrRKKISMVFQ----SFAllphrTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 733 DNILFG-------KTFDAQLYKEVLEACALNDDLSILPagDQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLA 805
Cdd:cd03294 121 ENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYP--DE---------LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 806 AVD----ADVANHLLHrcILGMLSYTTrLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:cd03294 190 ALDplirREMQDELLR--LQAELQKTI-VFITHDlDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
666-862 |
3.11e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.98 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 666 ETFIS---HLEVKKGMLVGIVGKVGCGKSSLLAAIAG-------ELhrLRGHVAVRGL---SKGFGLATQE----PWIQF 728
Cdd:PRK11000 15 DVVISkdiNLDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgDL--FIGEKRMNDVppaERGVGMVFQSyalyPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 729 AtirDNILFG----KTFDAQLYKEVLEACAlnddlsILPAGDQTEVGEKgvTLSGGQRARIALARAVYQEKELYLLDDPL 804
Cdd:PRK11000 93 A---ENMSFGlklaGAKKEEINQRVNQVAE------VLQLAHLLDRKPK--ALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 805 AAVDADVANHL------LHRcilgmlsyttRLLC-----TH-RTEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK11000 162 SNLDAALRVQMrieisrLHK----------RLGRtmiyvTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1313-1453 |
3.21e-11 |
|
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: 66.23 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP---SSGRVLLDGVDTSQL---ELAQLR-SQLAIIPQEPF--- 1382
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLsekELRKIRgREIQMIFQDPMtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1383 --LFsgTVRENL-DPQGLH--------KDRALwQALKQCHLSEVITSMggldgelgeggRS----LSLGQRQLLCLARAL 1447
Cdd:COG0444 100 npVM--TVGDQIaEPLRIHgglskaeaRERAI-ELLERVGLPDPERRL-----------DRypheLSGGMRQRVMIARAL 165
|
....*.
gi 2462611208 1448 LTDAKV 1453
Cdd:COG0444 166 ALEPKL 171
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1297-1391 |
3.27e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 66.75 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLP--NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 1371
Cdd:PRK11153 2 IELKNISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100
....*....|....*....|..
gi 2462611208 1372 SQLAIIPQEpF--LFSGTVREN 1391
Cdd:PRK11153 82 RQIGMIFQH-FnlLSSRTVFDN 102
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
672-862 |
3.40e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.84 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG------------LSKGFGLATQEPWIQF--ATIRDNILF 737
Cdd:PRK13637 28 IEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdIRKKVGLVFQYPEYQLfeETIEKDIAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 GKT----FDAQLYKEVLEACALnddlsilpAG-DQTEVGEKG-VTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA-- 809
Cdd:PRK13637 108 GPInlglSEEEIENRVKRAMNI--------VGlDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkg 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 810 --DVANHL--LHRcilgmlSYT-TRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK13637 180 rdEILNKIkeLHK------EYNmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
662-862 |
3.48e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.01 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 662 GTSLETF----IShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--------------LSKGFGLATQE 723
Cdd:PRK13641 15 GTPMEKKgldnIS-FELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkkLRKKVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 724 PWIQF--ATIRDNILFG-KTFDAQlykevlEACALNDDLS-ILPAGDQTEVGEKG-VTLSGGQRARIALARAVYQEKELY 798
Cdd:PRK13641 94 PEAQLfeNTVLKDVEFGpKNFGFS------EDEAKEKALKwLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 799 LLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1306-1447 |
4.01e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1306 YRPGLPNALDGVTFCVQPGE-KLgIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLF 1384
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEfKL-ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 1385 SGTVRENL-----------DPQGLHKDRALWqALKQCHLSEVITsmggldgelgeggrSLSLGQRQLLCLARAL 1447
Cdd:PRK10247 94 GDTVYDNLifpwqirnqqpDPAIFLDDLERF-ALPDTILTKNIA--------------ELSGGEKQRISLIRNL 152
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1298-1453 |
4.25e-11 |
|
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: 64.09 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1298 EFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqLELAQLRSQLAII 1377
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1378 PQE---PFLFSGTVRE----NLDPQG--------LHKDRALwQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLC 1442
Cdd:cd03235 74 PQRrsiDRDFPISVRDvvlmGLYGHKglfrrlskADKAKVD-EALERVGLSELADR----------QIGELSGGQQQRVL 142
|
170
....*....|.
gi 2462611208 1443 LARALLTDAKV 1453
Cdd:cd03235 143 LARALVQDPDL 153
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
672-863 |
4.40e-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: 64.38 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----------LSKGFGLATQEPWIqFA--TIRDNILFG 738
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglppherARAGIGYVPEGRRI-FPelTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 ktfdAQLYKEVLEACALNDDLSILPAGDQTEvGEKGVTLSGGQRARIALARAVYQEKELYLLDDP---LA-AVDADVANH 814
Cdd:cd03224 100 ----AYARRRAKRKARLERVYELFPRLKERR-KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLApKIVEEIFEA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462611208 815 LLHRCILGMlsytTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:cd03224 175 IRELRDEGV----TILLVEQNaRFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
672-848 |
6.17e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.02 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlSKGFGLATQ---EPWIQFATIRDNILFGK--------- 739
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-GARVAYVPQrseVPDSLPLTVRDLVAMGRwarrglwrr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 740 --TFDAQLYKEVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA----DVAN 813
Cdd:NF040873 92 ltRDDRAAVDDALERVGL-ADLAGRQLG----------ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAesreRIIA 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2462611208 814 HLLHRCILGmlsyTTRLLCTHRTEYLERADAVLLM 848
Cdd:NF040873 161 LLAEEHARG----ATVVVVTHDLELVRRADPCVLL 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
672-863 |
9.22e-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: 9.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV----------------RGLSKGF-GLATQE-PWIQFATIRD 733
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgRGRAKRYiGILHQEyDLYPHRTVLD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 734 NILfgKTFDAQLYKE--------VLEACALNDD--LSILPAGDQTevgekgvtLSGGQRARIALARAVYQEKELYLLDDP 803
Cdd:TIGR03269 385 NLT--EAIGLELPDElarmkaviTLKMVGFDEEkaEEILDKYPDE--------LSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 804 LAAVD----ADVANHLLH-RCILGmlsyTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:TIGR03269 455 TGTMDpitkVDVTHSILKaREEME----QTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1314-1447 |
1.25e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.64 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFL-FSGTVRE-- 1390
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEvv 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 1391 --NLDPQGLHK---DRALWQALKQC---HLSEvitsmggldgelgEGGRSLSLGQRQLLCLARAL 1447
Cdd:PRK13548 98 amGRAPHGLSRaedDALVAAALAQVdlaHLAG-------------RDYPQLSGGEQQRVQLARVL 149
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
672-809 |
1.32e-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: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRG-----HVAVRGLSKGFGLATQE----PWIqfaTIRDNILFGKTFD 742
Cdd:COG4525 28 LTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGeitldGVPVTGPGADRGVVFQKdallPWL---NVLDNVAFGLRLR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 743 ----AQLYKEVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 809
Cdd:COG4525 105 gvpkAERRARAEELLAL--------------VGLADFarrriwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
672-861 |
1.75e-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: 62.84 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAG--------------ELHRL--RGHVAVRGLSKGFGLatQ-EPWIQFATIRDN 734
Cdd:COG4181 33 LEVEAGESVAIVGASGSGKSTLLGLLAGldrptsgtvrlagqDLFALdeDARARLRARHVGFVF--QsFQLLPTLTALEN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 735 I-----LFGKTFDAQLYKEVLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 809
Cdd:COG4181 111 VmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTGNLDA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 810 DVANHllhrcILGML------SYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSE 861
Cdd:COG4181 180 ATGEQ-----IIDLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
672-862 |
1.85e-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: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSS-------LLAAIAGELHrLRGHVAVR---GLSKGFGLATQEPWIQFA-TIRDNI-LFGK 739
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTtikmlttLLKPTSGRAT-VAGHDVVReprEVRRRIGIVFQDLSVDDElTGWENLyIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 740 TFD------AQLYKEVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 812
Cdd:cd03265 100 LYGvpgaerRERIDELLDFVGL------------LEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 813 NHLLhRCILGMLSY--TTRLLCTHrteYLERADA----VLLMEAGRLIRAGPPSEI 862
Cdd:cd03265 168 AHVW-EYIEKLKEEfgMTILLTTH---YMEEAEQlcdrVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
672-863 |
2.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.09 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFG- 738
Cdd:PRK13632 30 FEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkeIRKKIGIIFQNPDNQFigATVEDDIAFGl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 --KTFDAQLYKEVLeacalnDDLSilpagdqTEVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 810
Cdd:PRK13632 110 enKKVPPKKMKDII------DDLA-------KKVGMEDYldkepqNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 811 vANHLLHRCILGMLSYTTRLL--CTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK13632 177 -GKREIKKIMVDLRKTRKKTLisITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
672-871 |
3.70e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.41 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS-----------KGFGLATQEPWIQF-ATI-RDNILFG 738
Cdd:PRK13633 31 LEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdirNKAGMVFQNPDNQIvATIvEEDVAFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 KtfdaqlykevleacalnDDLSILPAGDQTEVGE--KGVT-----------LSGGQRARIALARAVYQEKELYLLDDPLA 805
Cdd:PRK13633 111 P-----------------ENLGIPPEEIRERVDEslKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 806 AVDA----DVANHLLHrciLGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPK 871
Cdd:PRK13633 174 MLDPsgrrEVVNTIKE---LNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVEMMKK 240
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
672-863 |
3.78e-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: 61.93 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIagelHRL----RGHVAVRG----------LSKGFGLATQE----PWIqfaTIRD 733
Cdd:cd03295 22 LEIAKGEFLVLIGPSGSGKTTTMKMI----NRLieptSGEIFIDGedireqdpveLRRKIGYVIQQiglfPHM---TVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 734 NI-----LFGKTfDAQLYKEVLEACALNDdlsiLPagDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 808
Cdd:cd03295 95 NIalvpkLLKWP-KEKIRERADELLALVG----LD--PAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 809 ADVANHL------LHRcilgmLSYTTRLLCTHRT-EYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:cd03295 168 PITRDQLqeefkrLQQ-----ELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
675-862 |
4.40e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.95 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 675 KKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--------------------------LSKGFGLATQEPWIQF 728
Cdd:PRK13631 50 EKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitnpyskkiknfkeLRRRVSMVFQFPEYQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 729 --ATIRDNILFG-------KTFDAQLYKEVLEACALNDD-LSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKELY 798
Cdd:PRK13631 130 fkDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 799 LLDDPLAAVDADvANHLLHRCIL-GMLSYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK13631 199 IFDEPTAGLDPK-GEHEMMQLILdAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
671-863 |
4.82e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.52 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV------------AVRGLSKGFglatQEPWIqFA--TIRDNIL 736
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhtttppSRRPVSMLF----QENNL-FShlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 737 FG-----KTFDAQlyKEVLEACA----LNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAV 807
Cdd:PRK10771 94 LGlnpglKLNAAQ--REKLHAIArqmgIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 808 DADVANHllhrcILGMLS------YTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK10771 161 DPALRQE-----MLTLVSqvcqerQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
671-862 |
5.09e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.34 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV--------------RGLSKGFGLATQEPWIQF--ATIRDN 734
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkknkklKPLRKKVGIVFQFPEHQLfeETVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 735 ILFG-KTF-----DA-QLYKEVLEACALNDDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAV 807
Cdd:PRK13634 107 ICFGpMNFgvseeDAkQKAREMIELVGLPEELLARSPFE----------LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 808 DADVANHL------LHRcILGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK13634 177 DPKGRKEMmemfykLHK-EKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
672-854 |
5.22e-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: 59.75 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlskgfglatqEPwIQFATIRDnilfgktfdAQlykevle 751
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG----------KE-VSFASPRD---------AR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 752 acalnddlsilpagdqtevgEKGVT----LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGML--S 825
Cdd:cd03216 74 --------------------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLraQ 131
|
170 180 190
....*....|....*....|....*....|
gi 2462611208 826 YTTRLLCTHR-TEYLERADAVLLMEAGRLI 854
Cdd:cd03216 132 GVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1297-1453 |
5.85e-10 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 61.26 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRpGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDtsqleLAQLRSQLAI 1376
Cdd:COG1121 7 IELENLTVSYG-GRP-VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1377 IPQEPFL---FSGTVRE----NLDPQ-GL-----HKDRAL-WQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLLC 1442
Cdd:COG1121 80 VPQRAEVdwdFPITVRDvvlmGRYGRrGLfrrpsRADREAvDEALERVGLEDLADRPI----------GELSGGQQQRVL 149
|
170
....*....|.
gi 2462611208 1443 LARALLTDAKV 1453
Cdd:COG1121 150 LARALAQDPDL 160
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
662-871 |
6.06e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.07 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 662 GTSLET---FISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV--------------RGLSKGFGLATQEP 724
Cdd:PRK13649 15 GTPFEGralFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVddtlitstsknkdiKQIRKKVGLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 725 WIQ-FA-TIRDNILFG-KTFDAQlyKEVLEACALNddlSILPAGDQTEVGEKG-VTLSGGQRARIALARAVYQEKELYLL 800
Cdd:PRK13649 95 ESQlFEeTVLKDVAFGpQNFGVS--QEEAEALARE---KLALVGISESLFEKNpFELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 801 DDPLAAVDADVANHL------LHRciLGMlsytTRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEILPLVQ------ 867
Cdd:PRK13649 170 DEPTAGLDPKGRKELmtlfkkLHQ--SGM----TIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIFQDVDfleekq 243
|
....*
gi 2462611208 868 -AVPK 871
Cdd:PRK13649 244 lGVPK 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1313-1447 |
6.61e-10 |
|
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: 63.55 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSlLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQLAIIPQEPFlfsG--- 1386
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKST-LGLALLRLIPSEGEIRFDGQDLDGLsrrALRPLRRRMQVVFQDPF---Gsls 376
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 1387 -------TVRENLDPQGLHKDRA-----LWQALKQCHLSEvitsmggldgelGEGGR---SLSLGQRQLLCLARAL 1447
Cdd:COG4172 377 prmtvgqIIAEGLRVHGPGLSAAerrarVAEALEEVGLDP------------AARHRyphEFSGGQRQRIAIARAL 440
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
671-851 |
7.36e-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: 7.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGelhrL----RGHVAVRGLSKGFGLAtQEPWIQFATIRDNILF---GKTFDA 743
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARPAGARVLFLP-QRPYLPLGTLREALLYpatAEAFSD 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 744 QLYKEVLEACALnDDLsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGM 823
Cdd:COG4178 458 AELREALEAVGL-GHL----AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREE 531
|
170 180
....*....|....*....|....*...
gi 2462611208 824 LSYTTRLLCTHRTEYLERADAVLLMEAG 851
Cdd:COG4178 532 LPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
672-862 |
7.69e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.43 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGfglATQEPWI-----QFA-----TIRDNILFG- 738
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedVTHR---SIQQRDIcmvfqSYAlfphmSLGENVGYGl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 ---KTFDAQLYKEVLEACALNDdlsilPAG------DQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 809
Cdd:PRK11432 104 kmlGVPKEERKQRVKEALELVD-----LAGfedryvDQ---------ISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 810 DvanhlLHRCI------LGMLSYTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK11432 170 N-----LRRSMrekireLQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
672-853 |
1.02e-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: 60.24 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGeLHRL-RGHVAVRGLS------------KGFGLATQepwiQFA-----TIRD 733
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINL-LEEPdSGTIIIDGLKltddkkninelrQKVGMVFQ----QFNlfphlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 734 NILFGKTF-------DAQ-LYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLA 805
Cdd:cd03262 96 NITLAPIKvkgmskaEAEeRALELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 806 AVDA-------DVANHLLHRcilGMlsytTRLLCTHRTEY-LERADAVLLMEAGRL 853
Cdd:cd03262 165 ALDPelvgevlDVMKDLAEE---GM----TMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
671-808 |
1.08e-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: 60.25 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS-----------KGFGLATQEPWIqFA--TIRDNIL- 736
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarLGIGYLPQEASI-FRklTVEENILa 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 737 ----FGKTFDAQlyKEVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 808
Cdd:cd03218 99 vleiRGLSKKER--EEKLEE--LLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
672-863 |
1.12e-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: 60.53 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH------RLRGH---------VAVRGLSKGFglatQEPWIqFA--TIRDN 734
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsvLFDGEditglppheIARLGIGRTF----QIPRL-FPelTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 735 ILFGKTFDAQLY-----------------KEVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKEL 797
Cdd:cd03219 96 VMVAAQARTGSGlllararreereareraEELLERVGL-ADLADRPAG----------ELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 798 YLLDDPLAAVDADVANHLLHRcILGM-LSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAEL-IRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1312-1453 |
1.13e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 60.14 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1312 NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ-LAIIPQ-EPFLFSG 1386
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRARhVGFVFQsFQLLPTL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 1387 TVREN------LDPQGLHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:COG4181 106 TALENvmlpleLAGRRDARARAR-ALLERVGLGHRLDHY----------PAQLSGGEQQRVALARAFATEPAI 167
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1306-1388 |
1.30e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.22 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1306 YRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTS--QLELAQLRSQLAIIPQE 1380
Cdd:PRK13637 12 YMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90
....*....|
gi 2462611208 1381 P--FLFSGTV 1388
Cdd:PRK13637 92 PeyQLFEETI 101
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1265-1449 |
1.61e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.52 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1265 SVERLEEYTCDLpQEPQGQPLQLGTGWLTQGG-VEFQDVVLAyrpgLPNA---LDGVTFCVQPGEKLGIVGRTGSGKSSl 1340
Cdd:COG4178 331 TVDRLAGFEEAL-EAADALPEAASRIETSEDGaLALEDLTLR----TPDGrplLEDLSLSLKPGERLLITGPSGSGKST- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1341 llvlfrllepssgrvLLDGvdtsqleLAQL------------RSQLAIIPQEPFLFSGTVRENL---DPQGLHKDRALWQ 1405
Cdd:COG4178 405 ---------------LLRA-------IAGLwpygsgriarpaGARVLFLPQRPYLPLGTLREALlypATAEAFSDAELRE 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462611208 1406 ALKQCHLSEVITSMggldGELGEGGRSLSLGQRQLLCLARALLT 1449
Cdd:COG4178 463 ALEAVGLGHLAERL----DEEADWDQVLSLGEQQRLAFARLLLH 502
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1313-1453 |
1.72e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.96 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAIIPQEPFLFSG-TVRE 1390
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1391 NL------------DPQGLHKdRALwQALKQCHLS-----EVitsmggldgelgeggRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:COG1129 99 NIflgreprrggliDWRAMRR-RAR-ELLARLGLDidpdtPV---------------GDLSVAQQQLVEIARALSRDARV 161
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
672-871 |
1.72e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.79 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV---------------AVRGLSKGFGLATQEPWIQF--ATIRDN 734
Cdd:PRK13645 32 LTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyaipanlkkikEVKRLRKEIGLVFQFPEYQLfqETIEKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 735 ILFGKTF----DAQLYKEVLEACalndDLSILPagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 810
Cdd:PRK13645 112 IAFGPVNlgenKQEAYKKVPELL----KLVQLP---EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 811 VANHLLHRCILGMLSYTTR-LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEILPLVQAVPK 871
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRiIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFSNQELLTK 247
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
671-863 |
1.85e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.17 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFA-TIRDNILFG- 738
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaeLARRRAVLPQHSSLSFPfTVEEVVAMGr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 ------KTFDAQLYKEVLEACALnDDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQ------EKELYLLDDPLAA 806
Cdd:PRK13548 102 aphglsRAEDDALVAAALAQVDL-AHLA----------GRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 807 VD-------ADVANHLLHR------CILGMLSYTTRllcthrteYlerADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK13548 171 LDlahqhhvLRLARQLAHErglaviVVLHDLNLAAR--------Y---ADRIVLLHQGRLVADGTPAEVL 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1308-1453 |
2.16e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1308 PGLpNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTS-QLELAQLRSQLAIIPQE----PF 1382
Cdd:PRK11288 15 PGV-KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQElhlvPE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 1383 LfsgTVRENLD----PQ--GLHKDRAL-WQALKQC-HLSEVITSmggldgelGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK11288 94 M---TVAENLYlgqlPHkgGIVNRRLLnYEAREQLeHLGVDIDP--------DTPLKYLSIGQRQMVEIAKALARNARV 161
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
672-862 |
2.38e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.01 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAG-------ELH---RLRGHV--AVRGLSKGFglatqepwiQ-FA-----TIRD 733
Cdd:PRK11650 25 LDVADGEFIVLVGPSGCGKSTLLRMVAGleritsgEIWiggRVVNELepADRDIAMVF---------QnYAlyphmSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 734 NILFG----KTFDAQLYKEVLEACALnddLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 809
Cdd:PRK11650 96 NMAYGlkirGMPKAEIEERVAEAARI---LELEPLLDR-----KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 810 DVANHL------LHRCiLGmlsyTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK11650 168 KLRVQMrleiqrLHRR-LK----TTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
672-863 |
2.58e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 59.74 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfgLATQEPW--------------IQFA-TIRDNIL 736
Cdd:COG4559 22 LTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRP----LAAWSPWelarrravlpqhssLAFPfTVEEVVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 737 FG-------KTFDAQLYKEVLEACalndDLSILPAGDQTevgekgvTLSGGQRARIALARA-------VYQEKELYLLDD 802
Cdd:COG4559 98 LGraphgssAAQDRQIVREALALV----GLAHLAGRSYQ-------TLSGGEQQRVQLARVlaqlwepVDGGPRWLFLDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 803 PLAAVD-------ADVANHLLHR-----CILGMLSYTTRllcthrteYlerADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG4559 167 PTSALDlahqhavLRLARQLARRgggvvAVLHDLNLAAQ--------Y---ADRILLLHQGRLVAQGTPEEVL 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
364-801 |
2.77e-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: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 364 LEEGQEPLSHGLLYALGLAGGAVLGAVL-QNQYGYEVYKVTLQARGAVLN-ILYC---KALQLGPSRpptgeALNLLGTD 438
Cdd:COG4615 40 LNATGAALARLLLLFAGLLVLLLLSRLAsQLLLTRLGQHAVARLRLRLSRrILAApleRLERIGAAR-----LLAALTED 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 439 SERLLNFAGSFHE-AWGLPLQLAITLYLLYQQVgVAFVGGLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELL 517
Cdd:COG4615 115 VRTISQAFVRLPElLQSVALVLGCLAYLAWLSP-PLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 518 SGIRVIK---------FcgwEQALGARVEACRARelgRLRVIKYLDAACVYLWAALPVVISIVIFityVLMGHQLTATKV 588
Cdd:COG4615 194 EGFKELKlnrrrrrafF---DEDLQPTAERYRDL---RIRADTIFALANNWGNLLFFALIGLILF---LLPALGWADPAV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 589 FTALALVRM-LILPLNNFPWVINGLLEAKVSLDRI-QLFLDLPNHNPQAYYSPDPPAEPS-TVLELHGALFSWDPVGTSl 665
Cdd:COG4615 265 LSGFVLVLLfLRGPLSQLVGALPTLSRANVALRKIeELELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGD- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 666 ETF----IShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlsKGFGLATQEPWIQ-FATI-RDNILF-- 737
Cdd:COG4615 344 EGFtlgpID-LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG--QPVTADNREAYRQlFSAVfSDFHLFdr 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 738 ----GKTFDAQLYKEVLEACALNDDLSIlpagdqtevgEKG----VTLSGGQRARIALARAVYQEKELYLLD 801
Cdd:COG4615 421 llglDGEADPARARELLERLELDHKVSV----------EDGrfstTDLSQGQRKRLALLVALLEDRPILVFD 482
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1314-1453 |
3.01e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.01 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFL-FSGTVRE-- 1390
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQvv 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 1391 ---------NLDPQGLHKDRALWQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK09536 99 emgrtphrsRFDTWTETDRAAVERAMERTGVAQFADR----------PVTSLSGGERQRVLLARALAQATPV 160
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
672-868 |
3.21e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.64 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS----------KGFGLATQEPWIQF--ATIRDNILFGk 739
Cdd:PRK13635 28 FSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrRQVGMVFQNPDNQFvgATVQDDVAFG- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 740 tfdaqlykevLEACALNDDLSIlPAGDQ--TEVG------EKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA-- 809
Cdd:PRK13635 107 ----------LENIGVPREEMV-ERVDQalRQVGmedflnREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrg 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 810 -----DVANHLLHRCILGMLSyttrllCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQA 868
Cdd:PRK13635 176 rrevlETVRQLKEQKGITVLS------ITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
671-865 |
4.03e-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: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGelHR----LRGHVAVRGLS-----------KGFGLATQEPwIQFATIRDni 735
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPkyevTEGEILFKGEDitdlppeerarLGIFLAFQYP-PEIPGVKN-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 736 lfgktfdAQLYKEVleacalnddlsilpagdqtevgekGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHL 815
Cdd:cd03217 95 -------ADFLRYV------------------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID-ALRL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 816 LHRCILGMLSYTTR-LLCTHRTEYLE--RADAVLLMEAGRLIRAGPPSEILPL 865
Cdd:cd03217 143 VAEVINKLREEGKSvLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKELALEI 195
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
662-857 |
4.28e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.87 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 662 GTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAI-------AGELHrLRGHV----------AVRGLSKGFGLATQE- 723
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLN-IAGNHfdfsktpsdkAIRELRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 724 -PWIQFaTIRDNIL--------FGKTFDAQLYKEVLEACALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQE 794
Cdd:PRK11124 92 nLWPHL-TVQQNLIeapcrvlgLSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 795 KELYLLDDPLAAVDADVANHLLHrcILGMLSYT--TRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 857
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVS--IIRELAETgiTQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1297-1392 |
5.23e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.23 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL-ELAQLRSQLA 1375
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVG 80
|
90
....*....|....*....
gi 2462611208 1376 IIPQEP-FLFSG-TVRENL 1392
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDL 99
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
672-869 |
7.25e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.12 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS-----------KGFGLATQEPWIqFA--TIRDNIL-- 736
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmhkrarLGIGYLPQEASI-FRklTVEDNILav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 737 ---FGKTFDAQlyKEVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVD----A 809
Cdd:COG1137 103 lelRKLSKKER--EERLEE--LLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiavA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 810 DVAN---HLLHRCIlGMlsyttrLLCTH--RtEYLERADAVLLMEAGRLIRAGPPSEIL--PLVQAV 869
Cdd:COG1137 174 DIQKiirHLKERGI-GV------LITDHnvR-ETLGICDRAYIISEGKVLAEGTPEEILnnPLVRKV 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
639-815 |
7.59e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.08 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 639 PDPPAEPSTVLELHGALFSWD--PVgtsLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV-RGLSK 715
Cdd:COG0488 306 PPPERLGKKVLELEGLSKSYGdkTL---LDDL--SLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 716 GFglatqepwiqFATIRDnilfgkTFDAQlyKEVLEA-CALNDDLSILPA----------GDQ--TEVGekgvTLSGGQR 782
Cdd:COG0488 381 GY----------FDQHQE------ELDPD--KTVLDElRDGAPGGTEQEVrgylgrflfsGDDafKPVG----VLSGGEK 438
|
170 180 190
....*....|....*....|....*....|...
gi 2462611208 783 ARIALARAVYQEKELYLLDDPlaavdadvANHL 815
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEP--------TNHL 463
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
672-863 |
8.79e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.93 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAI-----AGELHRLRGHVAVRGLS------------KGFGLATQEP-WIQFATIRD 733
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNiyspdvdpievrREVGMVFQYPnPFPHLTIYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 734 NILFGKTFDA---------QLYKEVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPL 804
Cdd:PRK14267 105 NVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 805 AAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK14267 178 ANIDP-VGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1308-1382 |
9.56e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 9.56e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 1308 PGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDT---SQLELAQLRSQLAIIPQEPF 1382
Cdd:PRK11308 25 ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPY 102
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
672-808 |
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 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAA-------IAGelHRLRGHVAVRG------------LSKGFGLATQEPWIQFATIR 732
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPG--FRVEGKVTFHGknlyapdvdpveVRRRIGMVFQKPNPFPKSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 733 DNILFGKTFDA------QLYKEVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 806
Cdd:PRK14243 109 DNIAYGARINGykgdmdELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
..
gi 2462611208 807 VD 808
Cdd:PRK14243 182 LD 183
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
682-862 |
1.11e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 682 IVGKVGCGKSSLLAAI--AGELH---RLRGHVAVRG------------LSKGFGLATQEPWIQFATIRDNILFGKTFDAQ 744
Cdd:PRK14239 36 LIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGhniysprtdtvdLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 745 LYKEVLEACALNddlSILPAGDQTEVGEK----GVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCI 820
Cdd:PRK14239 116 KDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDP-ISAGKIEETL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462611208 821 LGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK14239 192 LGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
593-857 |
1.27e-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: 59.45 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 593 ALVRMLILPLNNFPWVINgllEAKVSLDRIQLFLDLPNHNPQAYYSPDPPAEPSTvlelHGAL------FSWDPVGTSLE 666
Cdd:COG5265 303 AYLIQLYIPLNFLGFVYR---EIRQALADMERMFDLLDQPPEVADAPDAPPLVVG----GGEVrfenvsFGYDPERPILK 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 667 TfIShLEVKKGMLVGIVGKVGCGKSSLLaaiagelhRL--------RGHVAVRG----------LSKGFGLATQEPwIQF 728
Cdd:COG5265 376 G-VS-FEVPAGKTVAIVGPSGAGKSTLA--------RLlfrfydvtSGRILIDGqdirdvtqasLRAAIGIVPQDT-VLF 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 729 -ATIRDNILFGKTfDAQlYKEVLEA---CALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPL 804
Cdd:COG5265 445 nDTIAYNIAYGRP-DAS-EEEVEAAaraAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 805 AAVD-----------ADVANHllhrcilgmlsyTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 857
Cdd:COG5265 523 SALDsrteraiqaalREVARG------------RTTLVIAHRLSTIVDADEILVLEAGRIVERG 574
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
672-853 |
1.32e-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: 56.65 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------------LSKGFGLATQE-PWIQFATIRDNILF 737
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipyLRRKIGVVFQDfRLLPDRNVYENVAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 -------GKTFDAQLYKEVLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 810
Cdd:cd03292 102 alevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462611208 811 VANHLLHRCILGMLSYTTRLLCTHRTEYLERADA-VLLMEAGRL 853
Cdd:cd03292 171 TTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
672-862 |
1.43e-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: 56.74 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPWI----QF------ATIRDNILF---- 737
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgycpQFdalfdeLTVREHLRFyarl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 -GKtFDAQLYKEVLeacALNDDLSILPAGDqTEVGekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLL 816
Cdd:cd03263 103 kGL-PKSEIKEEVE---LLLRVLGLTDKAN-KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP-ASRRAI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462611208 817 HRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 862
Cdd:cd03263 173 WDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
673-819 |
1.53e-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: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 673 EVKKGMLVGIVGKVGCGKSSLLAaIAGELHRLRGHVAVRGLSKGFGLATQEPWIQFATIRDNILFGKTFDAQLYK----E 748
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRglsdK 552
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 749 VLEACALNDDLS-ILpagdQTEVGEKGV-----TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRC 819
Cdd:TIGR00954 553 DLEQILDNVQLThIL----EREGGWSAVqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
672-872 |
1.63e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 57.39 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG------------LSKGFGLATQEPWIQ-FA-TIRDNILF 737
Cdd:PRK13639 23 FKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkslleVRKTVGIVFQNPDDQlFApTVEEDVAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 G----KTFDAQLYKEVLEACAlnddlsilpagdqtEVGEKGVT------LSGGQRARIALARAVYQEKELYLLDDPLAAV 807
Cdd:PRK13639 103 GplnlGLSKEEVEKRVKEALK--------------AVGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 808 DADVANHLLHrcILGMLSY--TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEILPLVQAVPKA 872
Cdd:PRK13639 169 DPMGASQIMK--LLYDLNKegITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSDIETIRKA 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
672-863 |
1.64e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.21 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV------------RGLsKGFGLATQEPWI-QFATIRDNILFG 738
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplhaRAR-RGIGYLPQEASIfRRLSVYDNLMAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 KTFDAQLYKEVLE--ACALNDDLSILPAGDQTevgekGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLL 816
Cdd:PRK10895 103 LQIRDDLSAEQREdrANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP-ISVIDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462611208 817 HRCILGMLSYTTRLLCTHRT--EYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK10895 177 KRIIEHLRDSGLGVLITDHNvrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
671-815 |
1.66e-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: 54.76 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAvrglskgfglatqepWIQFATIrdnilfgktfdaqlykevl 750
Cdd:cd03221 20 SLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------------WGSTVKI------------------- 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 751 eacalnddlSILPagdQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLaavdadvaNHL 815
Cdd:cd03221 66 ---------GYFE---Q---------LSGGEKMRLALAKLLLENPNLLLLDEPT--------NHL 101
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
672-857 |
1.94e-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: 56.13 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlsKGFGLATQEpwiQFA------------TIRDNILFGk 739
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--KPLDIAARN---RIGylpeerglypkmKVIDQLVYL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 740 tfdAQLyKEVLEACALNDDLSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHR 818
Cdd:cd03269 95 ---AQL-KGLKKEEARRRIDEWLERLELSEYANKRVeELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462611208 819 CILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 857
Cdd:cd03269 170 VIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
672-840 |
2.02e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGElhrlrghvAVRGLSKGFGLATQEPWIQFATIRDNILFGKTFDAQLykEVLE 751
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGA--------LKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAV--ELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 752 ACALNDDLSILPAGDQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS---YTT 828
Cdd:COG2401 121 AVGLSDAVLWLRRFKE---------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR--NLQKLArraGIT 189
|
170
....*....|..
gi 2462611208 829 RLLCTHRTEYLE 840
Cdd:COG2401 190 LVVATHHYDVID 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1292-1453 |
2.53e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1292 LTQGGVEFQDVVLAY--RPGLPNALDgVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE-------------------- 1349
Cdd:PTZ00265 1161 DIKGKIEIMDVNFRYisRPNVPIYKD-LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtne 1239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1350 ----------------------------------PSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDpq 1395
Cdd:PTZ00265 1240 qdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-- 1317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 1396 gLHKDRALWQALKQ----CHLSEVITSMGGLD-GELGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PTZ00265 1318 -FGKEDATREDVKRackfAAIDEFIESLPNKYdTNVGPYGKSLSGGQKQRIAIARALLREPKI 1379
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
674-857 |
2.60e-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: 56.22 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 674 VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------------LSKGFGLAtqePWIqfaTIRDNILF 737
Cdd:cd03266 28 VKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrrlgfVSDSTGLY---DRL---TARENLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 gktFdAQLYKevLEACALNDDLSILpaGDQTEVGE----KGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN 813
Cdd:cd03266 102 ---F-AGLYG--LKGDELTARLEEL--ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462611208 814 HLL----HRCILGmlsyTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 857
Cdd:cd03266 174 ALRefirQLRALG----KCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
674-863 |
3.40e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.15 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 674 VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS---------KGFGLATQ----EPwiQFaTIRDNIL-FGK 739
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvpararlarARIGVVPQfdnlDL--EF-TVRENLLvFGR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 740 TFDAQLyKEVLEACALNDDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRC 819
Cdd:PRK13536 141 YFGMST-REIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWER 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462611208 820 ILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK13536 215 LRSLLARgKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
682-862 |
3.61e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.19 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 682 IVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----LSKGFGLATQEPWI----QFA------TIRDNILFG-KTFDAQL 745
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPPEKRRIgyvfQDArlfphyKVRGNLRYGmAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 746 YKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS 825
Cdd:PRK11144 109 FDKIVALLGIEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP--YLERLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462611208 826 YTTR---LLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK11144 176 REINipiLYVSHSlDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
672-857 |
3.89e-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: 55.28 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLvGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS---------KGFGLATQEP-WIQFATIRD-----NIL 736
Cdd:cd03264 21 LTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvlkqpqklrRRIGYLPQEFgVYPNFTVREfldyiAWL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 737 FG---KTFDAQLyKEVLEACALNDdlsilpagdqtEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVdaDVAN 813
Cdd:cd03264 100 KGipsKEVKARV-DEVLELVNLGD-----------RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL--DPEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462611208 814 HLLHRCILGMLSYT-TRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 857
Cdd:cd03264 166 RIRFRNLLSELGEDrIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
671-849 |
3.99e-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: 54.47 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLAtQEPWIQFATIRDNIlfgktfdaqlykevl 750
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLP-QRPYLPLGTLREQL--------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 751 eacalnddlsILPAGDqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCilgmlsytTRL 830
Cdd:cd03223 85 ----------IYPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL--------KEL 137
|
170 180
....*....|....*....|....
gi 2462611208 831 LCT-----HRTEYLERADAVLLME 849
Cdd:cd03223 138 GITvisvgHRPSLWKFHDRVLDLD 161
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
612-853 |
4.75e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.67 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 612 LLEAKVSLDRIQLFlDLpnhnpqAYYSPD---PPAEPS-TVLELHGALFSWDPVGTSLETFisHLEVKKGMLVGIVGKVG 687
Cdd:PRK10522 289 LLSAQVAFNKLNKL-AL------APYKAEfprPQAFPDwQTLELRNVTFAYQDNGFSVGPI--NLTIKRGELLFLIGGNG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 688 CGKSSLLAAIAGELHRLRGHVAVRGlsKGFGLATQEPWIQ-FATI-RDNILFGKTFDAQlyKEVLEACALNDDLSILPAG 765
Cdd:PRK10522 360 SGKSTLAMLLTGLYQPQSGEILLDG--KPVTAEQPEDYRKlFSAVfTDFHLFDQLLGPE--GKPANPALVEKWLERLKMA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 766 DQTEVGEKGVT---LSGGQRARIALARAVYQEKELYLLDDplAAVDAD-VANHLLHRCILGMLSYT--TRLLCTHRTEYL 839
Cdd:PRK10522 436 HKLELEDGRISnlkLSKGQKKRLALLLALAEERDILLLDE--WAADQDpHFRREFYQVLLPLLQEMgkTIFAISHDDHYF 513
|
250
....*....|....
gi 2462611208 840 ERADAVLLMEAGRL 853
Cdd:PRK10522 514 IHADRLLEMRNGQL 527
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1297-1381 |
4.96e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.25 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPN----ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLE-LAQLR 1371
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90
....*....|
gi 2462611208 1372 SQLAIIPQEP 1381
Cdd:PRK13633 85 NKAGMVFQNP 94
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1313-1447 |
6.73e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 55.43 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSS----------LllvlfrllEPS---SGRVLLDGVD--TSQLELAQLRSQLAII 1377
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTllrclnrmndL--------IPGarvEGEILLDGEDiyDPDVDVVELRRRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1378 PQEPFLFSGTVREN----LDPQGLHKDRAL----WQALKQCHL-SEVitsmggldgelgeGGR------SLSLGQRQLLC 1442
Cdd:COG1117 98 FQKPNPFPKSIYDNvaygLRLHGIKSKSELdeivEESLRKAALwDEV-------------KDRlkksalGLSGGQQQRLC 164
|
....*
gi 2462611208 1443 LARAL 1447
Cdd:COG1117 165 IARAL 169
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
672-863 |
7.24e-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: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAI---------------------------AGELHRLRGHVAVrgLSKGFGLATQEp 724
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirvgditidtarslsqqKGLIRQLRQHVGF--VFQNFNLFPHR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 725 wiqfaTIRDNILFGKTFDAQLYKEvlEACALNDDL--SILPAGDQTEVGEKgvtLSGGQRARIALARAVYQEKELYLLDD 802
Cdd:PRK11264 101 -----TVLENIIEGPVIVKGEPKE--EATARARELlaKVGLAGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 803 PLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
672-860 |
7.42e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.51 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFGK 739
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGrevnaenekwVRSKVGLVFQDPDDQVfsSTVWDDVAFGP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 740 TFDAQLYKEVLEAcaLNDDLSILpagDQTEVGEKG-VTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLlhR 818
Cdd:PRK13647 106 VNMGLDKDEVERR--VEEALKAV---RMWDFRDKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL--M 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462611208 819 CILGMLSY--TTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPS 860
Cdd:PRK13647 179 EILDRLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKS 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
672-872 |
7.51e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.40 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG------------LSKGFGLATQEP--WIQFATIRDNILF 737
Cdd:PRK13638 22 LDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpldyskrgllaLRQQVATVFQDPeqQIFYTDIDSDIAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 G----KTFDAQLYKEVLEACALNDDLSILPAGDQTevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN 813
Cdd:PRK13638 102 SlrnlGVPEAEITRRVDEALTLVDAQHFRHQPIQC--------LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 814 HLLH--RCILGMLSYTtrLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEILPLVQAVPKA 872
Cdd:PRK13638 174 QMIAiiRRIVAQGNHV--IISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEAMEQA 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
672-841 |
7.58e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.43 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIaGELHRLRGHVAVRGLSKGFGLATQEPWIQFATIRDNI--LFGKT--FDAQLYK 747
Cdd:PRK14258 28 MEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYERRVNLNRLRRQVsmVHPKPnlFPMSVYD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 748 EVLEACALN--------DDL--SILPAGD-----QTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 812
Cdd:PRK14258 107 NVAYGVKIVgwrpkleiDDIveSALKDADlwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAS 186
|
170 180 190
....*....|....*....|....*....|..
gi 2462611208 813 ---NHLLHRciLGMLSYTTRLLCTHRTEYLER 841
Cdd:PRK14258 187 mkvESLIQS--LRLRSELTMVIVSHNLHQVSR 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1297-1408 |
8.38e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.61 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG----VDTSQLELAQ 1369
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462611208 1370 LRSQLAIIPQ--EPFLFSGTVRENLD--PQ--GLHKDRALWQALK 1408
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEfgPKnfGFSEDEAKEKALK 127
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1297-1453 |
8.62e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.89 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLA 1375
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 1376 IIPQEPFLFSG-TVRENLDPQGLHKDRALWQAlkqcHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERDQFQE----RIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
635-808 |
8.99e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 635 AYYSPDPPAEPSTVLELHGalFSWDPVGTSletfIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-- 712
Cdd:COG1129 243 DLFPKRAAAPGEVVLEVEG--LSVGGVVRD----VS-FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkp 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 713 ---------LSKGFGLAT----QEPWIQFATIRDNI---LFGKTFDAQLY---KEVLEACALNDDLSILPAGDQTEVGek 773
Cdd:COG1129 316 vrirsprdaIRAGIAYVPedrkGEGLVLDLSIRENItlaSLDRLSRGGLLdrrRERALAEEYIKRLRIKTPSPEQPVG-- 393
|
170 180 190
....*....|....*....|....*....|....*
gi 2462611208 774 gvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 808
Cdd:COG1129 394 --NLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
989-1096 |
1.01e-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: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 989 LLLFSPGNLYIPVFP---LPKAAPNGS-SDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPV 1064
Cdd:cd18572 5 LVVAALSELAIPHYTgavIDAVVADGSrEAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDI 84
|
90 100 110
....*....|....*....|....*....|..
gi 2462611208 1065 TFFNATPTGRILNRFSSDVACADDSLPFILNI 1096
Cdd:cd18572 85 AFFDATKTGELTSRLTSDCQKVSDPLSTNLNV 116
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
680-883 |
1.03e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.19 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 680 VGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFGKT---FDAQ 744
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenireVRKFVGLVFQNPDDQIfsPTVEQDIAFGPInlgLDEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 745 LYK----EVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcI 820
Cdd:PRK13652 113 TVAhrvsSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID--F 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 821 LGMLSYT---TRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEI-------------LPLVQAVPKAWAENGQESDSA 883
Cdd:PRK13652 180 LNDLPETygmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIflqpdllarvhldLPSLPKLIRSLQAQGIAIDMA 259
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1314-1453 |
1.17e-07 |
|
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: 54.26 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSqlELAQLRSQLAIIPQEPFLFSG-TVRENL 1392
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 1393 DpQGLHKDRALWQALKQchlsEV--ITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03299 93 A-YGLKKRKVDKKEIER----KVleIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1318-1448 |
1.29e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 53.99 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1318 TFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlRSqLAIIPQEPFLFSG-TVRENLDpQG 1396
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP-VSMLFQENNLFPHlTVAQNIG-LG 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1397 LHKD--------RALWQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLLCLARALL 1448
Cdd:COG3840 96 LRPGlkltaeqrAQVEQALERVGLAGLLDRLP----------GQLSGGQRQRVALARCLV 145
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
766-863 |
1.50e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.59 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 766 DQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSY--TTRLLCTHRTEYLERAD 843
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEegKTMVVVTHEMGFARHVS 219
|
90 100
....*....|....*....|.
gi 2462611208 844 A-VLLMEAGRLIRAGPPSEIL 863
Cdd:PRK10619 220 ShVIFLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1297-1444 |
1.52e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.64 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1376
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 1377 IPQEP-FLFSG-TVREN----LDPQGLHKD---RALWQALKQCHLSEVITsmggldgelgEGGRSLSLGQRQLLCLA 1444
Cdd:PRK13635 86 VFQNPdNQFVGaTVQDDvafgLENIGVPREemvERVDQALRQVGMEDFLN----------REPHRLSGGQKQRVAIA 152
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1313-1381 |
1.56e-07 |
|
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: 55.85 E-value: 1.56e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKS----SLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLR----SQLAIIPQEP 1381
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEP 101
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1297-1392 |
2.16e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ 1373
Cdd:PRK10908 2 IRFEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQ 80
|
90 100
....*....|....*....|
gi 2462611208 1374 LAIIPQE-PFLFSGTVRENL 1392
Cdd:PRK10908 81 IGMIFQDhHLLMDRTVYDNV 100
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
672-862 |
2.51e-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: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLaaiagelHRLRG-------------HVA-------VRGLSK--------GFGLATQE 723
Cdd:TIGR03269 21 FTIEEGEVLGILGRSGAGKSVLM-------HVLRGmdqyeptsgriiyHVAlcekcgyVERPSKvgepcpvcGGTLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 724 P--WIQFATIRDN------ILFGKTFdaQLYKE--VLEAC--ALND-----DLSILPAGD---QTEVGEK----GVTLSG 779
Cdd:TIGR03269 94 VdfWNLSDKLRRRirkriaIMLQRTF--ALYGDdtVLDNVleALEEigyegKEAVGRAVDlieMVQLSHRithiARDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 780 GQRARIALARAVYQEKELYLLDDPLAAVDADVANhLLHRCILGML--SYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRA 856
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLENGEIKEE 250
|
....*.
gi 2462611208 857 GPPSEI 862
Cdd:TIGR03269 251 GTPDEV 256
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
680-854 |
2.52e-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: 51.61 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 680 VGIVGKVGCGKSSLLAAIAGELHRLRGHVavrglskgfglatqepwiqfatirdnilfgKTFDAQLYKEVLEACALNddl 759
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGV------------------------------IYIDGEDILEEVLDQLLL--- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 760 silpagdqTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGML-----SYTTRLLCTH 834
Cdd:smart00382 52 --------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllksEKNLTVILTT 123
|
170 180
....*....|....*....|
gi 2462611208 835 RTEYLERADAVLLMEAGRLI 854
Cdd:smart00382 124 NDEKDLGPALLRRRFDRRIV 143
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
672-809 |
3.12e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH------RLRGhVAVRGLSKGFGLATQE----PWiqfATIRDNILFGKTF 741
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDG-KPVEGPGAERGVVFQNegllPW---RNVQDNVAFGLQL 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 742 dAQLYKEVLEACALnddlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 809
Cdd:PRK11248 98 -AGVEKMQRLEIAH----QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1313-1368 |
3.18e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.16 E-value: 3.18e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELA 1368
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELG 96
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1296-1453 |
3.31e-07 |
|
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: 53.11 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1296 GVEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRsQLA 1375
Cdd:cd03296 2 SIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-VQER-NVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1376 IIPQEPFLFSG-TVRENL-----------DPQGLHKDRALWQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCL 1443
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPA----------QLSGGQRQRVAL 147
|
170
....*....|
gi 2462611208 1444 ARALLTDAKV 1453
Cdd:cd03296 148 ARALAVEPKV 157
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1296-1451 |
3.53e-07 |
|
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: 53.71 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1296 GVEFQDVVLAYRPGLPNaldgVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqlelaqlrsQLA 1375
Cdd:cd03291 39 NLFFSNLCLVGAPVLKN----INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RIS 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 1376 IIPQEPFLFSGTVRENLdPQGLHKDRALWQA-LKQCHLSEVITSMGGLDGELGEGGR-SLSLGQRQLLCLARALLTDA 1451
Cdd:cd03291 102 FSSQFSWIMPGTIKENI-IFGVSYDEYRYKSvVKACQLEEDITKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDA 178
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1297-1453 |
3.64e-07 |
|
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: 52.64 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLE-----LAQLR 1371
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkdrdIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1372 SQLAIIPQEpflfsgTVRENLD-PQGLHK------DRALWQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLA 1444
Cdd:cd03301 79 QNYALYPHM------TVYDNIAfGLKLRKvpkdeiDERVREVAELLQIEHLLDR----------KPKQLSGGQRQRVALG 142
|
....*....
gi 2462611208 1445 RALLTDAKV 1453
Cdd:cd03301 143 RAIVREPKV 151
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
674-857 |
3.67e-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: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 674 VKKGMLVGIVGKVGCGKSSLLAAIAGEL--HRLRGHVAVRG-------LSKGFGLATQEPwIQFA--TIRDNILFGktfd 742
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGrpldkrsFRKIIGYVPQDD-ILHPtlTVRETLMFA---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 743 AQLykevleacalnddlsilpagdqtevgeKGvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILG 822
Cdd:cd03213 107 AKL---------------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS--LLR 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462611208 823 MLSYTTR-LLCT-H--RTEYLERADAVLLMEAGRLIRAG 857
Cdd:cd03213 156 RLADTGRtIICSiHqpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1304-1453 |
4.16e-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: 51.98 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1304 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLelaqlrsqlAIIPQEPFL 1383
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ---------RDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1384 FSG---------TVRENLD---PQGLHKDRALWQALKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLARALLTDA 1451
Cdd:TIGR01189 77 YLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTG----------FEDLPAAQLSAGQQRRLALARLWLSRR 146
|
..
gi 2462611208 1452 KV 1453
Cdd:TIGR01189 147 PL 148
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1314-1453 |
4.29e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRsQLAI--IPQEPFLFSG-TVRE 1390
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAH-QLGIylVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 1391 NL------DPQGLHKDRALWQALkQCHLSevitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK15439 106 NIlfglpkRQASMQKMKQLLAAL-GCQLD------------LDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1321-1453 |
4.83e-07 |
|
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: 52.11 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1321 VQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAqlRSQLAIIPQEPFLFSG-TVRENLD---PQG 1396
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGlglSPG 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 1397 LH---KDR-ALWQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03298 99 LKltaEDRqAIEVALARVGLAGLEKRL----------PGELSGGERQRVALARVLVRDKPV 149
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
659-863 |
5.88e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.50 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 659 DPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGfglATQEPWIQFATIRDNILFG 738
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIA---KISDAELREVRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 KTFDAQLYKEVLEACALNDDLSILPAGDQTE--------VGEKGVT------LSGGQRARIALARAVYQEKELYLLDDPL 804
Cdd:PRK10070 113 QSFALMPHMTVLDNTAFGMELAGINAEERREkaldalrqVGLENYAhsypdeLSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 805 AAVDADVANHLLHRCI-LGMLSYTTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK10070 193 SALDPLIRTEMQDELVkLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
672-812 |
6.00e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.71 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAG--------ELH-RLRGHVA------VRGLSKGFG----LATQEPWIQFATIR 732
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksaGSHiELLGRTVqregrlARDIRKSRAntgyIFQQFNLVNRLSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 733 DNILFGKTFDAQLYKEVLEACALNDDLSILPAgdQTEVG------EKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 806
Cdd:PRK09984 105 ENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
....*.
gi 2462611208 807 VDADVA 812
Cdd:PRK09984 183 LDPESA 188
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
672-863 |
6.65e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------------LSKGFGLATQEP-WIQFATIRDN 734
Cdd:PRK14246 31 IKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyfgkdifqidaikLRKEVGMVFQQPnPFPHLSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 735 ILF----GKTFDAQLYKEVLEACalnddlsILPAGDQTEVGEK----GVTLSGGQRARIALARAVYQEKELYLLDDPLAA 806
Cdd:PRK14246 111 IAYplksHGIKEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 807 VDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK14246 184 IDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
671-810 |
7.24e-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: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGFGLATQE-PWIQFA-------TIRDNILFGKT 740
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtpLAEQRDEPHENiLYLGHLpglkpelSALENLHFWAA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 741 F--DAQLY-KEVLEACALNDdLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 810
Cdd:TIGR01189 100 IhgGAQRTiEDALAAVGLTG-FEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1313-1453 |
7.25e-07 |
|
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: 50.50 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAIIPQepflfsgtvren 1391
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 1392 ldpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARL 103
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1306-1462 |
7.59e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.48 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1306 YRPGL-----PNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtSQLELA--QLRSQ-LAII 1377
Cdd:PRK15112 16 YRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHFGdySYRSQrIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1378 PQEPF-----------LFSGTVRENLDPQGLHKDRALWQALKQCHLsevitsmggLDGELGEGGRSLSLGQRQLLCLARA 1446
Cdd:PRK15112 93 FQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGL---------LPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180
....*....|....*....|....
gi 2462611208 1447 LLTDAKVRSC--------VSMRPQ 1462
Cdd:PRK15112 164 LILRPKVIIAdealasldMSMRSQ 187
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
682-846 |
7.90e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.64 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 682 IVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----LS-----KGFGLATQEPWIQFATIRDNILfgktFDAQLYKEVLE 751
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistLKpeiyrQQVSYCAQTPTLFGDTVYDNLI----FPWQIRNQQPD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 752 ACALNDDLSI--LPagdqTEVGEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDAD---VANHLLHRcilgmls 825
Cdd:PRK10247 114 PAIFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESnkhNVNEIIHR------- 182
|
170 180
....*....|....*....|....*.
gi 2462611208 826 YTTR-----LLCTHRTEYLERADAVL 846
Cdd:PRK10247 183 YVREqniavLWVTHDKDEINHADKVI 208
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
672-863 |
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 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH--------RLRGHVAVRG----------LSKGFGLATQEPWIQFA-TIR 732
Cdd:PRK13547 22 LRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGeplaaidaprLARLRAVLPQAAQPAFAfSAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 733 DNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQ---------EKELYLLDDP 803
Cdd:PRK13547 102 EIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 804 LAAVDadvanhllhrcilgmLSYTTRLLCTHRTEYLE-----------------RADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK13547 182 TAALD---------------LAHQHRLLDTVRRLARDwnlgvlaivhdpnlaarHADRIAMLADGAIVAHGAPADVL 243
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
677-809 |
1.19e-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: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 677 GMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVavrgLSKGFGLATQEPWIQfatirDNILFGKTFDAqlYKEVLEA---- 752
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----LLNGGPLDFQRDSIA-----RGLLYLGHAPG--IKTTLSVlenl 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 753 ---CALNDDLSILPAGDQteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 809
Cdd:cd03231 95 rfwHADHSDEQVEEALAR--VGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1313-1368 |
1.21e-06 |
|
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: 50.99 E-value: 1.21e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELA 1368
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG 92
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
645-863 |
1.24e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.77 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 645 PSTVLELHGALFSWdPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG------------ 712
Cdd:PRK13636 2 EDYILKVEELNYNY-SDGTHALKGIN-INIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 713 LSKGFGLATQEPwiqfatirDNILFgktfDAQLYKEVlEACALNDDLSilpagdQTEVGEK--------GVT-------- 776
Cdd:PRK13636 80 LRESVGMVFQDP--------DNQLF----SASVYQDV-SFGAVNLKLP------EDEVRKRvdnalkrtGIEhlkdkpth 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 777 -LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhRCILGMLSYT--TRLLCTHRTEYLE-RADAVLLMEAGR 852
Cdd:PRK13636 141 cLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM-KLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGR 219
|
250
....*....|.
gi 2462611208 853 LIRAGPPSEIL 863
Cdd:PRK13636 220 VILQGNPKEVF 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
673-810 |
1.25e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.64 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 673 EVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFG--------LATQEPWIQFATIRDNILFGKTFDAQ 744
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPdvaeachyLGHRNAMKPALTVAENLEFWAAFLGG 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 745 LYKEVLEA-CALN-DDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 810
Cdd:PRK13539 104 EELDIAAAlEAVGlAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1276-1448 |
1.26e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1276 LPQEPQGQPLQLGTGWLTQGGVEFQDVVLAYRPGL-------PNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLL 1348
Cdd:PRK15134 257 LNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKGIlkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1349 ePSSGRVLLDGVDTSQLELAQL---RSQLAIIPQEPFlfsgtvrENLDPQgLHKDRALWQALK--QCHLS------EVIT 1417
Cdd:PRK15134 337 -NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN-------SSLNPR-LNVLQIIEEGLRvhQPTLSaaqreqQVIA 407
|
170 180 190
....*....|....*....|....*....|....
gi 2462611208 1418 SMGGLDGELGEGGR---SLSLGQRQLLCLARALL 1448
Cdd:PRK15134 408 VMEEVGLDPETRHRypaEFSGGQRQRIAIARALI 441
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1297-1392 |
1.44e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 51.62 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQL 1374
Cdd:PRK13639 2 LETRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100
....*....|....*....|
gi 2462611208 1375 AIIPQEP--FLFSGTVRENL 1392
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDV 100
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1314-1451 |
1.50e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 52.76 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqlelaQLRsqLAIIPQEPFLFSG-TVRENL 1392
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------GLR--IGYLPQEPPLDDDlTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1393 dpqgLHKDRALWQALKQchLSEVITSMGGLDGELGEGGR------------------------------------SLSLG 1436
Cdd:COG0488 83 ----LDGDAELRALEAE--LEELEAKLAEPDEDLERLAElqeefealggweaearaeeilsglgfpeedldrpvsELSGG 156
|
170
....*....|....*
gi 2462611208 1437 QRQLLCLARALLTDA 1451
Cdd:COG0488 157 WRRRVALARALLSEP 171
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1304-1396 |
1.89e-06 |
|
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: 50.45 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1304 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlELAQLRSQLAIIPQEPFL 1383
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV 84
|
90
....*....|....
gi 2462611208 1384 FSG-TVRENLDPQG 1396
Cdd:cd03265 85 DDElTGWENLYIHA 98
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
674-862 |
1.94e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.27 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 674 VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFG--- 738
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdIRHKIGMVFQNPDNQFvgATVEDDVAFGlen 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 KTFDAQLYKE-VLEACALnddlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLH 817
Cdd:PRK13650 110 KGIPHEEMKErVNEALEL--------VGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462611208 818 -----RCILGMlsytTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK13650 182 tikgiRDDYQM----TVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1297-1392 |
1.97e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.39 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQL 1374
Cdd:PRK13636 6 LKVEELNYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100
....*....|....*....|
gi 2462611208 1375 AIIPQEP--FLFSGTVRENL 1392
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDV 104
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
672-808 |
1.97e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.04 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGL----------ATQEPWIQFATIRDNILFG--- 738
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALqknlvayvpqSEEVDWSFPVLVEDVVMMGryg 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 739 --------KTFDAQLYKEVLEACALNDDlsilpagDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVD 808
Cdd:PRK15056 108 hmgwlrraKKRDRQIVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1313-1453 |
2.07e-06 |
|
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: 50.70 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAqlRSQLAIIPQEPFLFSG-TVREN 1391
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPHlTVFEN 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 1392 ----LDPQGLHKD---RALWQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03300 93 iafgLRLKKLPKAeikERVAEALDLVQLEGYANRK----------PSQLSGGQQQRVAIARALVNEPKV 151
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
672-863 |
2.20e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 51.34 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGFGLATQEPWI--QFA------TIRDNIL-FGKT 740
Cdd:PRK13537 28 FHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepVPSRARHARQRVGVvpQFDnldpdfTVRENLLvFGRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 741 F---DAQLYKEV---LEacalnddLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANH 814
Cdd:PRK13537 108 FglsAAAARALVpplLE-------FAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 815 LLHRCILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK13537 176 LMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1297-1453 |
2.25e-06 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 49.97 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPglPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtSQLELAQlRSQLAI 1376
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAA-RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1377 IPQEPFLFSG-TVRENL----DPQGLHKDRALWQA---LKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLARALL 1448
Cdd:cd03269 75 LPEERGLYPKmKVIDQLvylaQLKGLKKEEARRRIdewLERLELSE----------YANKRVEELSKGNQQKVQFIAAVI 144
|
....*
gi 2462611208 1449 TDAKV 1453
Cdd:cd03269 145 HDPEL 149
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1313-1453 |
2.34e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQL--AIIPQEPFLFSG-TVR 1389
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLgiGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 1390 ENLdPQGLHKDRAL-------WQALKQchLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK09700 99 ENL-YIGRHLTKKVcgvniidWREMRV--RAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
672-863 |
2.85e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.76 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV----------AVRGLSKGFGLATQEPWIQF-ATIRDNILFGKT 740
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyASKEVARRIGLLAQNATTPGdITVQELVARGRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 741 FDAQLY----KEVLEACAlnddlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL 815
Cdd:PRK10253 108 PHQPLFtrwrKEDEEAVT-----KAMQATGITHLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 816 LHrcILGMLS----YTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK10253 183 LE--LLSELNrekgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
676-843 |
2.89e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 676 KGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPWIQFA----------TIRDNILFGKTFDAQL 745
Cdd:PRK13540 26 AGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVghrsginpylTLRENCLYDIHFSPGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 746 YkEVLEACALN--DDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLL-----HR 818
Cdd:PRK13540 106 V-GITELCRLFslEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIItkiqeHR 174
|
170 180
....*....|....*....|....*
gi 2462611208 819 CILGMLsyttrLLCTHRTEYLERAD 843
Cdd:PRK13540 175 AKGGAV-----LLTSHQDLPLNKAD 194
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
672-863 |
3.14e-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: 49.99 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAG---------------------ELHRLRGHVavrglskgfGLATQepwiQF-- 728
Cdd:COG1126 22 LDVEKGEVVVIIGPSGSGKSTLLRCINLleepdsgtitvdgedltdskkDINKLRRKV---------GMVFQ----QFnl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 729 ---ATIRDNILFGKTFDAQLYKEVLEACALNddlsILpagDQTEVGEKG----VTLSGGQRARIALARAVYQEKELYLLD 801
Cdd:COG1126 89 fphLTVLENVTLAPIKVKKMSKAEAEERAME----LL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 802 DPLAAVD-------ADVANHLLHRcilGMlsytTRLLCTH-----RteylERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG1126 162 EPTSALDpelvgevLDVMRDLAKE---GM----TMVVVTHemgfaR----EVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
671-808 |
3.30e-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: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGML-----VGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFglATQEPWIQFATIRDNILFGKTFD--- 742
Cdd:cd03237 14 TLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY--KPQYIKADYEGTVRDLLSSITKDfyt 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 743 -AQLYKEVLeacalnDDLSILPAGDQtEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVD 808
Cdd:cd03237 92 hPYFKTEIA------KPLQIEQILDR-EVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1314-1453 |
3.48e-06 |
|
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: 49.96 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDGvdtSQLELAQLRSQLAIIPQEPFLFSG-TVR 1389
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 1390 ENL-----------DPQGLHKDRALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03234 100 ETLtytailrlprkSSDAIRKKRVEDVLLRDLALTRI----------GGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1312-1447 |
3.63e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 50.99 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1312 NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlrSQLAIIPQEPFLFSG-TVRE 1390
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1391 NLdPQGLHKDRalwqaLKQCHLSEVITSMGGLDGELGEGGR---SLSLGQRQLLCLARAL 1447
Cdd:PRK11607 111 NI-AFGLKQDK-----LPKAEIASRVNEMLGLVHMQEFAKRkphQLSGGQRQRVALARSL 164
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1297-1392 |
3.80e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 50.12 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1376
Cdd:PRK13647 5 IEVEDLHFRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90
....*....|....*...
gi 2462611208 1377 IPQEP--FLFSGTVRENL 1392
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDV 101
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1314-1453 |
3.84e-06 |
|
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: 49.09 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSL--LLVLFRLLEPSSGRVLLDGVdtsQLELAQLRSQLAIIPQEPFLFSG-TVRE 1390
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILHPTlTVRE 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 1391 nldpqglhkdrALWQALKqchlsevitsmggldgelgegGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03213 102 -----------TLMFAAK---------------------LRGLSGGERKRVSIALELVSNPSL 132
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
672-808 |
4.04e-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: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLL------------AAIAGELhRLRGH---------VAVRglsKGFGLATQEPwIQFA- 729
Cdd:COG1117 32 LDIPENKVTALIGPSGCGKSTLLrclnrmndlipgARVEGEI-LLDGEdiydpdvdvVELR---RRVGMVFQKP-NPFPk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 730 TIRDNILFG--------KTFDAQLYKEVLEACALNDdlsilpagdqtEV----GEKGVTLSGGQRARIALARAVYQEKEL 797
Cdd:COG1117 107 SIYDNVAYGlrlhgiksKSELDEIVEESLRKAALWD-----------EVkdrlKKSALGLSGGQQQRLCIARALAVEPEV 175
|
170
....*....|.
gi 2462611208 798 YLLDDPLAAVD 808
Cdd:COG1117 176 LLMDEPTSALD 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
674-913 |
4.17e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 674 VKKGMLVGIVGKVGCGKSSLLA------------AIAGELHRLRgHVAVRGLSKGFGLATQEPWIQFATIRDNILFG--- 738
Cdd:PTZ00265 408 LTEGKTYAFVGESGCGKSTILKlierlydptegdIIINDSHNLK-DINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlys 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 -------------KTFDAQLYKEVLEACA------------------------------------------LNDDLSILP 763
Cdd:PTZ00265 487 lkdlealsnyyneDGNDSQENKNKRNSCRakcagdlndmsnttdsneliemrknyqtikdsevvdvskkvlIHDFVSALP 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 764 AGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDaDVANHLLHRCILGMLSYTTR--LLCTHRTEYLER 841
Cdd:PTZ00265 567 DKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRitIIIAHRLSTIRY 645
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 842 ADAVLLMeAGRliRAGPPSEILPLVQAVPKAWAENGQESDSATAQSVQNPEKTKEGLEE----EQSTSGRLLQEES 913
Cdd:PTZ00265 646 ANTIFVL-SNR--ERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGsyiiEQGTHDALMKNKN 718
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1304-1370 |
4.89e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 4.89e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 1304 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL 1370
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAL 78
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
672-863 |
5.63e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.63 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWI-QFATIRDNILFGKT 740
Cdd:PRK11231 23 LSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqLARRLALLPQHHLTpEGITVRELVAYGRS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 741 FDAQLYKEVleacALNDDLSILPAGDQTEV---GEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDadvANH-- 814
Cdd:PRK11231 103 PWLSLWGRL----SAEDNARVNQAMEQTRInhlADRRLTdLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD---INHqv 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 815 -LLHrcILGMLSYTTRLLCT--HRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK11231 176 eLMR--LMRELNTQGKTVVTvlHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1314-1453 |
5.69e-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: 48.64 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLD 1393
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 1394 -PQGLHKDRALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03231 96 fWHADHSDEQVEEALARVGLNGF----------EDRPVAQLSAGQQRRVALARLLLSGRPL 146
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
672-871 |
6.24e-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: 50.84 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAI------AGE-------LHRLRGHvAVRGLSKGFGLATQEPwiqFA------TIR 732
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLGLALlrlipsEGEirfdgqdLDGLSRR-ALRPLRRRMQVVFQDP---FGslsprmTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 733 D------NILFGKTFDAQLYKEVLEACAlnddlsilpagdqtEVGEKGVTL-------SGGQRARIALARAVYQEKELYL 799
Cdd:COG4172 383 QiiaeglRVHGPGLSAAERRARVAEALE--------------EVGLDPAARhryphefSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 800 LDDPLAAVDADVANHLL---------HRcilgmLSYttrLLCTH-----RteYLerADAVLLMEAGRLIRAGPPSEIL-- 863
Cdd:COG4172 449 LDEPTSALDVSVQAQILdllrdlqreHG-----LAY---LFISHdlavvR--AL--AHRVMVMKDGKVVEQGPTEQVFda 516
|
250
....*....|....*
gi 2462611208 864 P-------LVQAVPK 871
Cdd:COG4172 517 PqhpytraLLAAAPL 531
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1318-1448 |
6.49e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 49.20 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1318 TFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlrSQLAIIPQEPFLFSG-TVREN----L 1392
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHlTVAQNiglgL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1393 DPqGL---HKDRALWQAL-KQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALL 1448
Cdd:PRK10771 97 NP-GLklnAAQREKLHAIaRQMGIEDLLARLPG----------QLSGGQRQRVALARCLV 145
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1296-1412 |
6.64e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.74 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1296 GVEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVD-TSQ---LELA 1368
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTsknKDIK 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1369 QLRSQLAIIPQ--EPFLFSGTVRENL--DPQ--GLHKDRALWQALKQCHL 1412
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVafGPQnfGVSQEEAEALAREKLAL 131
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1297-1381 |
6.81e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 49.36 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1376
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
....*
gi 2462611208 1377 IPQEP 1381
Cdd:PRK13648 88 VFQNP 92
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1314-1448 |
8.13e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 48.63 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP---SSGRVLLDGVDTSQLElAQLRsQLAIIPQEPFLFSG-TVR 1389
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP-AEQR-RIGILFQDDLLFPHlSVG 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 1390 ENL------DPQGLHKDRALWQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALL 1448
Cdd:COG4136 95 ENLafalppTIGRAQRRARVEQALEEAGLAGFADRDPA----------TLSGGQRARVALLRALL 149
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
674-864 |
8.79e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 49.41 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 674 VKKGMLVGIVGKVGCGKSSLLAAIAGEL---HRLRGHVAVRGLSKG----------FGLATQEPWIQF--ATIRDNILFG 738
Cdd:PRK13640 30 IPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTaktvwdirekVGIVFQNPDNQFvgATVGDDVAFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 KTFDA-------QLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADV 811
Cdd:PRK13640 110 LENRAvprpemiKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 812 ANHLLHRCI-LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILP 864
Cdd:PRK13640 179 KEQILKLIRkLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1314-1453 |
9.28e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 48.33 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTsqlELAQLRSQLAII----PQEPFLfsgTVR 1389
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLghrnAMKPAL---TVA 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 1390 ENLdpqglhkdrALWQALKQCHLSEVITSMGGL--DGELGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK13539 92 ENL---------EFWAAFLGGEELDIAAALEAVglAPLAHLPFGYLSAGQKRRVALARLLVSNRPI 148
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
672-862 |
9.41e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGEL----HRLRGHVAVRGLS------KGFGLAT--QEPWIQF---ATIRDNIL 736
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPvapcalRGRKIATimQNPRSAFnplHTMHTHAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 737 -----FGKTFDAQLYKEVLEACALNDDLSILPAgdqtevgeKGVTLSGG--QRARIALarAVYQEKELYLLDDPLAAVDA 809
Cdd:PRK10418 104 etclaLGKPADDATLTAALEAVGLENAARVLKL--------YPFEMSGGmlQRMMIAL--ALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 810 DVANH---LLHRCI----LGMlsyttrLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK10418 174 VAQARildLLESIVqkraLGM------LLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1314-1453 |
1.03e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 48.86 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSG-TVREnL 1392
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRE-L 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 1393 DPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGR--SLSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK11231 97 VAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRltDLSGGQRQRAFLAMVLAQDTPV 159
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1314-1447 |
1.14e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.91 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRS-----QL-------AIIPQEp 1381
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiQMvfqdsisAVNPRK- 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 1382 flfsgTVRENLDPQGLHKDRaLWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARAL 1447
Cdd:PRK10419 107 -----TVREIIREPLRHLLS-LDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARAL 166
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1297-1453 |
1.15e-05 |
|
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: 48.10 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPNaLDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ--- 1373
Cdd:cd03290 1 VQVTNGYFSWGSGLAT-LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnry 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1374 -LAIIPQEPFLFSGTVRENL---DPQGLHKDRALWQAlkqCHLSEVItSMGGLDGELGEGGRSLSL--GQRQLLCLARAL 1447
Cdd:cd03290 80 sVAYAAQKPWLLNATVEENItfgSPFNKQRYKAVTDA---CSLQPDI-DLLPFGDQTEIGERGINLsgGQRQRICVARAL 155
|
....*.
gi 2462611208 1448 LTDAKV 1453
Cdd:cd03290 156 YQNTNI 161
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1259-1453 |
1.30e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1259 TEAMLVSVERLEEYT-CDLPQ--------EPQGQPLQLGTGWLTQGG--VEFQDVVLAY--RPGLPN-------ALDGVT 1318
Cdd:PRK10261 265 TRALLAAVPQLGAMKgLDYPRrfplisleHPAKQEPPIEQDTVVDGEpiLQVRNLVTRFplRSGLLNrvtrevhAVEKVS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1319 FCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDT-SQLELAQLRSQLAIIPQEPFlfsgtvrENLDP- 1394
Cdd:PRK10261 345 FDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTlSPGKLQALRRDIQFIFQDPY-------ASLDPr 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 1395 --------QGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK10261 418 qtvgdsimEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKV 484
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1294-1453 |
1.47e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.37 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1294 QGGVEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE--PS---SGRVLLDGVDTSQLELA 1368
Cdd:PRK14247 1 MNKIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1369 QLRSQLAIIPQEPFLFSG-TVREN----LDPQGLHKDRA-----LWQALKQCHLSEVITSMGGLDGElgeggrSLSLGQR 1438
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNlSIFENvalgLKLNRLVKSKKelqerVRWALEKAQLWDEVKDRLDAPAG------KLSGGQQ 152
|
170
....*....|....*
gi 2462611208 1439 QLLCLARALLTDAKV 1453
Cdd:PRK14247 153 QRLCIARALAFQPEV 167
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1313-1381 |
1.56e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.93 E-value: 1.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL---RSQLAIIPQEP 1381
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP 107
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
675-865 |
1.78e-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: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 675 KKGMLVGIVGKVGCGKSSLLAAIAgelHRLRGHVAVRGLSKGFGLATQEPWIQ----FA----------TIRDNILFGKT 740
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALA---FRSPKGVKGSGSVLLNGMPIDAKEMRaisaYVqqddlfiptlTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 741 F--DAQLYKE--VLEACALNDDLSILPAGDqTEVGEKGVT--LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH 814
Cdd:TIGR00955 126 LrmPRRVTKKekRERVDEVLQALGLRKCAN-TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 815 LLhRCILGMLSYTTRLLCT-HR--TEYLERADAVLLMEAGRLIRAGPPSEILPL 865
Cdd:TIGR00955 205 VV-QVLKGLAQKGKTIICTiHQpsSELFELFDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
672-863 |
1.91e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.99 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAG--ELH---RLRGHVAVRG----------LSKGFGLATQEP-WIQFATIRDNI 735
Cdd:PRK14247 24 LEIPDNTITALMGPSGSGKSTLLRVFNRliELYpeaRVSGEVYLDGqdifkmdvieLRRRVQMVFQIPnPIPNLSIFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 736 LFGKTFD---------AQLYKEVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 806
Cdd:PRK14247 104 ALGLKLNrlvkskkelQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 807 VDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK14247 177 LDP-ENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVF 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1314-1381 |
1.99e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.19 E-value: 1.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEP 1381
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNP 90
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
673-853 |
2.01e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.50 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 673 EVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGFGLATQE------PWI-QFA------TIRDNI-- 735
Cdd:PRK11629 31 SIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpMSKLSSAAKAElrnqklGFIyQFHhllpdfTALENVam 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 736 --LFGKTFDAQLYKEVLEACAlnddlsilPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN 813
Cdd:PRK11629 111 plLIGKKKPAEINSRALEMLA--------AVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462611208 814 HLLHrcILGMLSY---TTRLLCTHRTEYLERADAVLLMEAGRL 853
Cdd:PRK11629 183 SIFQ--LLGELNRlqgTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1314-1452 |
2.13e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.58 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLEL-AQLRSQLAIIPQEPFLFSG------ 1386
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlsvydn 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 1387 -----TVRENLDPQGlHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARALLTDAK 1452
Cdd:PRK10895 99 lmavlQIRDDLSAEQ-REDRAN-ELMEEFHIEHLRDSM----------GQSLSGGERRRVEIARALAANPK 157
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1012-1096 |
2.38e-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: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1012 SSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLP 1091
Cdd:cd18557 32 LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVT 111
|
....*
gi 2462611208 1092 FILNI 1096
Cdd:cd18557 112 DNLSQ 116
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
661-863 |
2.70e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.23 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 661 VGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAG---------------------ELHRLRGHvavrgLSKGFGL 719
Cdd:PRK03695 8 VSTRLGPL--SAEVRAGEILHLVGPNGAGKSTLLARMAGllpgsgsiqfagqpleawsaaELARHRAY-----LSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 720 ATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSilpagdqTEVGekgvTLSGGQRARIALARAVYQ------ 793
Cdd:PRK03695 81 PFAMPVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLG-------RSVN----QLSGGEWQRVRLAAVVLQvwpdin 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 794 -EKELYLLDDPLAAVD-ADVA--NHLLHR-CILGMlsytTRLLCTH---RTeyLERADAVLLMEAGRLIRAGPPSEIL 863
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 ... |
1025-1082 |
2.74e-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: 2.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 1025 IAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSD 1082
Cdd:cd18780 51 VVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSD 108
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1323-1449 |
3.81e-05 |
|
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: 46.52 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1323 PGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGV---DTSQ-LELAQLRSQLAIIPQEPFLFSG-TVRENLDpQGL 1397
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGLVFQQYALFPHlNVRENLA-FGL 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 1398 HKDRalwQALKQCHLSEVITSMGGLDGELGEGGRsLSLGQRQLLCLARALLT 1449
Cdd:cd03297 101 KRKR---NREDRISVDELLDLLGLDHLLNRYPAQ-LSGGEKQRVALARALAA 148
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
672-863 |
4.00e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.39 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSS-------LLAAIAGELH---------------------------RLRGHVAVRGLSKGF 717
Cdd:PRK13651 28 VEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGTIEwifkdeknkkktkekekvleklviqktRFKKIKKIKEIRRRV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 718 GLATQEPWIQF--ATIRDNILFG-------KTFDAQLYKEVLEACALndDLSILPagdqtevgEKGVTLSGGQRARIALA 788
Cdd:PRK13651 108 GVVFQFAEYQLfeQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQ--------RSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 789 RAVYQEKELYLLDDPLAAVDADVANHLLHrcILGML--SYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLnkQGKTIILVTHDLDNvLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1297-1390 |
4.10e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.08 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVD----TSQLELAQ 1369
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRP 82
|
90 100
....*....|....*....|....
gi 2462611208 1370 LRSQLAIIPQ--EPFLFSGTV-RE 1390
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVeRE 106
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1307-1447 |
4.20e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.72 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1307 RPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRS----QLAIIPQEPF 1382
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFA 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462611208 1383 LFSG-TVRENLD--------PQGLHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARAL 1447
Cdd:PRK10070 117 LMPHmTVLDNTAfgmelagiNAEERREKAL-DALRQVGLENYAHSY----------PDELSGGMRQRVGLARAL 179
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1264-1450 |
4.57e-05 |
|
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: 47.87 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1264 VSVERLEEYTCDLPQEPQGQPLQLGTGWLTQ-GGVEFQDVVLAYrpglPNALDGVTFCV-------QPGEKLGIVGRTGS 1335
Cdd:COG4615 294 VALRKIEELELALAAAEPAAADAAAPPAPADfQTLELRGVTYRY----PGEDGDEGFTLgpidltiRRGELVFIVGGNGS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1336 GKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFsgtvRENLDPQGLHKDRALWQALKQCHLSEV 1415
Cdd:COG4615 370 GKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLERLELDHK 445
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462611208 1416 IT------SmggldgelgegGRSLSLGQRQLLCLARALLTD 1450
Cdd:COG4615 446 VSvedgrfS-----------TTDLSQGQRKRLALLVALLED 475
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
680-815 |
4.62e-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: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 680 VGIVGKVGCGKSSLLAAIAGELHRLRGHVAvrgLSKGF--GLATQEPWI-QFATIRDNILFG--------KTFDA----- 743
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKDFNGEAR---PQPGIkvGYLPQEPQLdPTKTVRENVEEGvaeikdalDRFNEisaky 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 744 --------QLYKE------VLEACA---LNDDLSI------LPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLL 800
Cdd:TIGR03719 111 aepdadfdKLAAEqaelqeIIDAADawdLDSQLEIamdalrCPPWDA-----DVTKLSGGERRRVALCRLLLSKPDMLLL 185
|
170
....*....|....*....
gi 2462611208 801 DDPLAAVDAD-VA---NHL 815
Cdd:TIGR03719 186 DEPTNHLDAEsVAwleRHL 204
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
673-862 |
4.83e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 673 EVKKGMLVGIVGKVGCGKSSL---LAAI----AGELhRLRG-------HVAVRGLSKGFGLATQEPwiqFATI--Rdnil 736
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLarlLTMIetptGGEL-YYQGqdllkadPEAQKLLRQKIQIVFQNP---YGSLnpR---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 737 fgKTFDAQLYkevlEACALNDDLSILPAGDQTEVGEKGVTL------------SGGQRARIALARAVYQEKELYLLDDPL 804
Cdd:PRK11308 109 --KKVGQILE----EPLLINTSLSAAERREKALAMMAKVGLrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 805 AAVDADVANHLLHrciLGM-------LSYttrLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK11308 183 SALDVSVQAQVLN---LMMdlqqelgLSY---VFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
671-819 |
4.95e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.95 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfgLATQEPwiQFAtirdnilfgktfDAQLY---- 746
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP----IRRQRD--EYH------------QDLLYlghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 747 ---KEVLEA-------CALNDDLS---ILPAGDQteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAV 807
Cdd:PRK13538 83 pgiKTELTAlenlrfyQRLHGPGDdeaLWEALAQ--VGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170
....*....|....*.
gi 2462611208 808 D----ADVANHLLHRC 819
Cdd:PRK13538 161 DkqgvARLEALLAQHA 176
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
337-622 |
5.75e-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: 46.73 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 337 LALGLLKLVGTMLGFSGPLLLSLLV-GFLEEGQEPLSHGLL--YALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNI 413
Cdd:cd18563 2 ILGFLLMLLGTALGLVPPYLTKILIdDVLIQLGPGGNTSLLllLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 414 LYCKALQLGPS---RPPTGEALNLLGTDSERLLNFAgsfheAWGLPlqlaitlYLLYQQVGVAFVGGLI------LALL- 483
Cdd:cd18563 82 LYEHLQRLSLSffdKRQTGSLMSRVTSDTDRLQDFL-----SDGLP-------DFLTNILMIIGIGVVLfslnwkLALLv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 484 LVPVNKVIAT-----RIMASNQEMLQHKDARVK-LVTELLSGIRVIKFCGWEQalgarveacraRELGRLRVI--KYLDA 555
Cdd:cd18563 150 LIPVPLVVWGsyffwKKIRRLFHRQWRRWSRLNsVLNDTLPGIRVVKAFGQEK-----------REIKRFDEAnqELLDA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 556 --ACVYLWAALPVVISIVIFITYVLM----GHQLTATK----VFTA-LALVRMLILPLNNFPWVINGLLEAKVSLDRI 622
Cdd:cd18563 219 niRAEKLWATFFPLLTFLTSLGTLIVwyfgGRQVLSGTmtlgTLVAfLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
680-862 |
6.23e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 680 VGIVGKVGCGKSSLLAAI-------AGELH---RLRGHVAVRGLSKGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYKe 748
Cdd:PTZ00243 1339 VGIVGRTGSGKSTLLLTFmrmvevcGGEIRvngREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVdPFLEASSAEVWA- 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 749 VLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELY-LLDDPLAAVDadvanHLLHRCI----LGM 823
Cdd:PTZ00243 1418 ALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFiLMDEATANID-----PALDRQIqatvMSA 1492
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462611208 824 LSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI 862
Cdd:PTZ00243 1493 FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1313-1453 |
7.04e-05 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 46.17 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQ----------LELAQlRSQLA--IIPQE 1380
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKrrkkflrrigVVFGQ-KTQLWwdLPVID 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 1381 PFLFSGTVReNLDPQGLHKDRAlwqalkqcHLSEvitsMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03267 115 SFYLLAAIY-DLPPARFKKRLD--------ELSE----LLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
671-862 |
7.31e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 46.31 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 671 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------------KGFGLATQEPWIQF--ATIRDN 734
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyirpvrKRIGMVFQFPESQLfeDTVERE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 735 ILFG-KTFDAQL-------YKEVLEACALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQEKELYLLDDPLAA 806
Cdd:PRK13646 107 IIFGpKNFKMNLdevknyaHRLLMDLGFSRDVMSQSP-----------FQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 807 VDADvANHLLHRCI--LGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK13646 176 LDPQ-SKRQVMRLLksLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1297-1450 |
7.38e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 46.75 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDT-SQLELAqlRSQLA 1375
Cdd:PRK13536 42 IDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIG 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 1376 IIPQEPFL-FSGTVRENLDPQGlhkdraLWQALKQCHLSEVITSM---GGLDGELGEGGRSLSLGQRQLLCLARALLTD 1450
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLVFG------RYFGMSTREIEAVIPSLlefARLESKADARVSDLSGGMKRRLTLARALIND 190
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1314-1379 |
7.98e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 45.96 E-value: 7.98e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLEL---AQLRSQ-LAIIPQ 1379
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQ 94
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
672-871 |
8.34e-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: 46.58 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGeLHRLRGHVA--------------------VRGlsKGFGLATQEPwiqFA-- 729
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGITSgeilfdgedllklsekelrkIRG--REIQMIFQDP---MTsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 730 ----TIRDNI-----LFGKTFDAQLYK---EVLEACALNDDLSIL---PagdqtevGEkgvtLSGGQRARIALARAVYQE 794
Cdd:COG0444 100 npvmTVGDQIaeplrIHGGLSKAEAREraiELLERVGLPDPERRLdryP-------HE----LSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 795 KELYLLDDPLAAVD----ADVANHL--LHRcILGMlSYttrLLCTH-----RteylERADAVLLMEAGRLIRAGPPSEIL 863
Cdd:COG0444 169 PKLLIADEPTTALDvtiqAQILNLLkdLQR-ELGL-AI---LFITHdlgvvA----EIADRVAVMYAGRIVEEGPVEELF 239
|
250
....*....|....*..
gi 2462611208 864 -----P----LVQAVPK 871
Cdd:COG0444 240 enprhPytraLLSSIPR 256
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
677-869 |
9.03e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 677 GMLVGIVGKVGCGKSSLLAAIAGELH--RLRGHVAVRG------LSKGFGLATQEPWI-QFATIRDNILF------GKTF 741
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNrkptkqILKRTGFVTQDDILyPHLTVRETLVFcsllrlPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 742 DAQlyKEVLEACALNDDLSILPAGDqTEVGEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcI 820
Cdd:PLN03211 174 TKQ--EKILVAESVISELGLTKCEN-TIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL--T 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 821 LGMLSYTTRLLCTHRTEYLERA----DAVLLMEAGRLIRAGPPSEILPLVQAV 869
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQPSSRVyqmfDSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1297-1381 |
9.30e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.24 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAY-RPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLA 1375
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
....*.
gi 2462611208 1376 IIPQEP 1381
Cdd:PRK13642 85 MVFQNP 90
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1268-1448 |
9.68e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1268 RLEEYTCDLPQePQGQPlqlgtGWLTqggVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRL 1347
Cdd:PRK10522 303 ALAPYKAEFPR-PQAFP-----DWQT---LELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1348 LEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTvrenLDPQGLHKDRALWQA-LKQCHLSEVITsmgglDGEL 1426
Cdd:PRK10522 373 YQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHKLE-----LEDG 443
|
170 180
....*....|....*....|..
gi 2462611208 1427 GEGGRSLSLGQRQLLCLARALL 1448
Cdd:PRK10522 444 RISNLKLSKGQKKRLALLLALA 465
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1313-1447 |
1.18e-04 |
|
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: 46.72 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVL--FRLLEPSSGRVL---------------------------------L 1357
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1358 DGVDTSQLELAQLRSQLAIIPQEPFLFSG--TVREN----LDPQGLHKDRALWQA---LKQCHLSEVITSMggldgelge 1428
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvleaLEEIGYEGKEAVGRAvdlIEMVQLSHRITHI--------- 165
|
170
....*....|....*....
gi 2462611208 1429 gGRSLSLGQRQLLCLARAL 1447
Cdd:TIGR03269 166 -ARDLSGGEKQRVVLARQL 183
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
776-839 |
1.40e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 776 TLSGGQRARIALARAVYQEKELYLLDDPlaavdadvANHLLHRCILGMLSYTTR-----LLCTHRTEYL 839
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEP--------TNHLDLHAVLWLETYLLKwpktfIVVSHAREFL 404
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1314-1453 |
1.47e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 46.26 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ-LAIIPQEPFLFSG-TV 1388
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREhFGFIFQRYHLLSHlTA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 1389 RENLD-PQ---GLHKDRALWQA---LKQCHLSEVITsmggldgelgEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK10535 104 AQNVEvPAvyaGLERKQRLLRAqelLQRLGLEDRVE----------YQPSQLSGGQQQRVSIARALMNGGQV 165
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1317-1392 |
1.53e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 1.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 1317 VTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL-DGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL 1392
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1309-1392 |
1.67e-04 |
|
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: 45.95 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1309 GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL----DGVDTSQ---LELAQLRSQLAIIPQEP 1381
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKpgpDGRGRAKRYIGILHQEY 374
|
90
....*....|..
gi 2462611208 1382 FLFS-GTVRENL 1392
Cdd:TIGR03269 375 DLYPhRTVLDNL 386
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1297-1392 |
1.96e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.18 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 1376
Cdd:PRK13652 4 IETRDLCYSYS-GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90
....*....|....*...
gi 2462611208 1377 IPQEP--FLFSGTVRENL 1392
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDI 100
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1315-1452 |
2.10e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.02 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1315 DGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLaiipqepfLFSG-------- 1386
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDL--------LYLGhqpgikte 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 1387 -TVRENLD-PQGLH---KDRALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAK 1452
Cdd:PRK13538 89 lTALENLRfYQRLHgpgDDEALWEALAQVGLAGF----------EDVPVRQLSAGQQRRVALARLWLTRAP 149
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1314-1462 |
2.18e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 44.74 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGV--DTS------QLELAQLRSQLAIIPQEPFLFS 1385
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItiDTArslsqqKGLIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1386 G-TVRENL--DP---QGLHKDRALwqALKQCHLSEVITSmggldGELGEGGRSLSLGQRQLLCLARALltdakvrscvSM 1459
Cdd:PRK11264 99 HrTVLENIieGPvivKGEPKEEAT--ARARELLAKVGLA-----GKETSYPRRLSGGQQQRVAIARAL----------AM 161
|
...
gi 2462611208 1460 RPQ 1462
Cdd:PRK11264 162 RPE 164
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1297-1449 |
2.24e-04 |
|
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: 43.30 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLPNaLDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqlelaqlRSQLAI 1376
Cdd:cd03223 1 IELENLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 1377 IPQEPFLFSGTVRENLdpqglhkdRALWQalkqchlsevitsmggldgelgeggRSLSLGQRQLLCLARALLT 1449
Cdd:cd03223 69 LPQRPYLPLGTLREQL--------IYPWD-------------------------DVLSGGEQQRLAFARLLLH 108
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1301-1453 |
2.25e-04 |
|
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: 43.57 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1301 DVVLAYRP-GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ-LAIIP 1378
Cdd:cd03215 2 EPVLEVRGlSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVP 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462611208 1379 QEPF---LFSG-TVRENLdpqglhkdralwqalkqchlseVITSMggldgelgeggrsLSLGQRQLLCLARALLTDAKV 1453
Cdd:cd03215 82 EDRKregLVLDlSVAENI----------------------ALSSL-------------LSGGNQQKVVLARWLARDPRV 125
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
672-862 |
2.45e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.18 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGeLHR-LRGHVAVRG-----LS-KGFGLATQEPWIQFA--------TIRDNIL 736
Cdd:PRK11153 26 LHIPAGEIFGVIGASGAGKSTLIRCINL-LERpTSGRVLVDGqdltaLSeKELRKARRQIGMIFQhfnllssrTVFDNVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 737 F----GKTFDAQLYK---EVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 809
Cdd:PRK11153 105 LplelAGTPKAEIKArvtELLELVGLSDKADRYPA-----------QLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 810 DVAnhllhRCILGMLSYTTR------LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK11153 174 ATT-----RSILELLKDINRelgltiVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEV 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1297-1355 |
3.08e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 44.69 E-value: 3.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 1297 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRV 1355
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI 64
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1313-1359 |
4.16e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 43.94 E-value: 4.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG 1359
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG 62
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
652-872 |
4.38e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 43.91 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 652 HGALFSWDPVGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSK--GFGLATQEPWIQ 727
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNV--SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGepLAKlnRAQRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 728 FA------------TIRDNI------LFGKTFDAQLYK--EVLEACALND-DLSILPAgdqtevgekgvTLSGGQRARIA 786
Cdd:PRK10419 93 MVfqdsisavnprkTVREIIreplrhLLSLDKAERLARasEMLRAVDLDDsVLDKRPP-----------QLSGGQLQRVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 787 LARAVYQEKELYLLDDPLAAVDAdvanhLLHRCILGML------SYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPP 859
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDL-----VLQAGVIRLLkklqqqFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPV 236
|
250
....*....|...
gi 2462611208 860 SEILPLVQAVPKA 872
Cdd:PRK10419 237 GDKLTFSSPAGRV 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1314-1386 |
4.51e-04 |
|
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: 42.90 E-value: 4.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLF--RLLEPSSGRVLLDGVDTSQLElAQLRSQLAII--PQEPFLFSG 1386
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLP-PEERARLGIFlaFQYPPEIPG 91
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
679-863 |
5.15e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.55 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 679 LVGIVGKVGCGKSSLLAA-------IAGelHRLRGHVAVRGLS-----------KGFGLATQEPWIQFATIRDNILFG-- 738
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTlnrmndkVSG--YRYSGDVLLGGRSifnyrdvlefrRRVGMLFQRPNPFPMSIMDNVLAGvr 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 739 --KTFDAQLYKEVLEAC--------ALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 808
Cdd:PRK14271 127 ahKLVPRKEFRGVAQARltevglwdAVKDRLSDSP-----------FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 809 ADVANHlLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 863
Cdd:PRK14271 196 PTTTEK-IEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1297-1447 |
5.96e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 43.16 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQL 1374
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1375 AIIPQEPFLFSG-TVREN-----LDPQGLHKDRALWQA---LKQCHLSEvitsmggldgelgeggRS------LSLGQRQ 1439
Cdd:PRK09493 80 GMVFQQFYLFPHlTALENvmfgpLRVRGASKEEAEKQArelLAKVGLAE----------------RAhhypseLSGGQQQ 143
|
....*...
gi 2462611208 1440 LLCLARAL 1447
Cdd:PRK09493 144 RVAIARAL 151
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1257-1453 |
6.08e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.62 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1257 TQTEAMLVSVERLEEYTCDlPQEPQGQPLQLGT----GWLTqgGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGR 1332
Cdd:TIGR01257 888 TREERALEKTEPLTEEMED-PEHPEGINDSFFErelpGLVP--GVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1333 TGSGKSSLLLVLFRLLEPSSGRVLLDGVDTsQLELAQLRSQLAIIPQEPFLFSG-TVRENLDPQGLHKDRALWQAlkQCH 1411
Cdd:TIGR01257 965 NGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQLKGRSWEEA--QLE 1041
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462611208 1412 LsEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:TIGR01257 1042 M-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1297-1453 |
6.88e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 43.64 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlELAQLRSQLAI 1376
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1377 IPQ----EPFLfsgTVRENLDPQGlhkdRALWQALKQCH-LSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDA 1451
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFG----RYFGLSAAAARaLVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
..
gi 2462611208 1452 KV 1453
Cdd:PRK13537 158 DV 159
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1297-1402 |
6.88e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 43.57 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL-DGVDTS---QLELAQ 1369
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSStskQKEIKP 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462611208 1370 LRSQLAIIPQEP--FLFSGTVRENL--DPQ--GLHKDRA 1402
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafGPQnfGIPKEKA 120
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1314-1456 |
7.01e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 44.27 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDGVdtsQLELAQLRSQLAIIPQ-EPFLFSGTVR 1389
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM---PIDAKEMRAISAYVQQdDLFIPTLTVR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 1390 ENLDPQG-LHKDRALWQALKQCHLSEVITSMGGLDGE-----LGEGGRSLSLGQRQLLCLARALLTDAKVRSC 1456
Cdd:TIGR00955 118 EHLMFQAhLRMPRRVTKKEKRERVDEVLQALGLRKCAntrigVPGRVKGLSGGERKRLAFASELLTDPPLLFC 190
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1304-1453 |
7.90e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.03 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1304 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG---------------VDTSQLELa 1368
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvADKNQLRL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1369 qLRSQLAIIPQEPFLFSG-TVREN-----LDPQGLHKDRALWQALKqcHLSEV-ITSMGGLDGELgeggrSLSLGQRQLL 1441
Cdd:PRK10619 90 -LRTRLTMVFQHFNLWSHmTVLENvmeapIQVLGLSKQEARERAVK--YLAKVgIDERAQGKYPV-----HLSGGQQQRV 161
|
170
....*....|..
gi 2462611208 1442 CLARALLTDAKV 1453
Cdd:PRK10619 162 SIARALAMEPEV 173
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
674-862 |
8.38e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.82 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 674 VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV----------AVRGLSKGFGLATQEPWIQF--ATIRDNILFGKTF 741
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddNFEKLRKHIGIVFQNPDNQFvgSIVKYDVAFGLEN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 742 DAQLYKEVLE--ACALNDDLSILPAGDQTEvgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLL--- 816
Cdd:PRK13648 112 HAVPYDEMHRrvSEALKQVDMLERADYEPN------ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLdlv 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462611208 817 HRciLGMLSYTTRLLCTHR-TEYLErADAVLLMEAGRLIRAGPPSEI 862
Cdd:PRK13648 186 RK--VKSEHNITIISITHDlSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
478-622 |
9.88e-04 |
|
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: 42.78 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 478 LILALLLVPVNKVIATRIMASnQEMLQHKDARVKlvtELLSGIRVIKFCGWEQALGARVEAcRARELGR--LRVIKylda 555
Cdd:cd18541 151 PLLALLVYRLGKKIHKRFRKV-QEAFSDLSDRVQ---ESFSGIRVIKAFVQEEAEIERFDK-LNEEYVEknLRLAR---- 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462611208 556 acvyLWAALPVVISIVIFITYVL---MGHQLTATKVFTALALV------RMLILPLNNFPWVINGLLEAKVSLDRI 622
Cdd:cd18541 222 ----VDALFFPLIGLLIGLSFLIvlwYGGRLVIRGTITLGDLVafnsylGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1008-1090 |
1.00e-03 |
|
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: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1008 APNGSSDIRFYLTVyATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACAD 1087
Cdd:cd18573 34 EIFGLSLKTFALAL-LGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVG 112
|
...
gi 2462611208 1088 DSL 1090
Cdd:cd18573 113 KSL 115
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
672-816 |
1.10e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.47 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG---------LSKGFGLAT--QE----PWIqfaTIRDNIL 736
Cdd:COG1129 25 LELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvrfrsprDAQAAGIAIihQElnlvPNL---SVAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 737 FGK------TFD-AQLYKEVLEACA-LndDLSILPAgdqTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVD 808
Cdd:COG1129 102 LGReprrggLIDwRAMRRRARELLArL--GLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
....*...
gi 2462611208 809 ADVANHLL 816
Cdd:COG1129 173 EREVERLF 180
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
679-859 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 679 LVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG---------LSKGFGLATQEPWI-QFATIRDNILFGKTFDAQLYKE 748
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldaVRQSLGMCPQHNILfHHLTVAEHILFYAQLKGRSWEE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 749 V-LEACALNDDlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYT 827
Cdd:TIGR01257 1038 AqLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP-YSRRSIWDLLLKYRSGR 1111
|
170 180 190
....*....|....*....|....*....|...
gi 2462611208 828 TRLLCTHRTEYLE-RADAVLLMEAGRLIRAGPP 859
Cdd:TIGR01257 1112 TIIMSTHHMDEADlLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1312-1453 |
1.26e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.07 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1312 NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQLAIIPQEPFLFSGTV 1388
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462611208 1389 --RENLDPQGL--------HKDRALwQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK10584 104 naLENVELPALlrgessrqSRNGAK-ALLEQLGLGKRLDHLPA----------QLSGGEQQRVALARAFNGRPDV 167
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
672-808 |
1.42e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 42.41 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSS-------LLAAIAGELH-------RLRGHvAVRGLSKGFGLATQEPwiqFA------TI 731
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTlgrlllrLEEPTSGEILfdgqditGLSGR-ELRPLRRRMQMVFQDP---YAslnprmTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 732 RDNI-----LFGKTFDAQLYKEV---LEACALN-DDLSILPagdqtevGEkgvtLSGGQRARIALARAVYQEKELYLLDD 802
Cdd:COG4608 115 GDIIaeplrIHGLASKAERRERVaelLELVGLRpEHADRYP-------HE----FSGGQRQRIGIARALALNPKLIVCDE 183
|
....*.
gi 2462611208 803 PLAAVD 808
Cdd:COG4608 184 PVSALD 189
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1297-1450 |
1.72e-03 |
|
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: 41.99 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAY--RPglpnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSG---RVLldGVDTSQLELAQLR 1371
Cdd:COG1119 4 LELRNVTVRRggKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1372 SQLAII-P--QEPFLFSGTVRE--------------NLDPQglHKDRAlWQALKQCHLSEVITsmggldgelgEGGRSLS 1434
Cdd:COG1119 78 KRIGLVsPalQLRFPRDETVLDvvlsgffdsiglyrEPTDE--QRERA-RELLELLGLAHLAD----------RPFGTLS 144
|
170
....*....|....*.
gi 2462611208 1435 LGQRQLLCLARALLTD 1450
Cdd:COG1119 145 QGEQRRVLIARALVKD 160
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1314-1461 |
2.08e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 41.56 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSS-----GRVLLDG--VDTSQLELAQLRSQLAIIPQEPFLFSG 1386
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNqnIYERRVNLNRLRRQVSMVHPKPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1387 TVRENL---------DPQgLHKDRALWQALKQCHLSEVITSMGGLDGElgeggrSLSLGQRQLLCLARALLTDAKV---- 1453
Cdd:PRK14258 103 SVYDNVaygvkivgwRPK-LEIDDIVESALKDADLWDEIKHKIHKSAL------DLSGGQQQRLCIARALAVKPKVllmd 175
|
....*...
gi 2462611208 1454 RSCVSMRP 1461
Cdd:PRK14258 176 EPCFGLDP 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
778-839 |
2.11e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 2.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 778 SGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHllhrcILGMLSyttRLLCTHRTEYL 839
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQ-----ILALLK---SLQQKHQLAYL 480
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1313-1447 |
2.45e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.54 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG----------VDTSQLELAQLR----SQLAIIP 1378
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhvrgADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1379 QEP-------FLFSGTVRENLD-PQGLHKDRALWQA---LKQCHLSEVITSMggldgelGEGGRSLSLGQRQLLCLARAL 1447
Cdd:PRK10261 111 QEPmtslnpvFTVGEQIAESIRlHQGASREEAMVEAkrmLDQVRIPEAQTIL-------SRYPHQLSGGMRQRVMIAMAL 183
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1018-1084 |
3.13e-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: 41.38 E-value: 3.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 1018 YLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVA 1084
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVD 107
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
640-863 |
3.32e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.93 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 640 DPPAEPSTVLELHGALFSWdPVGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL------ 713
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRV-PGRTLLHPL--SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplesws 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 714 SKGFG-----LATQEPWIQFATIRDNILFGK--------TFDAQLYKEVLEACALnddlsilpagdqteVGEKGV----- 775
Cdd:PRK10575 80 SKAFArkvayLPQQLPAAEGMTVRELVAIGRypwhgalgRFGAADREKVEEAISL--------------VGLKPLahrlv 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 776 -TLSGGQRARIALARAVYQEKELYLLDDPLAAVD----ADVANhLLHRciLGMLSYTTRLLCTHRTEYLER-ADAVLLME 849
Cdd:PRK10575 146 dSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLA-LVHR--LSQERGLTVIAVLHDINMAARyCDYLVALR 222
|
250
....*....|....
gi 2462611208 850 AGRLIRAGPPSEIL 863
Cdd:PRK10575 223 GGEMIAQGTPAELM 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1297-1388 |
3.40e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 41.16 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1297 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL-DGV---DTSQLELAQ 1369
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVitaGKKNKKLKP 82
|
90 100
....*....|....*....|.
gi 2462611208 1370 LRSQLAIIPQ--EPFLFSGTV 1388
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETV 103
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1313-1453 |
4.28e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 40.53 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE--PS---SGRVLLDGVD--TSQLELAQLRSQLAIIPQEPFLFS 1385
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462611208 1386 GTVREN----LDPQGLHK----DRALWQALKQCHL-SEVITSMGGLDGelgeggrSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK14239 100 MSIYENvvygLRLKGIKDkqvlDEAVEKSLKGASIwDEVKDRLHDSAL-------GLSGGQQQRVCIARVLATSPKI 169
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1297-1358 |
4.91e-03 |
|
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: 38.97 E-value: 4.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611208 1297 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLD 1358
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG 60
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1309-1462 |
5.10e-03 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 40.38 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1309 GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG------VDTSQLELAQLRSQLAIIPQE-- 1380
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1381 --PFLfsgTVRENL--DP---QGLHKDRALWQA---LKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLtd 1450
Cdd:PRK11124 93 lwPHL---TVQQNLieAPcrvLGLSKDQALARAeklLERLRLKPYADRFPL----------HLSGGQQQRVAIARALM-- 157
|
170
....*....|..
gi 2462611208 1451 akvrscvsMRPQ 1462
Cdd:PRK11124 158 --------MEPQ 161
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1309-1381 |
5.92e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.48 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1309 GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDG---VDTSQLELAQLRS-QLAIIPQEP 1381
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGreiLNLPEKELNKLRAeQISMIFQDP 106
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1313-1390 |
6.14e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.16 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1313 ALDGVTFCVqPGEKL--------------GIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIP 1378
Cdd:PRK10575 13 ALRNVSFRV-PGRTLlhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90
....*....|...
gi 2462611208 1379 QE-PFLFSGTVRE 1390
Cdd:PRK10575 92 QQlPAAEGMTVRE 104
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
682-802 |
6.45e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 682 IVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGfglATQEPWIQF----------ATIRDNILFGKTF--DAQLYKEV 749
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN---NIAKPYCTYighnlglkleMTVFENLKFWSEIynSAETLYAA 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462611208 750 LEACALNDDLSilpagdqtevgEKGVTLSGGQRARIALARAVYQEKELYLLDD 802
Cdd:PRK13541 108 IHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1314-1381 |
6.70e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 40.38 E-value: 6.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQLAIIPQEP 1381
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDP 86
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1298-1392 |
7.54e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.78 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1298 EFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ-LAI 1376
Cdd:COG3845 259 EVENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAY 337
|
90 100
....*....|....*....|
gi 2462611208 1377 IPQEPFLF----SGTVRENL 1392
Cdd:COG3845 338 IPEDRLGRglvpDMSVAENL 357
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
456-622 |
8.69e-03 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 40.10 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 456 PLQLAITL-YLLYQQVGVAFVGGLILALLLVPVNKV------IATRIMASNQEMLQHkdarvklVTELLSGIRVIK-FCG 527
Cdd:cd18552 124 PLTVIGLLgVLFYLDWKLTLIALVVLPLAALPIRRIgkrlrkISRRSQESMGDLTSV-------LQETLSGIRVVKaFGA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 528 wEQALGARV-EACRARELGRLRVIKYLDAA--CVYLWAAlpVVISIVIFI-TYVLMGHQLTATKVFTALALVRMLILPLN 603
Cdd:cd18552 197 -EDYEIKRFrKANERLRRLSMKIARARALSspLMELLGA--IAIALVLWYgGYQVISGELTPGEFISFITALLLLYQPIK 273
|
170
....*....|....*....
gi 2462611208 604 NFPWVINGLLEAKVSLDRI 622
Cdd:cd18552 274 RLSNVNANLQRGLAAAERI 292
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1314-1453 |
8.79e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 39.65 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 1314 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE------PSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSG- 1386
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462611208 1387 TVREN----LDPQGLHKDRALWQALKQChLSEViTSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKV 1453
Cdd:PRK14246 106 SIYDNiaypLKSHGIKEKREIKKIVEEC-LRKV-GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
672-816 |
8.84e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.58 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 672 LEVKKGMLVGIVGKVGCGKSSLLAAIA---------GELHRLRGHVAVRGLS----KGFGLATQE-PWIQFATIRDNILF 737
Cdd:TIGR02633 22 LEVRPGECVGLCGENGAGKSTLMKILSgvyphgtwdGEIYWSGSPLKASNIRdterAGIVIIHQElTLVPELSVAENIFL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611208 738 G--------KTFDAQLY---KEVLEACALNDDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAA 806
Cdd:TIGR02633 102 GneitlpggRMAYNAMYlraKNLLRELQLDADNVTRPVGD----------YGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170
....*....|
gi 2462611208 807 VDADVANHLL 816
Cdd:TIGR02633 172 LTEKETEILL 181
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1297-1374 |
8.91e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 40.43 E-value: 8.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611208 1297 VEFQDVVLAYrPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLdGVDTSQLELAQLRSQL 1374
Cdd:COG0488 316 LELEGLSKSY-GDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIGYFDQHQEEL 390
|
|
| |
