|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
273-1222 |
1.85e-172 |
|
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: 551.09 E-value: 1.85e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 273 LWRALYGAFGRCYLALGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVT 352
Cdd:TIGR00957 307 LFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSG 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 353 LQARGAVLNILYCKALQLGPS--RPPT-GEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLIL 429
Cdd:TIGR00957 387 MRIKTAVMGAVYRKALVITNSarKSSTvGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAV 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 430 ALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYL 509
Cdd:TIGR00957 467 MVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFT 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 510 WAALPVVISIVIFITYVLMGHQ--LTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLFLDLPNHNPQAYYS 587
Cdd:TIGR00957 547 WVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIER 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 588 PDPPAEPSTVLELHGALFSW---DPVGTSLETFishlEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlsk 664
Cdd:TIGR00957 627 RTIKPGEGNSITVHNATFTWardLPPTLNGITF----SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--- 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 665 GFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEK 744
Cdd:TIGR00957 700 SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 745 ELYLLDDPLAAVDADVANHLLHRCI--LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPK-- 820
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEfl 859
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 821 ---AWAENGQESDSATAQSVQNPEKTKEGLE----------------------------------------EEQSTSGRL 857
Cdd:TIGR00957 860 rtyAPDEQQGHLEDSWTALVSGEGKEAKLIEngmlvtdvvgkqlqrqlsasssdsgdqsrhhgssaelqkaEAKEETWKL 939
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 858 LQEESKKEGAVALHVYQAYWKAVGQGLALAILFSLLLMQATRNAADWWLSHWISQLKAeNSSQEaqpstspasmglfspq 937
Cdd:TIGR00957 940 MEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMV-NGTQN---------------- 1002
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 938 lllfspgnlyipvfplpkaapngssDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFN 1017
Cdd:TIGR00957 1003 -------------------------NTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE 1057
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1018 ATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGS 1097
Cdd:TIGR00957 1058 RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLES 1137
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1098 LTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQg 1177
Cdd:TIGR00957 1138 VSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHS- 1216
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*
gi 2217363546 1178 lANPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEYT 1222
Cdd:TIGR00957 1217 -LSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYS 1260
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
215-1228 |
6.63e-145 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 476.01 E-value: 6.63e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 215 EDGESWLSRFSYAWLAPLLARGacgeLRQP---QDICRLPHRLQPTYLARVFQAHWQEGAR-----LWRALYGAFGRCYL 286
Cdd:PLN03232 229 ERYASIFSRIYFSWMTPLMQLG----YRKPiteKDVWQLDQWDQTETLIKRFQRCWTEESRrpkpwLLRALNNSLGGRFW 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 287 ALGLLKLVGTMLGFSGPLLLSLLVGFLEEGqEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCK 366
Cdd:PLN03232 305 LGGIFKIGHDLSQFVGPVILSHLLQSMQEG-DPAWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 367 ALQL---GPSRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATR 443
Cdd:PLN03232 384 SLRLtheARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRK 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 444 IMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFI 523
Cdd:PLN03232 464 MRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 524 TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI-QLFLdlpnhNPQAYYSPDPPAEPST-VLELH 601
Cdd:PLN03232 544 VFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIeELLL-----SEERILAQNPPLQPGApAISIK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 602 GALFSWDPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGEL-HRLRGHVAVRGlskGFGLATQEPWIQFATI 680
Cdd:PLN03232 619 NGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELsHAETSSVVIRG---SVAYVPQVSWIFNATV 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 681 RDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADV 760
Cdd:PLN03232 696 RENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 761 ANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEiLPLVQAVPKAWAENGQESDSATAQSVQNP 840
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAGKMDATQEVNTNDE 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 841 EKTKEGLEEEQSTSGR--------------LLQEESKKEGAVALHVYQAYWKAVGQGLALAILFS-LLLMQATRNAADWW 905
Cdd:PLN03232 855 NILKLGPTVTIDVSERnlgstkqgkrgrsvLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVcYLTTEVLRVSSSTW 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 906 LSHWISQLKAENssqeaqpstspasmglfspqlllFSPGnlyipvfplpkaapngssdirFYLTVYATIAGVNSLCTLLR 985
Cdd:PLN03232 935 LSIWTDQSTPKS-----------------------YSPG---------------------FYIVVYALLGFGQVAVTFTN 970
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 986 AVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLP 1065
Cdd:PLN03232 971 SFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVST 1050
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1066 WLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATS 1145
Cdd:PLN03232 1051 ISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANT 1130
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1146 ATMQWLDIRLQLMGAAVVSAIAGIALVQH-----QQGLANpgLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEE 1220
Cdd:PLN03232 1131 SSNRWLTIRLETLGGVMIWLTATFAVLRNgnaenQAGFAS--TMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGN 1208
|
....*...
gi 2217363546 1221 YTcDLPQE 1228
Cdd:PLN03232 1209 YI-DLPSE 1215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
203-1228 |
1.90e-136 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 454.97 E-value: 1.90e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 203 PLLPEDQEPEVAED---GE--------SWLSRFSYAWLAPLLARGACGELRQPqDICRLPHRLQPTYLARVFQAHWQEGA 271
Cdd:PLN03130 206 PIGSESVDDYEYEElpgGEqicperhaNIFSRIFFGWMTPLMQLGYKRPLTEK-DVWKLDTWDQTETLYRSFQKCWDEEL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 272 R-----LWRALYGAFGRCYLALGLLKLVGTMLGFSGPLLLSLLVGFLEEGqEPLSHGLLYALGLAGGAVLGAVLQNQYGY 346
Cdd:PLN03130 285 KkpkpwLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNG-EPAWIGYIYAFSIFVGVVLGVLCEAQYFQ 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 347 EVYKVTLQARGAVLNILYCKALQL---GPSRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAF 423
Cdd:PLN03130 364 NVMRVGFRLRSTLVAAVFRKSLRLtheGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVAS 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 424 VGGLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLD 503
Cdd:PLN03130 444 LIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLS 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 504 AACVYLWAALPVVISIVIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQ-LFLdlpnhNP 582
Cdd:PLN03130 524 AFNSFILNSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEeLLL-----AE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 583 QAYYSPDPPAEPST-VLELHGALFSWDPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGEL-HRLRGHVAVR 660
Cdd:PLN03130 599 ERVLLPNPPLEPGLpAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 661 GlskGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAV 740
Cdd:PLN03130 679 G---TVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAV 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 741 YQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL---PLVQ- 816
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSnngPLFQk 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 817 ----------AVPKAWAENGQESDSATAQSVQNPEKTKEGLEEEQSTSGR--LLQEESKKEGAVALHVYQAYWKAVGQGL 884
Cdd:PLN03130 836 lmenagkmeeYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKsvLIKQEERETGVVSWKVLERYKNALGGAW 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 885 ALAILF-SLLLMQATRNAADWWLSHWISQlkaenssqeaqpsTSPASMGlfspqlllfsPGnlyipvfplpkaapngssd 963
Cdd:PLN03130 916 VVMILFlCYVLTEVFRVSSSTWLSEWTDQ-------------GTPKTHG----------PL------------------- 953
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 964 irFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFIL 1043
Cdd:PLN03130 954 --FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFV 1031
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1044 NILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGAT 1123
Cdd:PLN03130 1032 NMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAY 1111
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1124 YRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQH-----QQGLANpgLVGLSLSYALSLTGLL 1198
Cdd:PLN03130 1112 DRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNgraenQAAFAS--TMGLLLSYALNITSLL 1189
|
1050 1060 1070
....*....|....*....|....*....|
gi 2217363546 1199 SGLVSSFTQTEAMLVSVERLEEYTcDLPQE 1228
Cdd:PLN03130 1190 TAVLRLASLAENSLNAVERVGTYI-DLPSE 1218
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
288-571 |
2.25e-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: 411.18 E-value: 2.25e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 288 LGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKA 367
Cdd:cd18598 2 LGLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 368 LQLGPSR---PPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRI 444
Cdd:cd18598 82 LRVRSSSlskFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 445 MASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFIT 524
Cdd:cd18598 162 GALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2217363546 525 YVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18598 242 YVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
287-571 |
1.24e-126 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 391.19 E-value: 1.24e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 287 ALGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCK 366
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 367 ALQLGPS---RPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATR 443
Cdd:cd18559 81 ALRSPISffeRTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 444 IMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFI 523
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2217363546 524 TYVLMGH--QLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18559 241 AYVSRHSlaGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
273-1228 |
3.70e-114 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 391.06 E-value: 3.70e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 273 LWRALYGAFGRCYLALGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVT 352
Cdd:PTZ00243 234 LLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 353 LQARGAVLNILYCKALQLGP---SRPP--TGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGL 427
Cdd:PTZ00243 314 LQYRSALNALIFEKCFTISSkslAQPDmnTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 428 ILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACV 507
Cdd:PTZ00243 394 AVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 508 YLWAALPVVISIVIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLFLDLPN-------- 579
Cdd:PTZ00243 474 FVNNATPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNatcstvqd 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 580 ----------HNP-------------QAYYSPDPPAEPSTVLELHGALFSW----------------------------- 607
Cdd:PTZ00243 554 meeywreqreHSTacqlaavlenvdvTAFVPVKLPRAPKVKTSLLSRALRMlcceqcrptkrhpspsvvvedtdygspss 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 608 -----DPVGTS-------------------LETFIS----------HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRL 653
Cdd:PTZ00243 634 asrhiVEGGTGggheatptsersaktpkmkTDDFFElepkvllrdvSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 654 RGHVAVrglSKGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRAR 733
Cdd:PTZ00243 714 EGRVWA---ERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKAR 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 734 IALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL- 812
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMr 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 813 -PLVQAVPKAWAEN--GQESDS-----------ATAQSVQNPEKTKEGLEEEQ------STSGRLLQEESKKEGAVALHV 872
Cdd:PTZ00243 871 tSLYATLAAELKENkdSKEGDAdaevaevdaapGGAVDHEPPVAKQEGNAEGGdgaaldAAAGRLMTREEKASGSVPWST 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 873 YQAYWKAVGQGL-ALAILFSLLLMQATRNAADWWLSHWisqlkaenssqeaqpstSPASMGLfspqlllfspgnlyipvf 951
Cdd:PTZ00243 951 YVAYLRFCGGLHaAGFVLATFAVTELVTVSSGVWLSMW-----------------STRSFKL------------------ 995
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 952 plpkaapngSSDIrfYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSD 1031
Cdd:PTZ00243 996 ---------SAAT--YLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRD 1064
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1032 VACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTL 1111
Cdd:PTZ00243 1065 IDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEAL 1144
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1112 AGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLA--NPGLVGLSLS 1189
Cdd:PTZ00243 1145 QGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATsqEIGLVSLSLT 1224
|
1050 1060 1070
....*....|....*....|....*....|....*....
gi 2217363546 1190 YALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTCDLPQE 1228
Cdd:PTZ00243 1225 MAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHE 1263
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
885-1222 |
1.60e-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: 329.49 E-value: 1.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 885 ALAILFSLLLMQATRNAADWWLSHWISQLKAENSSQeaqpstspasmglfspqlllfspgnlyipvfplpkaapnGSSDI 964
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNF---------------------------------------INDSF 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 965 RFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILN 1044
Cdd:cd18605 42 NFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1045 ILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATY 1124
Cdd:cd18605 122 ILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1125 RFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGL-ANPGLVGLSLSYALSLTGLLSGLVS 1203
Cdd:cd18605 202 RFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAVVQHFFGLsIDAGLIGLALSYALPITGLLSGLLN 281
|
330
....*....|....*....
gi 2217363546 1204 SFTQTEAMLVSVERLEEYT 1222
Cdd:cd18605 282 SFTETEKEMVSVERVRQYF 300
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
598-801 |
1.01e-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: 320.57 E-value: 1.01e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 598 LELHGALFSWDPVGTSLETFIS--HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlskGFGLATQEPWI 675
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKdiNLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG---SIAYVSQEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 676 QFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:cd03250 78 QNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217363546 756 VDADVANHLLHRCILGMLSYT-TRLLCTHRTEYLERADAVLLMEAGR 801
Cdd:cd03250 158 VDAHVGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
288-571 |
6.03e-89 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 289.39 E-value: 6.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 288 LGLLKLVGTMLGFSGPLLLSLLVGFLEE-GQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCK 366
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 367 ALQLGPS---RPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATR 443
Cdd:cd18579 82 ALRLSSSarqETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 444 IMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFI 523
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2217363546 524 TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
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, ... |
289-571 |
4.17e-78 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 259.32 E-value: 4.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 289 GLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKAL 368
Cdd:cd18595 3 ALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 369 QLGP-SRP--PTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRIM 445
Cdd:cd18595 83 RLSNsARKksTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 446 ASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITY 525
Cdd:cd18595 163 KLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2217363546 526 VLMG--HQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18595 243 VLSDpdNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
219-1228 |
5.92e-74 |
|
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: 270.63 E-value: 5.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 219 SWLSRFSYAWLAPLLARGACGELrQPQDICRLPHRLQPTYLARVFQAHW-------QEGARLWRALYGAFGRCYLALGLL 291
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKL-ELSDIYQIPSFDSADNLSERLEREWdrelasaKKNPKLLNALRRCFFWRFVFYGIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 292 KLVGTMLGFSGPLLLSLLVG-FLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKALQL 370
Cdd:TIGR01271 89 LYFGEATKAVQPLLLGRIIAsYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 371 GP---SRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRIMAS 447
Cdd:TIGR01271 169 SSrvlDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 448 NQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVI---KYLDAACVYLWAALPVVISIVifiT 524
Cdd:TIGR01271 249 RDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIaylRYFYSSAFFFSGFFVVFLSVV---P 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 525 YVLMgHQLTATKVFTALALVRMLILPLN-NFPWVINGLLEAKVSLDRIQLFLDLPNHNPQAYyspdppAEPSTVLELHGA 603
Cdd:TIGR01271 326 YALI-KGIILRRIFTTISYCIVLRMTVTrQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEY------NLTTTEVEMVNV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 604 LFSWDP-VGTSLET-----------------FISHLE-------------VKKGMLVGIVGKVGCGKSSLLAAIAGELHR 652
Cdd:TIGR01271 399 TASWDEgIGELFEKikqnnkarkqpngddglFFSNFSlyvtpvlknisfkLEKGQLLAVAGSTGSGKSSLLMMIMGELEP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 653 LRGHVAVRGLskgFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRA 732
Cdd:TIGR01271 479 SEGKIKHSGR---ISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 733 RIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI- 811
Cdd:TIGR01271 556 RISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELq 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 812 ---------LPLVQAVPKAWAENGQ------------ESDSATA-------QSVQNP-----EKTK-------------- 844
Cdd:TIGR01271 636 akrpdfsslLLGLEAFDNFSAERRNsiltetlrrvsiDGDSTVFsgpetikQSFKQPppefaEKRKqsiilnpiasarkf 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 845 ----------EGLEEEQSTSGRL-----------LQEESKKEGAVALH--VYQAYWK----------AVGQGL--ALAIL 889
Cdd:TIGR01271 716 sfvqmgpqkaQATTIEDAVREPSerkfslvpedeQGEESLPRGNQYHHglQHQAQRRqsvlqlmthsNRGENRreQLQTS 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 890 FSLLLMQATRNAADWWLSHWISQLKAENS------------------SQEAQPSTSPASMGL---FSPQLLLF------- 941
Cdd:TIGR01271 796 FRKKSSITQQNELASELDIYSRRLSKDSVyeiseeineedlkecfadERENVFETTTWNTYLryiTTNRNLVFvlifclv 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 942 --------SPGNLYI----PVFPL----------------PKAAPNGSSdirfYLTVYATIAGVNSLCTL--LRAVLFAA 991
Cdd:TIGR01271 876 iflaevaaSLLGLWLitdnPSAPNyvdqqhanasspdvqkPVIITPTSA----YYIFYIYVGTADSVLALgfFRGLPLVH 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 992 GTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLL 1071
Cdd:TIGR01271 952 TLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAA 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1072 PPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWL 1151
Cdd:TIGR01271 1032 IPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWF 1111
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217363546 1152 DIRLQLMGAAVVSAIAGIALVQHQQGlanPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTcDLPQE 1228
Cdd:TIGR01271 1112 QMRIDIIFVFFFIAVTFIAIGTNQDG---EGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFI-DLPQE 1184
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
287-571 |
2.83e-66 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 226.61 E-value: 2.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 287 ALGLLKLVGTMLGFSGPLLLSLLVGFLEE-GQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYC 365
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLEDpGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 366 KALQL----GPSRPP------------------TGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGV-A 422
Cdd:cd18596 81 KALRRrdksGSSKSSeskkkdkeededekssasVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWsA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 423 FVGGLILALLLvPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYL 502
Cdd:cd18596 161 LVGLAVMVLLL-PLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 503 DAACVYLWAALPVVISIVIFITYVL-MGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18596 240 DLLLSLLWFLIPILVTVVTFATYTLvMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
886-1222 |
1.36e-63 |
|
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: 218.14 E-value: 1.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 886 LAILFSLLLMQATRNAADWWLSHWISQlkaenssqeaqpstspasmglfspqlllfspgnlyipvfplpkAAPNGSSDIR 965
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSD-------------------------------------------WSSSPNSSSG 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 966 FYLTVYATIAGVNS-LCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILN 1044
Cdd:cd18580 39 YYLGVYAALLVLASvLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1045 ILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATY 1124
Cdd:cd18580 119 DFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1125 RFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQglANPGLVGLSLSYALSLTGLLSGLVSS 1204
Cdd:cd18580 199 RFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALLAVLLRSS--ISAGLVGLALTYALSLTGSLQWLVRQ 276
|
330
....*....|....*...
gi 2217363546 1205 FTQTEAMLVSVERLEEYT 1222
Cdd:cd18580 277 WTELETSMVSVERILEYT 294
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
289-571 |
2.87e-60 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 208.85 E-value: 2.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 289 GLLKLVGTMLGFSGPLLLSLLVGFLEEGQE-----PLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNIL 363
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLINFVEDAYLggpppSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 364 YCKALQL-GPSR--PPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVI 440
Cdd:cd18597 83 YRKSLRLsGKSRheFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 441 ATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIV 520
Cdd:cd18597 163 MKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASML 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2217363546 521 IFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18597 243 SFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
954-1222 |
1.97e-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: 203.48 E-value: 1.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 954 PKAAPNGSSDIR-FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDV 1032
Cdd:cd18603 29 PALNGTQDTEQRdYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1033 ACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLA 1112
Cdd:cd18603 109 DTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1113 GLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlaNPGLVGLSLSYAL 1192
Cdd:cd18603 189 GASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLFAALFAVLSRDSL--SPGLVGLSISYAL 266
|
250 260 270
....*....|....*....|....*....|
gi 2217363546 1193 SLTGLLSGLVSSFTQTEAMLVSVERLEEYT 1222
Cdd:cd18603 267 QITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
272-812 |
7.92e-55 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 201.93 E-value: 7.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 272 RLWRALYGAFGRCYLALgLLKLVGTMLGFSGPLLLSLLVGFLEEGQePLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKV 351
Cdd:COG1132 11 RLLRYLRPYRGLLILAL-LLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLLLLLLGLALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 352 TLQARGAVLNILYCKALQLGPS---RPPTGEALNLLGTDSERLLNFAG-SFHEAWGLPLQLAITL-YLLYQQVGVAFVGG 426
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSffdRRRTGDLLSRLTNDVDAVEQFLAhGLPQLVRSVVTLIGALvVLFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 427 LILALLLVPVnKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEAcRARELGR--LRVIKYLDA 504
Cdd:COG1132 169 LVLPLLLLVL-RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE-ANEELRRanLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 505 --ACVYLWAALPVVISIVIFITYVLMGhQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLFLDLPNHNP 582
Cdd:COG1132 247 ffPLMELLGNLGLALVLLVGGLLVLSG-SLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 583 QAYySPDPPAEPSTVLELHGALFSWDPVGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAG-------------- 648
Cdd:COG1132 326 DPP-GAVPLPPVRGEIEFENVSFSYPGDRPVLKDI--SLTIPPGETVALVGPSGSGKSTLVNLLLRfydptsgrilidgv 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 649 -----ELHRLRGHVAVrglskgfglATQEPWIQFATIRDNILFGK---TfDAQLyKEVLEACALNDDLSILPAGDQTEVG 720
Cdd:COG1132 403 dirdlTLESLRRQIGV---------VPQDTFLFSGTIRENIRYGRpdaT-DEEV-EEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 721 EKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAG 800
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETE-ALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
570
....*....|..
gi 2217363546 801 RLIRAGPPSEIL 812
Cdd:COG1132 551 RIVEQGTHEELL 562
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
886-1222 |
2.12e-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: 191.91 E-value: 2.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 886 LAILFSLLLMQATRNAADWWLSHWisqlkaenSSQEAQPSTSPASmglfspqlllfspgnlyipvfplpkaapngSSDIR 965
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIW--------ASAYETSSALPPS------------------------------EVSVL 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 966 FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNI 1045
Cdd:cd18604 44 YYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1046 LLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYR 1125
Cdd:cd18604 124 LLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEER 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1126 FEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQqglANPGLVGLSLSYALSLTGLLSGLVSSF 1205
Cdd:cd18604 204 FIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSFATAALLVYGPG---IDAGLAGFSLSFALGFSSAILWLVRSY 280
|
330
....*....|....*..
gi 2217363546 1206 TQTEAMLVSVERLEEYT 1222
Cdd:cd18604 281 NELELDMNSVERIQEYL 297
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
598-800 |
8.92e-53 |
|
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: 8.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 598 LELHGALFSWDPVGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV-------------AVRGLSK 664
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNI--NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 665 G-FGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQE 743
Cdd:cd03290 79 YsVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217363546 744 KELYLLDDPLAAVDADVANHLLHRCILGMLSYTTR--LLCTHRTEYLERADAVLLMEAG 800
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRtlVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
885-1222 |
4.24e-52 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 185.89 E-value: 4.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 885 ALAILFSLLLMQATRNAADWWLSHWisqlkaenssQEAQPSTSPASMGLFSPQLLlfspgnlyipvfplpkaapngSSDI 964
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADW----------TEANHDVASVVFNITSSSLE---------------------DDEV 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 965 RFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILN 1044
Cdd:cd18602 50 SYYISVYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1045 ILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATY 1124
Cdd:cd18602 130 RLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1125 RFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYALSLTGLLSGLVSS 1204
Cdd:cd18602 210 RFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRN 289
|
330
....*....|....*...
gi 2217363546 1205 FTQTEAMLVSVERLEEYT 1222
Cdd:cd18602 290 LADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
886-1222 |
8.61e-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: 184.22 E-value: 8.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 886 LAILFSLLLMQATRNAADWWLSHWISQLkaenssqeaqpstspasmglfspqlllfspgnlyipvFPLPKAapngssdir 965
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTEDF-------------------------------------FGLSQG--------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 966 FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNI 1045
Cdd:cd18606 36 FYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRM 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1046 LLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYR 1125
Cdd:cd18606 116 FLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1126 FEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVqhQQGLANPGLVGLSLSYALSLTGLLSGLVSSF 1205
Cdd:cd18606 196 FIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVT--RRFSISPSSTGLVLSYVLQITQVLSWLVRQF 273
|
330
....*....|....*..
gi 2217363546 1206 TQTEAMLVSVERLEEYT 1222
Cdd:cd18606 274 AEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
881-1222 |
2.24e-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: 175.06 E-value: 2.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 881 GQGLALAILFSLLLMQATRNAADWWLSHWISQLKAENSSQEAQPSTSPASMglfspqlllfspgnlyipvfplpkaapNG 960
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNI---------------------------SD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 961 SSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLP 1040
Cdd:cd18599 54 NPDLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1041 FILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRAT 1120
Cdd:cd18599 134 FTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1121 GATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHqqGLANPGLVGLSLSYALSLTGLLSG 1200
Cdd:cd18599 214 NKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITALLVVLLK--GSISPAFAGLALSYALQLSGLFQF 291
|
330 340
....*....|....*....|..
gi 2217363546 1201 LVSSFTQTEAMLVSVERLEEYT 1222
Cdd:cd18599 292 TVRLASETEARFTSVERILEYI 313
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
426-812 |
1.14e-47 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 182.73 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 426 GLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCG--------WEQALGARVEAcrarelgRLR 497
Cdd:COG2274 301 VLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGaesrfrrrWENLLAKYLNA-------RFK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 498 VIKYLDAAcvYLWA-ALPVVISIVIFI--TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLF 574
Cdd:COG2274 374 LRRLSNLL--STLSgLLQQLATVALLWlgAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDI 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 575 LDLPNHNPQAYYSPDPPAEPSTVlELHGALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLR 654
Cdd:COG2274 452 LDLPPEREEGRSKLSLPRLKGDI-ELENVSFRYPGDSPPVLDNIS-LTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 655 GHVAV----------RGLSKGFGLATQEPWIQFATIRDNILFGKTF--DAQLYkEVLEACALNDDLSILPAGDQTEVGEK 722
Cdd:COG2274 530 GRILIdgidlrqidpASLRRQIGVVLQDVFLFSGTIRENITLGDPDatDEEII-EAARLAGLHDFIEALPMGYDTVVGEG 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 723 GVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRL 802
Cdd:COG2274 609 GSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
410
....*....|
gi 2217363546 803 IRAGPPSEIL 812
Cdd:COG2274 688 VEDGTHEELL 697
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
316-812 |
1.88e-47 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 179.57 E-value: 1.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 316 GQEPLSHGLLYALGLAGGAVLGAVL---QNQYGYEV-YKVTLQARGAVLNilycKALQLGP---SRPPTGEALNLLGTDS 388
Cdd:COG4988 50 GGAPLSALLPLLGLLLAVLLLRALLawlRERAAFRAaARVKRRLRRRLLE----KLLALGPawlRGKSTGELATLLTEGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 389 ERLLNFAGSFheawgLP-------LQLAITLYLLYQQVGVAFVggLILALLLVPVNKVIATRIMASNQEmlQHKDARVKL 461
Cdd:COG4988 126 EALDGYFARY-----LPqlflaalVPLLILVAVFPLDWLSGLI--LLVTAPLIPLFMILVGKGAAKASR--RQWRALARL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 462 ---VTELLSGIRVIKFCGWEQALGARV----EACRARELGRLRV----IKYLDAAcVYLWAALpvvisIVIFITYVLMGH 530
Cdd:COG4988 197 sghFLDRLRGLTTLKLFGRAKAEAERIaeasEDFRKRTMKVLRVaflsSAVLEFF-ASLSIAL-----VAVYIGFRLLGG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 531 QLTATKVFTALALVRMLILPLNNFpwvinGL-----LEAKVSLDRIQLFLDLPNHNPQAYYSPDPPAEPSTvLELHGALF 605
Cdd:COG4988 271 SLTLFAALFVLLLAPEFFLPLRDL-----GSfyharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPS-IELEDVSF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 606 SWDPVGTSLEtFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWI 675
Cdd:COG4988 345 SYPGGRPALD-GLS-LTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpasWRRQIAWVPQNPYL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 676 QFATIRDNILFGKTF--DAQLyKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:COG4988 423 FAGTIRENLRLGRPDasDEEL-EAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217363546 754 AAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG4988 502 AHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
289-571 |
2.63e-46 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 168.95 E-value: 2.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 289 GLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALG--------------LAGGAVLGAVLQNQYGYEVYKVT-- 352
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVsyvtveeffsngyvLAVILFLALLLQATFSQASYHIVir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 353 --LQARGAVLNILYCKALQLGPSRPP-----TGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVG 425
Cdd:cd18591 83 egIRLKTALQAMIYEKALRLSSWNLSsgsmtIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 426 GLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAA 505
Cdd:cd18591 163 GAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217363546 506 CVYLWAALPVVISIVIFITYVLMGHQ-LTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18591 243 MTFLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
312-572 |
1.14e-45 |
|
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: 166.65 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 312 FLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKALQLGP---SRPPTGEALNLLGTDS 388
Cdd:cd18594 27 FVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSsalSKITTGHIVNLLSNDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 389 ERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSG 468
Cdd:cd18594 107 QKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 469 IRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITYVLMGHQLTATKVFTALAL---VR 545
Cdd:cd18594 187 MRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTARKVFTVISLlnaLR 266
|
250 260
....*....|....*....|....*..
gi 2217363546 546 MLIlpLNNFPWVINGLLEAKVSLDRIQ 572
Cdd:cd18594 267 MTI--TRFFPESIQTLSESRVSLKRIQ 291
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
377-812 |
1.76e-45 |
|
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: 173.80 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 377 TGEALNLLGTDSERLLNF-------AGSfheAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVnkvIATRIM-ASN 448
Cdd:COG4987 111 SGDLLNRLVADVDALDNLylrvllpLLV---ALLVILAAVAFLAFFSPALALVLALGLLLAGLLLPL---LAARLGrRAG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 449 QEMLQHKDARVKLVTELLSGIRVIKFCG-WEQALGA--RVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITY 525
Cdd:COG4987 185 RRLAAARAALRARLTDLLQGAAELAAYGaLDRALARldAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 526 VLMGHQ---LTATKVFTALALVRMLiLPLnnfPWVINGLLEAKVSLDRIQlflDLPNHNPQAYYSPDPPAEPSTV-LELH 601
Cdd:COG4987 265 VAAGALsgpLLALLVLAALALFEAL-APL---PAAAQHLGRVRAAARRLN---ELLDAPPAVTEPAEPAPAPGGPsLELE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 602 GALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQ 671
Cdd:COG4987 338 DVSFRYPGAGRPVLDGLS-LTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddLRRRIAVVPQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 672 EPWIQFATIRDNILFGK---TfDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYL 748
Cdd:COG4987 417 RPHLFDTTLRENLRLARpdaT-DEELW-AALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILL 494
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217363546 749 LDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG4987 495 LDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
621-811 |
3.84e-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: 3.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLskgFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLE 700
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR---ISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 701 ACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLL 780
Cdd:cd03291 135 ACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRIL 214
|
170 180 190
....*....|....*....|....*....|.
gi 2217363546 781 CTHRTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:cd03291 215 VTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
883-1222 |
2.42e-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: 157.87 E-value: 2.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 883 GLALAILFSLLlMQATRNAADWWLSHWisqlkaeNSSQEAQPSTSPASMGLFSpqlllfspGNLYIPVfplpkaapngsS 962
Cdd:cd18601 4 VFILLVLLNIA-AQVLYVLSDWWLSYW-------ANLEEKLNDTTDRVQGENS--------TNVDIED-----------L 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 963 DIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFI 1042
Cdd:cd18601 57 DRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1043 LNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGA 1122
Cdd:cd18601 137 FLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1123 TYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVqhqqgLA---NPGLVGLSLSYALSLTGLLS 1199
Cdd:cd18601 217 QERFQEEFDAHQDLHSEAWFLFLATSRWLAVRLDALCALFVTVVAFGSLF-----LAeslDAGLVGLSLSYALTLMGTFQ 291
|
330 340
....*....|....*....|...
gi 2217363546 1200 GLVSSFTQTEAMLVSVERLEEYT 1222
Cdd:cd18601 292 WCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
319-571 |
1.23e-40 |
|
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: 151.99 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 319 PLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKALQLGPS---RPPTGEALNLLGTDSERLLNFA 395
Cdd:cd18593 35 SLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAalgKTTVGQIVNLLSNDVNRFDQAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 396 GSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIAtRIMASN-QEMLQHKDARVKLVTELLSGIRVIKF 474
Cdd:cd18593 115 LFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG-KLFSKLrRKTAARTDKRIRIMNEIINGIRVIKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 475 CGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITYVLMGHQLTATKVFTALALVRMLILPLNN- 553
Cdd:cd18593 194 YAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILTAERVFVTMALYNAVRLTMTLf 273
|
250
....*....|....*...
gi 2217363546 554 FPWVINGLLEAKVSLDRI 571
Cdd:cd18593 274 FPFAIQFGSELSVSIRRI 291
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
290-571 |
5.60e-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: 135.38 E-value: 5.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 290 LLKLVGTMLGFSGPLLL-SLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKAL 368
Cdd:cd18592 4 LLLLISLIFGFIGPTILiRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 369 QL-GPSRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQL----AITLYLLyqqvG-VAFVGGLILaLLLVPVNKVIAT 442
Cdd:cd18592 84 RLrSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLilgiVYSTYLL----GpWALLGMLVF-LLFYPLQAFIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 443 RIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIF 522
Cdd:cd18592 159 LTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTF 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2217363546 523 ITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18592 239 LAHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
598-806 |
7.17e-35 |
|
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: 133.10 E-value: 7.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 598 LELHGALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFG 667
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVS-LTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 668 LATQEPWIQFATIRDNILFGKTF-DAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKEL 746
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 747 YLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 806
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
323-797 |
1.65e-33 |
|
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: 137.03 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 323 GLLYALGLAGGAVLG-AVLQNQYGYEVYKVTLQARGAVLNILYCKALQLGP---SRPPTGEALNLLGTDSERLLNFAGSF 398
Cdd:TIGR02857 42 ELLPALGALALVLLLrALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPrwlQGRPSGELATLALEGVEALDGYFARY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 399 heawgLP-LQLA--ITLYLLYQQVGVAFVGGLIL--ALLLVPVNKV-IATRIMASNQEMLQHKDARVKLVTELLSGIRVI 472
Cdd:TIGR02857 122 -----LPqLVLAviVPLAILAAVFPQDWISGLILllTAPLIPIFMIlIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 473 KFCGWEQALGARV----EACRARELGRLRvIKYLDAACVYLWAALPVVIsIVIFITYVLMGHQLTATKVFTALALVRMLI 548
Cdd:TIGR02857 197 KLFGRAKAQAAAIrrssEEYRERTMRVLR-IAFLSSAVLELFATLSVAL-VAVYIGFRLLAGDLDLATGLFVLLLAPEFY 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 549 LPLNNFPWVINGLLEAKVSLDRIQLFLDlpnHNPQAYYSPDP-PAEPSTVLELHGALFSW---DPVGTSLEtfishLEVK 624
Cdd:TIGR02857 275 LPLRQLGAQYHARADGVAAAEALFAVLD---AAPRPLAGKAPvTAAPASSLEFSGVSVAYpgrRPALRPVS-----FTVP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 625 KGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGKTF-DAQ 693
Cdd:TIGR02857 347 PGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadsWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 694 LYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGML 773
Cdd:TIGR02857 427 EIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA-LRALA 505
|
490 500
....*....|....*....|....
gi 2217363546 774 SYTTRLLCTHRTEYLERADAVLLM 797
Cdd:TIGR02857 506 QGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
621-801 |
1.20e-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: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILfgktf 690
Cdd:cd03228 23 LTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldlesLRKNIAYVPQDPFLFSGTIRENIL----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 691 daqlykevleacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCIL 770
Cdd:cd03228 98 ------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPE-TEALILEALR 140
|
170 180 190
....*....|....*....|....*....|.
gi 2217363546 771 GMLSYTTRLLCTHRTEYLERADAVLLMEAGR 801
Cdd:cd03228 141 ALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
621-812 |
5.08e-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: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAI-------AGELHrLRGH----VAVRGLSKGFGLATQEPWIQFATIRDNILFGKt 689
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEIL-LDGVdirdLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 690 FDAQLyKEVLEAC--ALNDDLSI-LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD---VANH 763
Cdd:cd03249 102 PDATD-EEVEEAAkkANIHDFIMsLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEsekLVQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217363546 764 LLHRCILGMlsytTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03249 181 ALDRAMKGR----TTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
355-784 |
6.84e-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: 122.85 E-value: 6.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 355 ARGAVLNILYCKALqLGPSRPPTGEALNLLGTDSERLLNFagsfHEAWGLPLQLAITLYL--------LYQQVGVAFVGG 426
Cdd:TIGR02868 88 LRVRVYERLARQAL-AGRRRLRRGDLLGRLGADVDALQDL----YVRVIVPAGVALVVGAaavaaiavLSVPAALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 427 LILALLLVPVNKVIATRimASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEAcRARELGRLR----VIKYL 502
Cdd:TIGR02868 163 LLLAGFVAPLVSLRAAR--AAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEE-ADRELTRAErraaAATAL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 503 DAACVYLWAALPVVISIVIFITYVlMGHQLT----ATKVFTALALVRmlilPLNNFPWVINGLLEAKVSLDRIqlfLDLP 578
Cdd:TIGR02868 240 GAALTLLAAGLAVLGALWAGGPAV-ADGRLApvtlAVLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERI---VEVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 579 NHNPQAYYSPDPPAEPSTV----LELHGALFSWDPvGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLR 654
Cdd:TIGR02868 312 DAAGPVAEGSAPAAGAVGLgkptLELRDLSAGYPG-APPVLDGVS-LDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 655 GHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGK--TFDAQLYkEVLEACALNDDLSILPAGDQTEVGEK 722
Cdd:TIGR02868 390 GEVTLDGvpvssldqdeVRRRVSVCAQDAHLFDTTVRENLRLARpdATDEELW-AALERVGLADWLRALPDGLDTVLGEG 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217363546 723 GVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHR 784
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHH 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
620-812 |
8.35e-28 |
|
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: 8.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGK- 688
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrksLRSMIGVVLQDTFLFSGTIMENIRLGRp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 689 TFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANhLLHRC 768
Cdd:cd03254 103 NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK-LIQEA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217363546 769 ILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03254 182 LEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
621-812 |
2.86e-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: 108.47 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAI-------AGELhRLRGH----VAVRGLSKGFGLATQEPWIQFATIRDNILFGKt 689
Cdd:cd03251 23 LDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRI-LIDGHdvrdYTLASLRRQIGLVSQDVFLFNDTVAENIAYGR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 690 FDAQLyKEVLEA---CALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDaDVANHLLH 766
Cdd:cd03251 101 PGATR-EEVEEAaraANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD-TESERLVQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217363546 767 RCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03251 179 AALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
598-812 |
5.14e-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: 5.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 598 LELHGALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFG 667
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNIS-LRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 668 LATQEPWIQFATIRDNILFGKTfdAQLYKEVLEACAL---NDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEK 744
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADP--GMSMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 745 ELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03252 158 RILIFDEATSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
620-806 |
6.30e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 114.17 E-value: 6.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAG-------------ELHRL-----RGHVAVRGlskgfglatQEPWIQFATIR 681
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingiELRELdpeswRKHLSWVG---------QNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 682 DNILFGKTF--DAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:PRK11174 441 DNVLLGNPDasDEQLQ-QALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217363546 760 VANHLLHRCILGMLSYTTrLLCTHRTEYLERADAVLLMEAGRLIRAG 806
Cdd:PRK11174 520 SEQLVMQALNAASRRQTT-LMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
621-808 |
2.40e-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: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNI-LFGKT 689
Cdd:cd03244 25 FSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdLRSRISIIPQDPVLFSGTIRSNLdPFGEY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 690 FDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLLHRCI 769
Cdd:cd03244 105 SDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETD-ALIQKTI 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217363546 770 LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPP 808
Cdd:cd03244 183 REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
621-802 |
1.72e-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: 97.54 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFG-KT 689
Cdd:cd03248 35 FTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkyLHSKVSLVGQEPVLFARSLQDNIAYGlQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 690 FDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCI 769
Cdd:cd03248 115 CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQVQQAL 193
|
170 180 190
....*....|....*....|....*....|...
gi 2217363546 770 LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRL 802
Cdd:cd03248 194 YDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
621-804 |
4.48e-22 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 96.00 E-value: 4.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV-----AVRGLSKGFGLATQE----PWiqfATIRDNILFGKTF- 690
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgePVTGPGPDRGYVFQQdallPW---LTVLDNVALGLELq 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 691 ---DAQLYKEVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 761
Cdd:cd03293 102 gvpKAEARERAEELLEL--------------VGLSGFenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217363546 762 NHlLHRCILGMLSYT--TRLLCTHRTE---YLerADAVLLMEA--GRLIR 804
Cdd:cd03293 168 EQ-LQEELLDIWRETgkTVLLVTHDIDeavFL--ADRVVVLSArpGRIVA 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
620-754 |
2.31e-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: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQ-FATIRDNILFG- 687
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderksLRKEIGYVFQDPQLFpRLTVRENLRLGl 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217363546 688 -------KTFDAQLYkEVLEACALNDDLSilpagdqTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:pfam00005 85 llkglskREKDARAE-EALEKLGLGDLAD-------RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
621-811 |
3.07e-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: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGfGLATQEPWIQFA----------TIRDNILFG--- 687
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT-DVPVQERNVGFVfqhyalfrhmTVFDNVAFGlrv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 --------KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:cd03296 102 kprserppEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217363546 760 VANHL------LHRCIlgmlsYTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:cd03296 171 VRKELrrwlrrLHDEL-----HVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
620-821 |
3.10e-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: 99.44 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEpwIQF--ATIRDNI-LF 686
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreeLGRHIGYLPQD--VELfdGTIAENIaRF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 GKTfDAQlykEVLEACALND--DLsI--LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN 762
Cdd:COG4618 430 GDA-DPE---KVVAAAKLAGvhEM-IlrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEA 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 763 HLLhRCILGM-LSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPKA 821
Cdd:COG4618 505 ALA-AAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
620-807 |
3.79e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 99.40 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAI-------AGE------------LHRLRGHVAVrglskgfglATQEPWIQFATI 680
Cdd:PRK10789 335 NFTLKPGQMLGICGPTGSGKSTLLSLIqrhfdvsEGDirfhdipltklqLDSWRSRLAV---------VSQTPFLFSDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 681 RDNILFGKTfDA--QLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:PRK10789 406 ANNIALGRP-DAtqQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 759 DVANHLLHRcilgmLS----YTTRLLCTHRTEYLERADAVLLMEAGRLIRAGP 807
Cdd:PRK10789 485 RTEHQILHN-----LRqwgeGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
605-812 |
4.62e-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: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 605 FSWDPVGTSLETfIShLEVKKGMLVGIVGKVGCGKSSLLAAiageLHRL----RGHVAVRG----------LSKGFGLAT 670
Cdd:cd03253 8 FAYDPGRPVLKD-VS-FTIPAGKKVAIVGPSGSGKSTILRL----LFRFydvsSGSILIDGqdirevtldsLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 671 QEPWIQFATIRDNILFGK--TFDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYL 748
Cdd:cd03253 82 QDTVLFNDTIGYNIRYGRpdATDEEVI-EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217363546 749 LDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03253 161 LDEATSALDT-HTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
428-811 |
4.98e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.41 E-value: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 428 ILALLLVP----VNKVIATRIMASNQEmLQHKDARV-KLVTELLSGIRVIKFCGWEQalgarVEACRARE-------LGR 495
Cdd:TIGR00958 305 MVTLINLPlvflAEKVFGKRYQLLSEE-LQEAVAKAnQVAEEALSGMRTVRSFAAEE-----GEASRFKEaleetlqLNK 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 496 LRVIKYLdaacVYLWAAlpVVISIVIFITYVLMGHQLTATKVFTALALVRMLILP------LNNFPWVINGLLEAKVSLD 569
Cdd:TIGR00958 379 RKALAYA----GYLWTT--SVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQeqlgeaVRVLSYVYSGMMQAVGASE 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 570 RIQLFLDL-PNHNPQAYYSPDPPaepSTVLELHGALFSW-----DPVGTSLeTFishlEVKKGMLVGIVGKVGCGKSSLL 643
Cdd:TIGR00958 453 KVFEYLDRkPNIPLTGTLAPLNL---EGLIEFQDVSFSYpnrpdVPVLKGL-TF----TLHPGEVVALVGPSGSGKSTVA 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 644 AAI-------AGEL------------HRLRGHVAVRGlskgfglatQEPWIQFATIRDNILFGKTF--DAQLYKEVLEAC 702
Cdd:TIGR00958 525 ALLqnlyqptGGQVlldgvplvqydhHYLHRQVALVG---------QEPVLFSGSVRENIAYGLTDtpDEEIMAAAKAAN 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 703 AlNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVaNHLLH--RCILGMlsytTRLL 780
Cdd:TIGR00958 596 A-HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-EQLLQesRSRASR----TVLL 669
|
410 420 430
....*....|....*....|....*....|.
gi 2217363546 781 CTHRTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:TIGR00958 670 IAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
621-806 |
6.50e-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: 91.22 E-value: 6.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG---------LSKGFGLATQEPWIQFATIRDNIlfgktfd 691
Cdd:cd03247 23 LELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekaLSSLISVLNQRPYLFDTTLRNNL------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 692 aqlykevleacalnddlsilpagdqtevgekGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhRCILG 771
Cdd:cd03247 96 -------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL-SLIFE 143
|
170 180 190
....*....|....*....|....*....|....*
gi 2217363546 772 MLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 806
Cdd:cd03247 144 VLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
621-806 |
1.30e-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: 91.43 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------KGFGLATQE----PWIqfaTIRDNILFG- 687
Cdd:cd03259 21 LTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperRNIGMVFQDyalfPHL---TVAENIAFGl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 ---KTFDAQLYKEVLEACALNDDLSILpagdqtevGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL 764
Cdd:cd03259 98 klrGVPKAEIRARVRELLELVGLEGLL--------NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217363546 765 LH--RCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 806
Cdd:cd03259 170 REelKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
621-801 |
1.62e-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: 91.37 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFG- 687
Cdd:cd03225 22 LTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkeLRRKVGLVFQNPDDQFfgPTVEEEVAFGl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 ------KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD---- 757
Cdd:cd03225 102 enlglpEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDpagr 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217363546 758 ADVANHLLHRCILGMlsytTRLLCTHRTEYLER-ADAVLLMEAGR 801
Cdd:cd03225 171 RELLELLKKLKAEGK----TIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
621-804 |
3.69e-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: 3.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV-----AVRGLSKGFGLATQE----PWiqfATIRDNILFG---- 687
Cdd:COG1116 32 LTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVlvdgkPVTGPGPDRGVVFQEpallPW---LTVLDNVALGlelr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 ---KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHl 764
Cdd:COG1116 109 gvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRER- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217363546 765 LHRCILGMLSYT--TRLLCTHRTE---YLerADAVLLMEA--GRLIR 804
Cdd:COG1116 177 LQDELLRLWQETgkTVLFVTHDVDeavFL--ADRVVVLSArpGRIVE 221
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
962-1218 |
5.07e-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: 92.56 E-value: 5.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 962 SDIRFYLTVYATIAGVNSLCTL--LRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSL 1039
Cdd:cd18600 65 TFTSSYYVFYIYVGVADSLLAMgfFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1040 PFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRA 1119
Cdd:cd18600 145 PLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1120 TGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlanPGLVGLSLSYALSLTGLLS 1199
Cdd:cd18600 225 FGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDG---EGRVGIILTLAMNIMSTLQ 301
|
250
....*....|....*....
gi 2217363546 1200 GLVSSFTQTEAMLVSVERL 1218
Cdd:cd18600 302 WAVNTSIDVDSLMRSVSRI 320
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
510-850 |
7.25e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.41 E-value: 7.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 510 WAALPVV-------ISIV-IFI--TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVsldRIQLFLDLPN 579
Cdd:PRK13657 238 WWALASVlnraastITMLaILVlgAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAP---KLEEFFEVED 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 580 HNPQAYYSPD--PPAEPSTVLELHGALFSWDPVGTSLE--TFishlEVKKGMLVGIVGKVGCGKSSLLAAiageLHRL-- 653
Cdd:PRK13657 315 AVPDVRDPPGaiDLGRVKGAVEFDDVSFSYDNSRQGVEdvSF----EAKPGQTVAIVGPTGAGKSTLINL----LQRVfd 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 654 --RGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGKT--FDAQLYkEVLEACALNDDLSILPAGDQTEV 719
Cdd:PRK13657 387 pqSGRILIDGtdirtvtrasLRRNIAVVFQDAGLFNRSIEDNIRVGRPdaTDEEMR-AAAERAQAHDFIERKPDGYDTVV 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 720 GEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHlLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEA 799
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAK-VKAALDELMKGRTTFIIAHRLSTVRNADRILVFDN 544
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2217363546 800 GRLIRAGPPSEILplvqavpkawAENGQESDSATAQSVQNPEKTKEGLEEE 850
Cdd:PRK13657 545 GRVVESGSFDELV----------ARGGRFAALLRAQGMLQEDERRKQPAAE 585
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
621-812 |
2.04e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 91.36 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH------RLRGHVAVRGLS---KGFGLATQepwiQFA-----TIRDNILF 686
Cdd:COG1118 23 LEIASGELVALLGPSGSGKTTLLRIIAGLETpdsgriVLNGRDLFTNLPpreRRVGFVFQ----HYAlfphmTVAENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 GktfdaqlykevleacalnddLSILPAGDQtEVGEKgVT------------------LSGGQRARIALARAVYQEKELYL 748
Cdd:COG1118 99 G--------------------LRVRPPSKA-EIRAR-VEellelvqlegladrypsqLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217363546 749 LDDPLAAVDADVANHL------LHRCILGmlsytTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1118 157 LDEPFGALDAKVRKELrrwlrrLHDELGG-----TTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
621-812 |
3.11e-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: 88.16 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFG- 687
Cdd:COG1122 22 LSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlreLRRKVGLVFQNPDDQLfaPTVEEDVAFGp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 -------KTFDAQLyKEVLEACALND--DLSILpagdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:COG1122 102 enlglprEEIRERV-EEALELVGLEHlaDRPPH-------------ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217363546 759 DVANHLLHrcILGML--SYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1122 168 RGRRELLE--LLKRLnkEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
621-802 |
6.41e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 86.41 E-value: 6.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS----------KGFGLATQEPWIQFATIRDNILF---- 686
Cdd:COG4619 21 LTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrRQVAYVPQEPALWGGTVRDNLPFpfql 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 -GKTFDAQLYKEVLEACALNDDlsILpagdQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLL 765
Cdd:COG4619 101 rERKFDRERALELLERLGLPPD--IL----DKPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT-RRV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217363546 766 HRCILGMLSY--TTRLLCTHRTEYLER-ADAVLLMEAGRL 802
Cdd:COG4619 170 EELLREYLAEegRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
621-812 |
1.09e-18 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 87.02 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFA-TIRDNILFGKT 689
Cdd:COG1120 22 LSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrreLARRIAYVPQEPPAPFGlTVRELVALGRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 690 --------FDAQLYKEVLEACAlnddlsilpagdQTEVG---EKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:COG1120 102 phlglfgrPSAEDREAVEEALE------------RTGLEhlaDRPVdELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217363546 758 advANHLLHrcILGMLSYTTR------LLCTH------RTeylerADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1120 170 ---LAHQLE--VLELLRRLARergrtvVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
620-806 |
1.21e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 85.81 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVK---KGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL-----SKGFGLATQEPWIQFA----------TIR 681
Cdd:cd03297 14 TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVfqqyalfphlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 682 DNILFGKTF-----DAQLYKEVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:cd03297 94 ENLAFGLKRkrnreDRISVDELLDLLGL------------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217363546 756 VDADVANHLLH--RCILGMLSYTTrLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:cd03297 162 LDRALRLQLLPelKQIKKNLNIPV-IFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
621-812 |
1.24e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 86.27 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS---------KGFGLATQEPWI-QFATIRDNILF---- 686
Cdd:COG1131 21 LTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvardpaevrRRIGYVPQEPALyPDLTVRENLRFfarl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 ---GKTFDAQLYKEVLEACALNDDLsilpagdqtevGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANH 763
Cdd:COG1131 101 yglPRKEARERIDELLELFGLTDAA-----------DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP-EARR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217363546 764 LLHRCILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1131 169 ELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
622-808 |
1.79e-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: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 622 EVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNI-LFGKTF 690
Cdd:cd03369 30 KVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledLRSSLTIIPQDPTLFSGTIRSNLdPFDEYS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 691 DAQLYKevleacALnddlsilpagdqtEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCIL 770
Cdd:cd03369 110 DEEIYG------AL-------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA-TDALIQKTIR 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217363546 771 GMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPP 808
Cdd:cd03369 170 EEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
620-811 |
1.83e-18 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 85.70 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAG-----ELHRLRGHVAVRG------------LSKGFGLATQEPWIQFATIRD 682
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGkdiydldvdvleLRRRVGMVFQKPNPFPGSIYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 683 NILFG--------KTFDAQLYKEVLEACALNDDLSilpagDQTevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:cd03260 100 NVAYGlrlhgiklKEELDERVEEALRKAALWDEVK-----DRL----HALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 755 AVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:cd03260 171 ALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
621-801 |
2.08e-18 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 83.45 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFglatqepwIQFATIRDNIlfgktfdaqlykevle 700
Cdd:cd00267 20 LTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--------LPLEELRRRI---------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 701 acalnddlSILPagdQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLLHRCILGML-SYTTRL 779
Cdd:cd00267 76 --------GYVP---Q---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAeEGRTVI 134
|
170 180
....*....|....*....|...
gi 2217363546 780 LCTHRTEYLERA-DAVLLMEAGR 801
Cdd:cd00267 135 IVTHDPELAELAaDRVIVLKDGK 157
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
567-812 |
2.77e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.19 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 567 SLDRIQLFLDLPNHNPQAYYSPDPPAepstvlelhgalfSWdPVGTSLETFISHLEVKKGM---------------LVGI 631
Cdd:PLN03232 1202 SVERVGNYIDLPSEATAIIENNRPVS-------------GW-PSRGSIKFEDVHLRYRPGLppvlhglsffvspseKVGV 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 632 VGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYkEVLE 700
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdLRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDADLW-EALE 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 701 ACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVaNHLLHRCILGMLSYTTRLL 780
Cdd:PLN03232 1347 RAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-DSLIQRTIREEFKSCTMLV 1425
|
250 260 270
....*....|....*....|....*....|..
gi 2217363546 781 CTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PLN03232 1426 IAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
620-812 |
3.13e-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: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGF---------GLATQEPWI-QFATIRDNILFgkt 689
Cdd:COG4555 21 SFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKeprearrqiGVLPDERGLyDRLTVRENIRY--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 690 FdAQLYKEVLEACALNDDlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRC 768
Cdd:COG4555 98 F-AELYGLFDEELKKRIE-ELIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM-ARRLLREI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217363546 769 ILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG4555 175 LRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
621-816 |
4.67e-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: 4.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------------LSKGFGLATQepwiQFA-----TIRD 682
Cdd:cd03261 21 LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrLRRRMGMLFQ----SGAlfdslTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 683 NILF--------GKTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:cd03261 97 NVAFplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217363546 755 AVD---ADVANHLLHRC--ILGMlsytTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL----PLVQ 816
Cdd:cd03261 166 GLDpiaSGVIDDLIRSLkkELGL----TSIMVTHDlDTAFAIADRIAVLYDGKIVAEGTPEELRasddPLVR 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
620-802 |
9.32e-18 |
|
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: 9.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILfgkt 689
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpneLGDHVGYLPQDDELFSGSIAENIL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 690 fdaqlykevleacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCI 769
Cdd:cd03246 98 -------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVE-GERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....
gi 2217363546 770 LGM-LSYTTRLLCTHRTEYLERADAVLLMEAGRL 802
Cdd:cd03246 140 AALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
621-837 |
1.52e-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: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGEL---HRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNIL 685
Cdd:COG1123 27 LTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGrdllelsealRGRRIGMVFQDPMTQLnpVTVGDQIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 686 FG----KTFDAQLYKEVLEACALnddlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 761
Cdd:COG1123 107 EAlenlGLSRAEARARVLELLEA--------VGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 762 NHLLHrcILGML---SYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEILPLVQ---AVPKAWAENGQESDSATA 834
Cdd:COG1123 179 AEILD--LLRELqreRGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQalaAVPRLGAARGRAAPAAAA 256
|
...
gi 2217363546 835 QSV 837
Cdd:COG1123 257 AEP 259
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
621-812 |
2.19e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 83.21 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfgLATQEPWI-----------QF-ATIRDNILFG- 687
Cdd:COG1121 27 LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP----PRRARRRIgyvpqraevdwDFpITVRDVVLMGr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 -------KTFDAQLYKEVLEACALnddLSILPAGDQTeVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADV 760
Cdd:COG1121 103 ygrrglfRRPSRADREAVDEALER---VGLEDLADRP-IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217363546 761 ANHLLHrcILGMLS--YTTRLLCTHRTEYLER-ADAVLLMeAGRLIRAGPPSEIL 812
Cdd:COG1121 175 EEALYE--LLRELRreGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVL 226
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
286-551 |
4.68e-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: 82.69 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 286 LALGLLKLVGTMLGFSGPLLLSLLVG-FLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILY 364
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDvLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 365 CKALQLGPS---RPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLL--YQQVGVAFVGgLILALLLVPVNKV 439
Cdd:pfam00664 82 KKILRQPMSffdTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVmfYYGWKLTLVL-LAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 440 IATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGR-LRVIKYLDAACVYLWAALPVVIS 518
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAgIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 2217363546 519 IVIFI-TYVLMGHQLTATKVFTALALVRMLILPL 551
Cdd:pfam00664 241 LALWFgAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
621-806 |
4.70e-17 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 81.43 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL-----SKGFGLATQEPWIQF---ATIRDNIL------- 685
Cdd:cd03235 20 FEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekeRKRIGYVPQRRSIDRdfpISVRDVVLmglyghk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 686 -FGKTFDAQLYKEVLEAcalnddlsiLPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVD----AD 759
Cdd:cd03235 100 gLFRRLSKADKAKVDEA---------LERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDpktqED 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217363546 760 VANHLLHRCILGMlsytTRLLCTH-RTEYLERADAVLLMeAGRLIRAG 806
Cdd:cd03235 171 IYELLRELRREGM----TILVVTHdLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
286-571 |
5.08e-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: 82.98 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 286 LALGLLkLVGTMLGFSGPLLLSLLVGFLEeGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYC 365
Cdd:cd07346 3 LALLLL-LLATALGLALPLLTKLLIDDVI-PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 366 KALQLGPS---RPPTGEALNLLGTDSERLLNFAGS-FHEAWGLPLQLAITL-YLLYQQVGVAFVGgLILALLLVPVNKVI 440
Cdd:cd07346 81 HLQRLSLSffdRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALvILFYLNWKLTLVA-LLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 441 ATRIMASNQEmLQHKDARV-KLVTELLSGIRVIKFCGWEQALGARVEAcRARELGRLRV-IKYLDAACVYLWAALPVVIS 518
Cdd:cd07346 160 RRRIRKASRE-VRESLAELsAFLQESLSGIRVVKAFAAEEREIERFRE-ANRDLRDANLrAARLSALFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2217363546 519 IVIFI--TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd07346 238 ALVLLygGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
621-802 |
5.41e-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: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlskgfglatQEPWIQFATIRDNILFgktfdaqlykeVLE 700
Cdd:cd03230 21 LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG---------KDIKKEPEEVKRRIGY-----------LPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 701 ACALNDDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS--YTTR 778
Cdd:cd03230 81 EPSLYENLT----------VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE--LLRELKkeGKTI 148
|
170 180
....*....|....*....|....*
gi 2217363546 779 LLCTHRTEYLER-ADAVLLMEAGRL 802
Cdd:cd03230 149 LLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
621-812 |
6.35e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.65 E-value: 6.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGK-- 688
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaaLRQAISVVSQRVHLFSATLRDNLLLAApn 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 689 TFDAQLyKEVLEACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhRC 768
Cdd:PRK11160 441 ASDEAL-IEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIL-EL 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217363546 769 ILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK11160 518 LAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
966-1221 |
1.24e-16 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 81.88 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 966 FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNI 1045
Cdd:cd18559 39 VYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1046 LLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYhVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYR 1125
Cdd:cd18559 119 WMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVP-VNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1126 FeEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQglaNPGLVGLSLSYALSLTGLLSGLVSSF 1205
Cdd:cd18559 198 F-IRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHS---LAGLVALKVFYSLALTTYLNWPLNMS 273
|
250
....*....|....*.
gi 2217363546 1206 TQTEAMLVSVERLEEY 1221
Cdd:cd18559 274 PEVITNIVAAEVSLER 289
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
621-811 |
3.29e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.68 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------KGFGLATQEpwiqFA-----TIRDNILFG 687
Cdd:COG3842 26 LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtglppekRNVGMVFQD----YAlfphlTVAENVAFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 ----KTFDAQLYKEVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:COG3842 102 lrmrGVPKAEIRARVAELLEL--------------VGLEGLadryphQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217363546 758 ADVANHL------LHRcILGmlsyTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:COG3842 168 AKLREEMreelrrLQR-ELG----ITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
567-813 |
3.56e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 84.40 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 567 SLDRIQLFLDLPNHNPQAYYS--PdPPAEPST--------VLELHGALfswDPVGTSLETFISHLEVkkgmlVGIVGKVG 636
Cdd:PLN03130 1205 AVERVGTYIDLPSEAPLVIENnrP-PPGWPSSgsikfedvVLRYRPEL---PPVLHGLSFEISPSEK-----VGIVGRTG 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 637 CGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYkEVLEACALN 705
Cdd:PLN03130 1276 AGKSSMLNALFRIVELERGRILIDGcdiskfglmdLRKVLGIIPQAPVLFSGTVRFNLdPFNEHNDADLW-ESLERAHLK 1354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 706 DDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRT 785
Cdd:PLN03130 1355 DVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR-TDALIQKTIREEFKSCTMLIIAHRL 1433
|
250 260
....*....|....*....|....*...
gi 2217363546 786 EYLERADAVLLMEAGRLIRAGPPSEILP 813
Cdd:PLN03130 1434 NTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
568-821 |
3.94e-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: 83.03 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 568 LDRIQLFLDLPNHNPQAYYSPDPPAEPSTVLELHGALFSWDPVGTslETF-----IShLEVKKGMLVGIVGKVGCGKSSL 642
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGK--GGVravddVS-LTLRRGETLGLVGESGSGKSTL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 643 LAAIAGELHRLRGHVAVRG-------------LSKGFGLATQEPWIQF---ATIRDNI-----LFGKTFDAQLYK---EV 698
Cdd:COG1123 308 ARLLLGLLRPTSGSILFDGkdltklsrrslreLRRRVQMVFQDPYSSLnprMTVGDIIaeplrLHGLLSRAERRErvaEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 699 LEACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD----ADVANHLLH-RCILGm 772
Cdd:COG1123 388 LERVGLPPDlADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDvsvqAQILNLLRDlQRELG- 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217363546 773 LSYttrLLCTH---RTEYLerADAVLLMEAGRLIRAGPPSEIL--P-------LVQAVPKA 821
Cdd:COG1123 456 LTY---LFISHdlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFanPqhpytraLLAAVPSL 511
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
620-806 |
4.57e-16 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 77.48 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVavrglskgfglatqepwiqfatirdnILFGKTFDAQLYKEVL 699
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI--------------------------LLDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 700 EACAlnddlsILP-AGDQTEVG---EKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS 774
Cdd:cd03214 73 RKIA------YVPqALELLGLAhlaDRPFnELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE--LLRRLA 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217363546 775 Y---TTRLLCTHrteYLERA----DAVLLMEAGRLIRAG 806
Cdd:cd03214 145 RergKTVVMVLH---DLNLAaryaDRVILLKDGRIVAQG 180
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
630-812 |
5.48e-16 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 80.92 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 630 GIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL-----SKGFGLAT---------QEPWIqFA--TIRDNILFG-----K 688
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsARGIFLPPhrrrigyvfQEARL-FPhlSVRGNLLYGrkrapR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 689 TFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrc 768
Cdd:COG4148 108 AERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217363546 769 ILGMLSYTTR---LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG4148 175 YLERLRDELDipiLYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
621-806 |
1.14e-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: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL--------SKGFGLATQepwiQFA-----TIRDNILFG 687
Cdd:cd03301 21 LDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkDRDIAMVFQ----NYAlyphmTVYDNIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 ----KTFDAQLYKEVLEACALnddLSIlpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH 763
Cdd:cd03301 97 lklrKVPKDEIDERVREVAEL---LQI-----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217363546 764 L------LHRcilgMLSYTTrLLCTH-RTEYLERADAVLLMEAGRLIRAG 806
Cdd:cd03301 169 MraelkrLQQ----RLGTTT-IYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
506-812 |
1.14e-15 |
|
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: 82.69 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 506 CVYLWAALPVVISivifityvlmGHQLTATKVFTALALVRMLILPLNnfpWVINGLLEAK---VSLDRIQLFLDLPNHNP 582
Cdd:TIGR00957 1201 CIVLFAALFAVIS----------RHSLSAGLVGLSVSYSLQVTFYLN---WLVRMSSEMEtniVAVERLKEYSETEKEAP 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 583 QAYYSPDPPAE--PSTVLELHGALFSWDPvgtSLETFISHLEV--KKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVA 658
Cdd:TIGR00957 1268 WQIQETAPPSGwpPRGRVEFRNYCLRYRE---DLDLVLRHINVtiHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 659 VRGLS-KGFGLAT---------QEPWIQFATIRDNI-LFGKTFDAQLYKeVLEACALNDDLSILPAGDQTEVGEKGVTLS 727
Cdd:TIGR00957 1345 IDGLNiAKIGLHDlrfkitiipQDPVLFSGSLRMNLdPFSQYSDEEVWW-ALELAHLKTFVSALPDKLDHECAEGGENLS 1423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 728 GGQRARIALARAVYQEKELYLLDDPLAAVDADVANhLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGP 807
Cdd:TIGR00957 1424 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDN-LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGA 1502
|
....*
gi 2217363546 808 PSEIL 812
Cdd:TIGR00957 1503 PSNLL 1507
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
621-801 |
1.69e-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: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLskgfGLATQEPWIQfaTIRDNIlfGKTF-DAQLY--KE 697
Cdd:cd03229 21 LNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE----DLTDLEDELP--PLRRRI--GMVFqDFALFphLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 698 VLEACALnddlsilpagdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL--LHRCILGMLSY 775
Cdd:cd03229 93 VLENIAL--------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVraLLKSLQAQLGI 152
|
170 180
....*....|....*....|....*..
gi 2217363546 776 TTrLLCTHRTEYLER-ADAVLLMEAGR 801
Cdd:cd03229 153 TV-VLVTHDLDEAARlADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
620-812 |
2.30e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 77.15 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGFGLAT--------QEPwiqFA------TIRDN 683
Cdd:COG1124 25 SLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpVTRRRRKAFrrrvqmvfQDP---YAslhprhTVDRI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 684 I-----LFGKTFDAQLYKEVLEACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:COG1124 102 LaeplrIHGLPDREERIAELLEQVGLPPSfLDRYPH-----------QLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217363546 758 ADVANHLLHrcILGML---SYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1124 171 VSVQAEILN--LLKDLreeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
621-811 |
5.02e-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: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGeLHRL-RGHVAV------------RGLSKGFglatQepwiQFA-----TIRD 682
Cdd:COG3839 24 LDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPtSGEILIggrdvtdlppkdRNIAMVF----Q----SYAlyphmTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 683 NILFG----KTFDAQLYKEVLEACALnddLSI------LPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDP 752
Cdd:COG3839 95 NIAFPlklrKVPKAEIDRRVREAAEL---LGLedlldrKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 753 LAAVDADVANHL------LHRcilgMLSYTTrLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:COG3839 161 LSNLDAKLRVEMraeikrLHR----RLGTTT-IYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
609-812 |
6.23e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.56 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 609 PVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKG-----------FGLATQEPWIQF 677
Cdd:PRK13644 12 PDGTPALENIN-LVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfsklqgirklVGIVFQNPETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 678 A--TIRDNILFGKTF----DAQLYKEVleacalndDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:PRK13644 91 VgrTVEEDLAFGPENlclpPIEIRKRV--------DRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217363546 752 PLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
621-811 |
8.49e-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: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------KGFGLATQepwiQFA-----TIRDNILFG 687
Cdd:cd03300 21 LDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpphkRPVNTVFQ----NYAlfphlTVFENIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 ----KTFDAQLYKEVLEACalndDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH 763
Cdd:cd03300 97 lrlkKLPKAEIKERVAEAL----DLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217363546 764 L------LHRcILGMlsytTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:cd03300 169 MqlelkrLQK-ELGI----TFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
620-802 |
9.43e-15 |
|
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: 9.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV-----AVRGLSKG----------------FGLatqepwIQFA 678
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtDISKLSEKelaafrrrhigfvfqsFNL------LPDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 679 TIRDNILFGKTF-------DAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:cd03255 98 TALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217363546 752 PLAAVDADVAnhllhRCILGML------SYTTRLLCTHRTEYLERADAVLLMEAGRL 802
Cdd:cd03255 167 PTGNLDSETG-----KEVMELLrelnkeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
621-812 |
1.09e-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: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------KGFGLATQEpWIQFA--TIRDNILFG--- 687
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDitnlppekRDISYVPQN-YALFPhmTVYKNIAYGlkk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 -KTFDAQLYKEVLEacaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdvanhLLH 766
Cdd:cd03299 99 rKVDKKEIERKVLE---IAEMLGIDHLLNR-----KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV-----RTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 767 RCILGMLSY------TTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03299 166 EKLREELKKirkefgVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
620-802 |
1.33e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.10 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLL-------AAIAGELhrLRGHVAVRGLSKGFGLATQE----PWiqfATIRDNI---L 685
Cdd:PRK11247 32 DLHIPAGQFVAVVGRSGCGKSTLLrllagleTPSAGEL--LAGTAPLAEAREDTRLMFQDarllPW---KKVIDNVglgL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 686 FGKTFDAQLykEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdvanhlL 765
Cdd:PRK11247 107 KGQWRDAAL--QALAAVGLADRANEWPA-----------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDA------L 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217363546 766 HRCILGMLSYT-------TRLLCTHR-TEYLERADAVLLMEAGRL 802
Cdd:PRK11247 168 TRIEMQDLIESlwqqhgfTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
510-798 |
1.86e-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: 78.80 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 510 WAALPVVISIVIF---ITYVLMG-HQLTATKVFTALALVrMLILplNNFPWVIN------GLLEakvSLDRIQLFLDLPN 579
Cdd:TIGR01271 1110 WFQMRIDIIFVFFfiaVTFIAIGtNQDGEGEVGIILTLA-MNIL--STLQWAVNssidvdGLMR---SVSRVFKFIDLPQ 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 580 HNPQAYYSPDPpAEPSTVL-----------------ELHGALFSWDPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSL 642
Cdd:TIGR01271 1184 EEPRPSGGGGK-YQLSTVLvienphaqkcwpsggqmDVQGLTAKYTEAGRAVLQDLS-FSVEGGQRVGLLGRTGSGKSTL 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 643 LAAIAgELHRLRGHVAVRGLS----------KGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYKeVLEACALNDDLSIL 711
Cdd:TIGR01271 1262 LSALL-RLLSTEGEIQIDGVSwnsvtlqtwrKAFGVIPQKVFIFSGTFRKNLdPYEQWSDEEIWK-VAEEVGLKSVIEQF 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 712 PAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLERA 791
Cdd:TIGR01271 1340 PDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLEC 1418
|
....*..
gi 2217363546 792 DAVLLME 798
Cdd:TIGR01271 1419 QQFLVIE 1425
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
621-806 |
1.91e-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: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH---RLRGHVAVRG--LSKG-----FGLATQ-EPWIQFATIRDNILFGKT 689
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGqpRKPDqfqkcVAYVRQdDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 690 F-----DAQLYKEVLEACALNDDLSILPAGDQTEVGekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL 764
Cdd:cd03234 108 LrlprkSSDAIRKKRVEDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217363546 765 LHrcILGMLSYTTRL-LCT-H--RTEYLERADAVLLMEAGRLIRAG 806
Cdd:cd03234 183 VS--TLSQLARRNRIvILTiHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
959-1191 |
2.86e-14 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 74.60 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 959 NGSSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDS 1038
Cdd:pfam00664 35 PETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1039 LPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLR 1118
Cdd:pfam00664 115 LGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 1119 ATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYA 1191
Cdd:pfam00664 195 AFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
621-803 |
2.92e-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: 73.31 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------------LSKGFGLATQEPwiqFA------TIR 681
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkiRRKEIQMVFQDP---MSslnprmTIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 682 DNI-----LFGKTFDAQLYKEV--LEACALNDDLSIL---PAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:cd03257 103 EQIaeplrIHGKLSKKEARKEAvlLLLVGVGLPEEVLnryPH-----------ELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 752 PLAAVDADVANHLLH--RCI---LGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLI 803
Cdd:cd03257 172 PTSALDVSVQAQILDllKKLqeeLGL----TLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
621-812 |
5.98e-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: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----LSKGFGLATQepwiqfATIRDNILFGktfdAQLY 695
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsalLELGAGFHPE------LTGRENIYLN----GRLL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 696 -------KEVLEACAlnddlsilpagDQTEVGE------KgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdvan 762
Cdd:COG1134 117 glsrkeiDEKFDEIV-----------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA---- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217363546 763 HLLHRCILGMLSY----TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1134 180 AFQKKCLARIRELresgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
620-812 |
6.29e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFA-TIRDNILFGK 688
Cdd:PRK09536 23 DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraASRRVASVPQDTSLSFEfDVRQVVEMGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 689 TFDAQLYKEVLEAcalnDDLSILPAGDQTEV---GEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDadvANHL 764
Cdd:PRK09536 103 TPHRSRFDTWTET----DRAAVERAMERTGVaqfADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLD---INHQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217363546 765 LHrcilgMLSYTTRLLCTHRTEY-----LERA----DAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK09536 176 VR-----TLELVRRLVDDGKTAVaaihdLDLAarycDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
621-811 |
9.07e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.35 E-value: 9.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGfGLATQEPWIQFA----------TIRDNILFGKTF 690
Cdd:PRK10851 23 LDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-RLHARDRKVGFVfqhyalfrhmTVFDNIAFGLTV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 691 --------DAQLYKEV---LEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:PRK10851 102 lprrerpnAAAIKAKVtqlLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217363546 760 VANHL------LHRcilgMLSYTTrLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK10851 171 VRKELrrwlrqLHE----ELKFTS-VFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
561-812 |
1.09e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.52 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 561 LLEAKVSLDRIQLFLDlpnhNPQAYYSPDPPAEPSTVLELHGALFSWDPvGTSLETFIShLEVKKGMLVGIVGKVGCGKS 640
Cdd:PRK10790 308 LQQAVVAGERVFELMD----GPRQQYGNDDRPLQSGRIDIDNVSFAYRD-DNLVLQNIN-LSVPSRGFVALVGHTGSGKS 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 641 SLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSI 710
Cdd:PRK10790 382 TLASLLMGYYPLTEGEIRLDGrplsslshsvLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARS 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 711 LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRTEYLER 790
Cdd:PRK10790 462 LPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG-TEQAIQQALAAVREHTTLVVIAHRLSTIVE 540
|
250 260
....*....|....*....|..
gi 2217363546 791 ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK10790 541 ADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
612-812 |
1.20e-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: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 612 TSLETFISHLE--VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFAT 679
Cdd:cd03288 31 NNLKPVLKHVKayIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtLRSRLSIILQDPILFSGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 680 IRDNI-LFGKTFDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:cd03288 111 IRFNLdPECKCTDDRLW-EALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217363546 759 DVANhLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03288 190 ATEN-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
621-812 |
1.32e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.06 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSllaaIAGELHR----------LRGH----VAVRGLSKGFGLATQEPWIQFATIRDNILF 686
Cdd:PRK11176 364 FKIPAGKTVALVGRSGSGKST----IANLLTRfydidegeilLDGHdlrdYTLASLRNQVALVSQNVHLFNDTIANNIAY 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 ---GKTFDAQLYKEVLEACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANH 763
Cdd:PRK11176 440 artEQYSREQIEEAARMAYAM-DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE-SER 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217363546 764 LLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK11176 518 AIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
621-811 |
1.50e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 73.72 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEP----WIQFA-----TIRDNILFGKTFD 691
Cdd:PRK11607 40 LTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPinmmFQSYAlfphmTVEQNIAFGLKQD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 692 AQLYKEVleACALNDDLSILPAgdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRC--I 769
Cdd:PRK11607 120 KLPKAEI--ASRVNEMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVvdI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217363546 770 LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11607 196 LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
659-824 |
1.51e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.84 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 659 VRGLSKGFGLATQEPWIQFATIRDNILFGKTfDAQLyKEVLEAC---ALNDDLSILPAGDQTEVGEKGVTLSGGQRARIA 735
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATR-EDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 736 LARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCT--HRTEYLERADAVLLM----EAGRLIRA-GPP 808
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITiaHRIASIKRSDKIVVFnnpdRTGSFVQAhGTH 1447
|
170
....*....|....*.
gi 2217363546 809 SEILPLVQAVPKAWAE 824
Cdd:PTZ00265 1448 EELLSVQDGVYKKYVK 1463
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
621-812 |
2.16e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.94 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfgLATQEPW-------IQ----FA--TIRDNILFG 687
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD----LTALPPAerpvsmlFQennlFPhlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 -------KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD--- 757
Cdd:COG3840 96 lrpglklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpal 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 758 ----ADVANHLLHRciLGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG3840 165 rqemLDLVDELCRE--RGL----TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
591-811 |
2.56e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 591 PAEPSTVLELHGALFSWDpvGTsleTFISH--LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGL 668
Cdd:PRK09452 8 PSSLSPLVELRGISKSFD--GK---EVISNldLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 669 ATQEP----WIQFA-----TIRDNILFG----KTFDAQLYKEVLEACALN--DDLSilpagdqtevGEKGVTLSGGQRAR 733
Cdd:PRK09452 83 AENRHvntvFQSYAlfphmTVFENVAFGlrmqKTPAAEITPRVMEALRMVqlEEFA----------QRKPHQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 734 IALARAVYQEKELYLLDDPLAAVDA----DVANHL--LHRcILGMlsytTRLLCTH-RTEYLERADAVLLMEAGRLIRAG 806
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYklrkQMQNELkaLQR-KLGI----TFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
....*
gi 2217363546 807 PPSEI 811
Cdd:PRK09452 228 TPREI 232
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
621-817 |
2.99e-13 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 70.78 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------------LSKGFGLATQEPwiqfA-----TIRD 682
Cdd:COG1127 26 LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyeLRRRIGMLFQGG----AlfdslTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 683 NILFG----KTFD----AQLYKEVLEACALNDDLSILPAgdqtevgEkgvtLSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:COG1127 102 NVAFPlrehTDLSeaeiRELVLEKLELVGLPGAADKMPS-------E----LSGGMRKRVALARALALDPEILLYDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 755 AVD---ADVANHLLHRC--ILGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL----PLVQA 817
Cdd:COG1127 171 GLDpitSAVIDELIRELrdELGL----TSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLasddPWVRQ 239
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
621-811 |
3.48e-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: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAG----------------------ELHRLRGHVAVrgLSKGFGLatqepwIQFA 678
Cdd:cd03256 22 LSINPGEFVALIGPSGAGKSTLLRCLNGlveptsgsvlidgtdinklkgkALRQLRRQIGM--IFQQFNL------IERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 679 TIRDNILFG--------KTFDAQLYK-EVLEACALNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLL 749
Cdd:cd03256 94 SVLENVLSGrlgrrstwRSLFGLFPKeEKQRALAALERVGLLDKAYQ-----RADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 750 DDPLAAVDADVAN---HLLHRciLGMLSYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEI 811
Cdd:cd03256 169 DEPVASLDPASSRqvmDLLKR--INREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
621-821 |
4.74e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.30 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV--------------RGLSKGFGLATQEPWIQF--ATIRDNI 684
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkeiKPVRKKVGVVFQFPESQLfeETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 685 LFGKTfDAQLYKEVLEACALnDDLSILpaGDQTEVGEKG-VTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH 763
Cdd:PRK13643 107 AFGPQ-NFGIPKEKAEKIAA-EKLEMV--GLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 764 LLHRCILGMLSYTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEILPLVQ-------AVPKA 821
Cdd:PRK13643 183 MMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDflkahelGVPKA 248
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
626-802 |
5.06e-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: 71.04 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 626 GMLVGIVGKVGCGKSSLLAAIAgELHRLRGHVAVRGLS----------KGFGLATQEPWIQFATIRDNI-LFGKTFDAQL 694
Cdd:cd03289 30 GQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSwnsvplqkwrKAFGVIPQKVFIFSGTFRKNLdPYGKWSDEEI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 695 YKeVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLS 774
Cdd:cd03289 109 WK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFA 186
|
170 180
....*....|....*....|....*...
gi 2217363546 775 YTTRLLCTHRTEYLERADAVLLMEAGRL 802
Cdd:cd03289 187 DCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
621-806 |
7.36e-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: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPwiQFATIRDNILFgktfdAQLYKEVLE 700
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENNLF-----AHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 701 ACALNDDLSiLPAGDQTEV----GEKGV---------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhR 767
Cdd:cd03298 92 GLGLSPGLK-LTAEDRQAIevalARVGLaglekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML-D 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217363546 768 CILGMLSYT--TRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:cd03298 170 LVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
621-806 |
9.04e-13 |
|
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: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------LSKGFGLAtqepwiqfATIRDNILFG------ 687
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvssllgLGGGFNPE--------LTGRENIYLNgrllgl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 -KTFDAQLYKEVLEACALNDDLSiLPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdvanHLLH 766
Cdd:cd03220 115 sRKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDA----AFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217363546 767 RC---ILGMLS-YTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:cd03220 180 KCqrrLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
620-759 |
9.32e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 68.66 E-value: 9.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELH---RLRGHVAVRG--------LSKGFGLATQEPWIqFA--TIRDNILF 686
Cdd:COG4136 21 SLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGrrltalpaEQRRIGILFQDDLL-FPhlSVGENLAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 G--KTFDAQLYKEVLEAcALnddlsilpagdqTEVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:COG4136 100 AlpPTIGRAQRRARVEQ-AL------------EEAGLAGFadrdpaTLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
.
gi 2217363546 759 D 759
Cdd:COG4136 167 A 167
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
621-796 |
2.62e-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: 67.12 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPWIQFA----------TIRDNILF---- 686
Cdd:COG4133 23 FTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLghadglkpelTVRENLRFwaal 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 -GKTFDAQLYKEVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLL 765
Cdd:COG4133 103 yGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-GVALL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217363546 766 HRCIL------GMLsyttrLLCTHRTEYLERADAVLL 796
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 ... |
620-812 |
2.70e-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: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAG--------------ELHRLRGHvAVRGLSKGFGLATQepwiQF-----ATI 680
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCINGlerptsgsvlvdgtDLTLLSGK-ELRKARRRIGMIFQ----HFnllssRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 681 RDNILF-------GKTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:cd03258 100 FENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 754 AAVDADVAnhllhRCILGMLSYTTR------LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03258 169 SALDPETT-----QSILALLRDINRelgltiVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
621-812 |
4.69e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 67.42 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH-----------RLRGHVAVRGLSKGFGLAT---QEPWIQFATIRDNILF 686
Cdd:COG1119 24 WTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygndvrlfgERRGGEDVWELRKRIGLVSpalQLRFPRDETVLDVVLS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 GKtFDA-QLYKEVLE-----ACALNDDLSILPAGDQTeVGekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDaDV 760
Cdd:COG1119 104 GF-FDSiGLYREPTDeqrerARELLELLGLAHLADRP-FG----TLSQGEQRRVLIARALVKDPELLILDEPTAGLD-LG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217363546 761 ANHLLHRCI--LGMLSYTTRLLCTHRTEYLERA-DAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1119 177 ARELLLALLdkLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
597-812 |
7.61e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 597 VLELHGALFSWDPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGF 666
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 667 GLATQEPWIQF--ATIRDNILFGKTFDAQLYKEVLEACalndDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEK 744
Cdd:PRK13642 84 GMVFQNPDNQFvgATVEDDVAFGMENQGIPREEMIKRV----DEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 745 ELYLLDDPLAAVDADVANHLLhRCILGMLS--YTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIM-RVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
621-804 |
1.09e-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: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSK-----------GFGLatqepwIQFAT 679
Cdd:COG1136 29 LSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslsereLARlrrrhigfvfqFFNL------LPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 680 IRDNILF-------GKTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDP 752
Cdd:COG1136 103 ALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217363546 753 LAAVDADVANH---LLHRCI--LGmlsyTTRLLCTHRTEYLERADAVLLMEAGRLIR 804
Cdd:COG1136 172 TGNLDSKTGEEvleLLRELNreLG----TTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
621-812 |
1.36e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.88 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAI-------AGEL-----HRLRGHVAVRGLSKGFGLATQepwiQF-----ATIRDN 683
Cdd:PRK09493 22 LNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLivdglKVNDPKVDERLIRQEAGMVFQ----QFylfphLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 684 ILFG-------KTFDA-QLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK09493 98 VMFGplrvrgaSKEEAeKQARELLAKVGLAERAHHYPS-----------ELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217363546 756 VDADvanhLLHRCILGMLSYT----TRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK09493 167 LDPE----LRHEVLKVMQDLAeegmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
621-810 |
1.88e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.07 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----LSKG--------FGLATQEpwiqFA-----TIRD 682
Cdd:COG2884 23 LEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrLKRReipylrrrIGVVFQD----FRllpdrTVYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 683 NILF-----GKTfDAQLYKEVLEACALnddlsilpagdqteVG--EKG----VTLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:COG2884 99 NVALplrvtGKS-RKEIRRRVREVLDL--------------VGlsDKAkalpHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217363546 752 PLAAVDADVAN---HLLHR-CILGmlsyTTRLLCTHRTEYLERADA-VLLMEAGRLIRAGPPSE 810
Cdd:COG2884 164 PTGNLDPETSWeimELLEEiNRRG----TTVLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
621-764 |
1.89e-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: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVR-GLSKGFgLAtQEPwiQF---ATIRDNILFGKTFDAQLYK 696
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGY-LP-QEP--PLdddLTVLDTVLDGDAELRALEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 697 EVLEACALNDDLSILP---AGDQTEVGEKGV--------------------------TLSGGQRARIALARAVYQEKELY 747
Cdd:COG0488 95 ELEELEAKLAEPDEDLerlAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEPDLL 174
|
170
....*....|....*..
gi 2217363546 748 LLDDPlaavdadvANHL 764
Cdd:COG0488 175 LLDEP--------TNHL 183
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
621-812 |
2.02e-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: 66.13 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL--------------SKGFGLATQepwiQFA-----TIR 681
Cdd:cd03294 45 LDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelrelrRKKISMVFQ----SFAllphrTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 682 DNILFG-------KTFDAQLYKEVLEACALNDDLSILPagDQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:cd03294 121 ENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYP--DE---------LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 755 AVD----ADVANHLLHrcILGMLSYTTrLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03294 190 ALDplirREMQDELLR--LQAELQKTI-VFITHDlDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
615-811 |
2.49e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.98 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 615 ETFIS---HLEVKKGMLVGIVGKVGCGKSSLLAAIAG-------ELhrLRGHVAVRGL---SKGFGLATQE----PWIQF 677
Cdd:PRK11000 15 DVVISkdiNLDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgDL--FIGEKRMNDVppaERGVGMVFQSyalyPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 678 AtirDNILFG----KTFDAQLYKEVLEACAlnddlsILPAGDQTEVGEKgvTLSGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:PRK11000 93 A---ENMSFGlklaGAKKEEINQRVNQVAE------VLQLAHLLDRKPK--ALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 754 AAVDADVANHL------LHRcilgmlsyttRLLC-----TH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11000 162 SNLDAALRVQMrieisrLHK----------RLGRtmiyvTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
621-811 |
2.75e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.84 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG------------LSKGFGLATQEPWIQF--ATIRDNILF 686
Cdd:PRK13637 28 IEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdIRKKVGLVFQYPEYQLfeETIEKDIAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 GKT----FDAQLYKEVLEACALnddlsilpAG-DQTEVGEKG-VTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA-- 758
Cdd:PRK13637 108 GPInlglSEEEIENRVKRAMNI--------VGlDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkg 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217363546 759 --DVANHL--LHRcilgmlSYT-TRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13637 180 rdEILNKIkeLHK------EYNmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
611-811 |
2.81e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.01 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 611 GTSLETF----IShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--------------LSKGFGLATQE 672
Cdd:PRK13641 15 GTPMEKKgldnIS-FELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkkLRKKVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 673 PWIQF--ATIRDNILFG-KTFDAQlykevlEACALNDDLS-ILPAGDQTEVGEKG-VTLSGGQRARIALARAVYQEKELY 747
Cdd:PRK13641 94 PEAQLfeNTVLKDVEFGpKNFGFS------EDEAKEKALKwLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217363546 748 LLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
621-812 |
4.13e-11 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 63.99 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----------LSKGFGLATQEPWIqFA--TIRDNILFG 687
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglppherARAGIGYVPEGRRI-FPelTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 ktfdAQLYKEVLEACALNDDLSILPAGDQTEvGEKGVTLSGGQRARIALARAVYQEKELYLLDDP---LA-AVDADVANH 763
Cdd:cd03224 100 ----AYARRRAKRKARLERVYELFPRLKERR-KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLApKIVEEIFEA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217363546 764 LLHRCILGMlsytTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03224 175 IRELRDEGV----TILLVEQNaRFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
621-797 |
4.55e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.41 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlSKGFGLATQ---EPWIQFATIRDNILFGK--------- 688
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-GARVAYVPQrseVPDSLPLTVRDLVAMGRwarrglwrr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 689 --TFDAQLYKEVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA----DVAN 762
Cdd:NF040873 92 ltRDDRAAVDDALERVGL-ADLAGRQLG----------ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAesreRIIA 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2217363546 763 HLLHRCILGmlsyTTRLLCTHRTEYLERADAVLLM 797
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 ... |
621-812 |
7.36e-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: 7.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV----------------RGLSKGF-GLATQE-PWIQFATIRD 682
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgRGRAKRYiGILHQEyDLYPHRTVLD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 683 NILfgKTFDAQLYKE--------VLEACALNDD--LSILPAGDQTevgekgvtLSGGQRARIALARAVYQEKELYLLDDP 752
Cdd:TIGR03269 385 NLT--EAIGLELPDElarmkaviTLKMVGFDEEkaEEILDKYPDE--------LSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 753 LAAVD----ADVANHLLH-RCILGmlsyTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:TIGR03269 455 TGTMDpitkVDVTHSILKaREEME----QTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
621-758 |
1.14e-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: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRG-----HVAVRGLSKGFGLATQE----PWIqfaTIRDNILFGKTFD 691
Cdd:COG4525 28 LTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGeitldGVPVTGPGADRGVVFQKdallPWL---NVLDNVAFGLRLR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217363546 692 ----AQLYKEVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:COG4525 105 gvpkAERRARAEELLAL--------------VGLADFarrriwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
621-811 |
1.51e-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: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSS-------LLAAIAGELHrLRGHVAVR---GLSKGFGLATQEPWIQFA-TIRDNI-LFGK 688
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTtikmlttLLKPTSGRAT-VAGHDVVReprEVRRRIGIVFQDLSVDDElTGWENLyIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 689 TFD------AQLYKEVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 761
Cdd:cd03265 100 LYGvpgaerRERIDELLDFVGL------------LEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 762 NHLLhRCILGMLSY--TTRLLCTHrteYLERADA----VLLMEAGRLIRAGPPSEI 811
Cdd:cd03265 168 AHVW-EYIEKLKEEfgMTILLTTH---YMEEAEQlcdrVAIIDHGRIIAEGTPEEL 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
621-810 |
1.53e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 62.45 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAG--------------ELHRL--RGHVAVRGLSKGFGLatQ-EPWIQFATIRDN 683
Cdd:COG4181 33 LEVEAGESVAIVGASGSGKSTLLGLLAGldrptsgtvrlagqDLFALdeDARARLRARHVGFVF--QsFQLLPTLTALEN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 684 I-----LFGKTFDAQLYKEVLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:COG4181 111 VmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTGNLDA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 759 DVANHllhrcILGML------SYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSE 810
Cdd:COG4181 180 ATGEQ-----IIDLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
621-812 |
1.79e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.09 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFG- 687
Cdd:PRK13632 30 FEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkeIRKKIGIIFQNPDNQFigATVEDDIAFGl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 --KTFDAQLYKEVLeacalnDDLSilpagdqTEVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:PRK13632 110 enKKVPPKKMKDII------DDLA-------KKVGMEDYldkepqNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217363546 760 vANHLLHRCILGMLSYTTRLL--CTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13632 177 -GKREIKKIMVDLRKTRKKTLisITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
621-812 |
2.96e-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: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIagelHRL----RGHVAVRG----------LSKGFGLATQE----PWIqfaTIRD 682
Cdd:cd03295 22 LEIAKGEFLVLIGPSGSGKTTTMKMI----NRLieptSGEIFIDGedireqdpveLRRKIGYVIQQiglfPHM---TVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 683 NI-----LFGKTfDAQLYKEVLEACALNDdlsiLPagDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:cd03295 95 NIalvpkLLKWP-KEKIRERADELLALVG----LD--PAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217363546 758 ADVANHL------LHRcilgmLSYTTRLLCTHRT-EYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03295 168 PITRDQLqeefkrLQQ-----ELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
621-820 |
3.00e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.41 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS-----------KGFGLATQEPWIQF-ATI-RDNILFG 687
Cdd:PRK13633 31 LEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdirNKAGMVFQNPDNQIvATIvEEDVAFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 KtfdaqlykevleacalnDDLSILPAGDQTEVGE--KGVT-----------LSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:PRK13633 111 P-----------------ENLGIPPEEIRERVDEslKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 755 AVDA----DVANHLLHrciLGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPK 820
Cdd:PRK13633 174 MLDPsgrrEVVNTIKE---LNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVEMMKK 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
624-811 |
3.55e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.95 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 624 KKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--------------------------LSKGFGLATQEPWIQF 677
Cdd:PRK13631 50 EKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitnpyskkiknfkeLRRRVSMVFQFPEYQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 678 --ATIRDNILFG-------KTFDAQLYKEVLEACALNDD-LSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKELY 747
Cdd:PRK13631 130 fkDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 748 LLDDPLAAVDADvANHLLHRCIL-GMLSYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13631 199 IFDEPTAGLDPK-GEHEMMQLILdAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
620-811 |
4.12e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.34 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV--------------RGLSKGFGLATQEPWIQF--ATIRDN 683
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkknkklKPLRKKVGIVFQFPEHQLfeETVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 684 ILFG-KTF-----DA-QLYKEVLEACALNDDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAV 756
Cdd:PRK13634 107 ICFGpMNFgvseeDAkQKAREMIELVGLPEELLARSPFE----------LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217363546 757 DADVANHL------LHRcILGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13634 177 DPKGRKEMmemfykLHK-EKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
620-812 |
4.73e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.14 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV------------AVRGLSKGFglatQEPWIqFA--TIRDNIL 685
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhtttppSRRPVSMLF----QENNL-FShlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 686 FG-----KTFDAQlyKEVLEACA----LNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAV 756
Cdd:PRK10771 94 LGlnpglKLNAAQ--REKLHAIArqmgIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 757 DADVANHllhrcILGMLS------YTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK10771 161 DPALRQE-----MLTLVSqvcqerQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
621-803 |
4.81e-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: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlskgfglatqEPwIQFATIRDnilfgktfdAQlykevle 700
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG----------KE-VSFASPRD---------AR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 701 acalnddlsilpagdqtevgEKGVT----LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGML--S 774
Cdd:cd03216 74 --------------------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLraQ 131
|
170 180 190
....*....|....*....|....*....|
gi 2217363546 775 YTTRLLCTHR-TEYLERADAVLLMEAGRLI 803
Cdd:cd03216 132 GVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
611-820 |
4.86e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.07 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 611 GTSLET---FISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV--------------RGLSKGFGLATQEP 673
Cdd:PRK13649 15 GTPFEGralFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVddtlitstsknkdiKQIRKKVGLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 674 WIQ-FA-TIRDNILFG-KTFDAQlyKEVLEACALNddlSILPAGDQTEVGEKG-VTLSGGQRARIALARAVYQEKELYLL 749
Cdd:PRK13649 95 ESQlFEeTVLKDVAFGpQNFGVS--QEEAEALARE---KLALVGISESLFEKNpFELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 750 DDPLAAVDADVANHL------LHRciLGMlsytTRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEILPLVQ------ 816
Cdd:PRK13649 170 DEPTAGLDPKGRKELmtlfkkLHQ--SGM----TIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIFQDVDfleekq 243
|
....*
gi 2217363546 817 -AVPK 820
Cdd:PRK13649 244 lGVPK 248
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
621-811 |
6.19e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.43 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGfglATQEPWI-----QFA-----TIRDNILFG- 687
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedVTHR---SIQQRDIcmvfqSYAlfphmSLGENVGYGl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 ---KTFDAQLYKEVLEACALNDdlsilPAG------DQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:PRK11432 104 kmlGVPKEERKQRVKEALELVD-----LAGfedryvDQ---------ISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 759 DvanhlLHRCI------LGMLSYTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
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 ... |
621-802 |
9.85e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 59.85 E-value: 9.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGeLHRL-RGHVAVRGLS------------KGFGLATQepwiQFA-----TIRD 682
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINL-LEEPdSGTIIIDGLKltddkkninelrQKVGMVFQ----QFNlfphlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 683 NILFGKTF-------DAQ-LYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLA 754
Cdd:cd03262 96 NITLAPIKvkgmskaEAEeRALELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 755 AVDA-------DVANHLLHRcilGMlsytTRLLCTHRTEY-LERADAVLLMEAGRL 802
Cdd:cd03262 165 ALDPelvgevlDVMKDLAEE---GM----TMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
621-812 |
1.04e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 60.14 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH------RLRGH---------VAVRGLSKGFglatQEPWIqFA--TIRDN 683
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsvLFDGEditglppheIARLGIGRTF----QIPRL-FPelTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 684 ILFGKTFDAQLY-----------------KEVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKEL 746
Cdd:cd03219 96 VMVAAQARTGSGlllararreereareraEELLERVGL-ADLADRPAG----------ELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 747 YLLDDPLAAVDADVANHLLHRcILGM-LSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAEL-IRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
620-800 |
1.05e-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: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGelhrL----RGHVAVRGLSKGFGLAtQEPWIQFATIRDNILF---GKTFDA 692
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARPAGARVLFLP-QRPYLPLGTLREALLYpatAEAFSD 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 693 QLYKEVLEACALnDDLsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGM 772
Cdd:COG4178 458 AELREALEAVGL-GHL----AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREE 531
|
170 180
....*....|....*....|....*...
gi 2217363546 773 LSYTTRLLCTHRTEYLERADAVLLMEAG 800
Cdd:COG4178 532 LPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
620-757 |
1.09e-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: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS-----------KGFGLATQEPWIqFA--TIRDNIL- 685
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarLGIGYLPQEASI-FRklTVEENILa 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 686 ----FGKTFDAQlyKEVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:cd03218 99 vleiRGLSKKER--EEKLEE--LLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
621-820 |
1.39e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.79 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV---------------AVRGLSKGFGLATQEPWIQF--ATIRDN 683
Cdd:PRK13645 32 LTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyaipanlkkikEVKRLRKEIGLVFQFPEYQLfqETIEKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 684 ILFGKTF----DAQLYKEVLEACalndDLSILPagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:PRK13645 112 IAFGPVNlgenKQEAYKKVPELL----KLVQLP---EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 760 VANHLLHRCILGMLSYTTR-LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEILPLVQAVPK 820
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRiIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFSNQELLTK 247
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
620-812 |
1.94e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQFA-TIRDNILFG- 687
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaeLARRRAVLPQHSSLSFPfTVEEVVAMGr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 ------KTFDAQLYKEVLEACALnDDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQ------EKELYLLDDPLAA 755
Cdd:PRK13548 102 aphglsRAEDDALVAAALAQVDL-AHLA----------GRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 756 VD-------ADVANHLLHR------CILGMLSYTTRllcthrteYlerADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13548 171 LDlahqhhvLRLARQLAHErglaviVVLHDLNLAAR--------Y---ADRIVLLHQGRLVADGTPAEVL 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
621-811 |
2.13e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.63 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAG-------ELH---RLRGHV--AVRGLSKGFglatqepwiQ-FA-----TIRD 682
Cdd:PRK11650 25 LDVADGEFIVLVGPSGCGKSTLLRMVAGleritsgEIWiggRVVNELepADRDIAMVF---------QnYAlyphmSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 683 NILFG----KTFDAQLYKEVLEACALnddLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:PRK11650 96 NMAYGlkirGMPKAEIEERVAEAARI---LELEPLLDR-----KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 759 DVANHL------LHRCiLGmlsyTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11650 168 KLRVQMrleiqrLHRR-LK----TTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
621-817 |
2.61e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.64 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS----------KGFGLATQEPWIQF--ATIRDNILFGk 688
Cdd:PRK13635 28 FSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrRQVGMVFQNPDNQFvgATVQDDVAFG- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 689 tfdaqlykevLEACALNDDLSIlPAGDQ--TEVG------EKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA-- 758
Cdd:PRK13635 107 ----------LENIGVPREEMV-ERVDQalRQVGmedflnREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrg 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217363546 759 -----DVANHLLHRCILGMLSyttrllCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQA 817
Cdd:PRK13635 176 rrevlETVRQLKEQKGITVLS------ITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
621-812 |
2.84e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 59.36 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfgLATQEPW--------------IQFA-TIRDNIL 685
Cdd:COG4559 22 LTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRP----LAAWSPWelarrravlpqhssLAFPfTVEEVVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 686 FG-------KTFDAQLYKEVLEACalndDLSILPAGDQTevgekgvTLSGGQRARIALARA-------VYQEKELYLLDD 751
Cdd:COG4559 98 LGraphgssAAQDRQIVREALALV----GLAHLAGRSYQ-------TLSGGEQQRVQLARVlaqlwepVDGGPRWLFLDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 752 PLAAVD-------ADVANHLLHR-----CILGMLSYTTRLlcthrteylerADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG4559 167 PTSALDlahqhavLRLARQLARRgggvvAVLHDLNLAAQY-----------ADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
620-814 |
3.30e-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: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGelHR----LRGHVAVRGLS-----------KGFGLATQEPwIQFATIRDni 684
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPkyevTEGEILFKGEDitdlppeerarLGIFLAFQYP-PEIPGVKN-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 685 lfgktfdAQLYKEVleacalnddlsilpagdqtevgekGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHL 764
Cdd:cd03217 95 -------ADFLRYV------------------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID-ALRL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 765 LHRCILGMLSYTTR-LLCTHRTEYLE--RADAVLLMEAGRLIRAGPPSEILPL 814
Cdd:cd03217 143 VAEVINKLREEGKSvLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKELALEI 195
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
611-806 |
4.43e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.49 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 611 GTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAI-------AGELHrLRGHV----------AVRGLSKGFGLATQE- 672
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLN-IAGNHfdfsktpsdkAIRELRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 673 -PWIQFaTIRDNIL--------FGKTFDAQLYKEVLEACALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQE 743
Cdd:PRK11124 92 nLWPHL-TVQQNLIeapcrvlgLSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 744 KELYLLDDPLAAVDADVANHLLHrcILGMLSYT--TRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVS--IIRELAETgiTQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
621-818 |
5.90e-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: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS-----------KGFGLATQEPWIqFA--TIRDNIL-- 685
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmhkrarLGIGYLPQEASI-FRklTVEDNILav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 686 ---FGKTFDAQlyKEVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVD----A 758
Cdd:COG1137 103 lelRKLSKKER--EERLEE--LLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiavA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217363546 759 DVAN---HLLHRCIlGMlsyttrLLCTH--RtEYLERADAVLLMEAGRLIRAGPPSEIL--PLVQAV 818
Cdd:COG1137 174 DIQKiirHLKERGI-GV------LITDHnvR-ETLGICDRAYIISEGKVLAEGTPEEILnnPLVRKV 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
313-750 |
6.90e-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: 59.81 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 313 LEEGQEPLSHGLLYALGLAGGAVLGAVL-QNQYGYEVYKVTLQARGAVLN-ILYC---KALQLGPSRpptgeALNLLGTD 387
Cdd:COG4615 40 LNATGAALARLLLLFAGLLVLLLLSRLAsQLLLTRLGQHAVARLRLRLSRrILAApleRLERIGAAR-----LLAALTED 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 388 SERLLNFAGSFHEA-WGLPLQLAITLYLLYQQVgVAFVGGLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELL 466
Cdd:COG4615 115 VRTISQAFVRLPELlQSVALVLGCLAYLAWLSP-PLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 467 SGIRVIK---------FcgwEQALGARVEACRARelgRLRVIKYLDAACVYLWAALPVVISIVIFityVLMGHQLTATKV 537
Cdd:COG4615 194 EGFKELKlnrrrrrafF---DEDLQPTAERYRDL---RIRADTIFALANNWGNLLFFALIGLILF---LLPALGWADPAV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 538 FTALALVRM-LILPLNNFPWVINGLLEAKVSLDRI-QLFLDLPNHNPQAYYSPDPPAEPS-TVLELHGALFSWDPVGTSl 614
Cdd:COG4615 265 LSGFVLVLLfLRGPLSQLVGALPTLSRANVALRKIeELELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGD- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 615 ETF----IShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlsKGFGLATQEPWIQ-FATI-RDNILF-- 686
Cdd:COG4615 344 EGFtlgpID-LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG--QPVTADNREAYRQlFSAVfSDFHLFdr 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217363546 687 ----GKTFDAQLYKEVLEACALNDDLSIlpagdqtevgEKG----VTLSGGQRARIALARAVYQEKELYLLD 750
Cdd:COG4615 421 llglDGEADPARARELLERLELDHKVSV----------EDGrfstTDLSQGQRKRLALLVALLEDRPILVFD 482
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
588-764 |
8.44e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.69 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 588 PDPPAEPSTVLELHGALFSWD--PVgtsLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV-RGLSK 664
Cdd:COG0488 306 PPPERLGKKVLELEGLSKSYGdkTL---LDDL--SLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 665 GFglatqepwiqFATIRDnilfgkTFDAQlyKEVLEA-CALNDDLSILPA----------GDQ--TEVGekgvTLSGGQR 731
Cdd:COG0488 381 GY----------FDQHQE------ELDPD--KTVLDElRDGAPGGTEQEVrgylgrflfsGDDafKPVG----VLSGGEK 438
|
170 180 190
....*....|....*....|....*....|...
gi 2217363546 732 ARIALARAVYQEKELYLLDDPlaavdadvANHL 764
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEP--------TNHL 463
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
621-757 |
8.67e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.87 E-value: 8.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAA-------IAGelHRLRGHVAVRG------------LSKGFGLATQEPWIQFATIR 681
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPG--FRVEGKVTFHGknlyapdvdpveVRRRIGMVFQKPNPFPKSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 682 DNILFGKTFDA------QLYKEVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK14243 109 DNIAYGARINGykgdmdELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
..
gi 2217363546 756 VD 757
Cdd:PRK14243 182 LD 183
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
631-811 |
9.06e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 631 IVGKVGCGKSSLLAAI--AGELH---RLRGHVAVRG------------LSKGFGLATQEPWIQFATIRDNILFGKTFDAQ 693
Cdd:PRK14239 36 LIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGhniysprtdtvdLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 694 LYKEVLEACALNddlSILPAGDQTEVGEK----GVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCI 769
Cdd:PRK14239 116 KDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDP-ISAGKIEETL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217363546 770 LGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK14239 192 LGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
621-812 |
9.51e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.54 E-value: 9.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAI-----AGELHRLRGHVAVRGLS------------KGFGLATQEP-WIQFATIRD 682
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNiyspdvdpievrREVGMVFQYPnPFPHLTIYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 683 NILFGKTFDA---------QLYKEVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:PRK14267 105 NVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 754 AAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK14267 178 ANIDP-VGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
621-811 |
1.06e-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: 57.13 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPWI----QF------ATIRDNILF---- 686
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgycpQFdalfdeLTVREHLRFyarl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 -GKtFDAQLYKEVLeacALNDDLSILPAGDqTEVGekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLL 765
Cdd:cd03263 103 kGL-PKSEIKEEVE---LLLRVLGLTDKAN-KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP-ASRRAI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217363546 766 HRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:cd03263 173 WDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
621-802 |
1.24e-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: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-------------LSKGFGLATQE-PWIQFATIRDNILF 686
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipyLRRKIGVVFQDfRLLPDRNVYENVAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 -------GKTFDAQLYKEVLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:cd03292 102 alevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217363546 760 VANHLLHRCILGMLSYTTRLLCTHRTEYLERADA-VLLMEAGRL 802
Cdd:cd03292 171 TTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
621-821 |
1.32e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 57.39 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG------------LSKGFGLATQEPWIQ-FA-TIRDNILF 686
Cdd:PRK13639 23 FKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkslleVRKTVGIVFQNPDDQlFApTVEEDVAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 G----KTFDAQLYKEVLEACAlnddlsilpagdqtEVGEKGVT------LSGGQRARIALARAVYQEKELYLLDDPLAAV 756
Cdd:PRK13639 103 GplnlGLSKEEVEKRVKEALK--------------AVGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 757 DADVANHLLHrcILGMLSY--TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEILPLVQAVPKA 821
Cdd:PRK13639 169 DPMGASQIMK--LLYDLNKegITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSDIETIRKA 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
621-812 |
1.33e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.21 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAV------------RGLsKGFGLATQEPWI-QFATIRDNILFG 687
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplhaRAR-RGIGYLPQEASIfRRLSVYDNLMAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 KTFDAQLYKEVLE--ACALNDDLSILPAGDQTevgekGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLL 765
Cdd:PRK10895 103 LQIRDDLSAEQREdrANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP-ISVIDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217363546 766 HRCILGMLSYTTRLLCTHRT--EYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK10895 177 KRIIEHLRDSGLGVLITDHNvrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
622-768 |
1.54e-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: 58.99 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 622 EVKKGMLVGIVGKVGCGKSSLLAaIAGELHRLRGHVAVRGLSKGFGLATQEPWIQFATIRDNIL--------FGKTFDAQ 693
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIypdssedmKRRGLSDK 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 694 LYKEVLEACALNDDLsilpagdQTEVGEKGV-----TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRC 768
Cdd:TIGR00954 553 DLEQILDNVQLTHIL-------EREGGWSAVqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
621-806 |
1.60e-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: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGlsKGFGLATQEpwiQFA------------TIRDNILFGk 688
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--KPLDIAARN---RIGylpeerglypkmKVIDQLVYL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 689 tfdAQLyKEVLEACALNDDLSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHR 767
Cdd:cd03269 95 ---AQL-KGLKKEEARRRIDEWLERLELSEYANKRVeELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217363546 768 CILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:cd03269 170 VIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
542-806 |
1.86e-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: 58.68 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 542 ALVRMLILPLNNFPWVINgllEAKVSLDRIQLFLDLPNHNPQAYYSPDPPAEPSTvlelHGAL------FSWDPVGTSLE 615
Cdd:COG5265 303 AYLIQLYIPLNFLGFVYR---EIRQALADMERMFDLLDQPPEVADAPDAPPLVVG----GGEVrfenvsFGYDPERPILK 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 616 TfIShLEVKKGMLVGIVGKVGCGKSSLLaaiagelhRL--------RGHVAVRG----------LSKGFGLATQEPwIQF 677
Cdd:COG5265 376 G-VS-FEVPAGKTVAIVGPSGAGKSTLA--------RLlfrfydvtSGRILIDGqdirdvtqasLRAAIGIVPQDT-VLF 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 678 -ATIRDNILFGKTfDAQlYKEVLEA---CALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:COG5265 445 nDTIAYNIAYGRP-DAS-EEEVEAAaraAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217363546 754 AAVD-----------ADVANHllhrcilgmlsyTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 806
Cdd:COG5265 523 SALDsrteraiqaalREVARG------------RTTLVIAHRLSTIVDADEILVLEAGRIVERG 574
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
623-806 |
1.95e-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: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 623 VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------------LSKGFGLAtqePWIqfaTIRDNILF 686
Cdd:cd03266 28 VKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrrlgfVSDSTGLY---DRL---TARENLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 gktFdAQLYKevLEACALNDDLSILpaGDQTEVGE----KGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN 762
Cdd:cd03266 102 ---F-AGLYG--LKGDELTARLEEL--ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217363546 763 HLL----HRCILGmlsyTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:cd03266 174 ALRefirQLRALG----KCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
621-789 |
2.08e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGElhrlrghvAVRGLSKGFGLATQEPWIQFATIRDNILFGKTFDAQLykEVLE 700
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGA--------LKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAV--ELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 701 ACALNDDLSILPAGDQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS---YTT 777
Cdd:COG2401 121 AVGLSDAVLWLRRFKE---------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR--NLQKLArraGIT 189
|
170
....*....|..
gi 2217363546 778 RLLCTHRTEYLE 789
Cdd:COG2401 190 LVVATHHYDVID 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
623-812 |
2.12e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.53 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 623 VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS---------KGFGLATQ----EPwiQFaTIRDNIL-FGK 688
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvpararlarARIGVVPQfdnlDL--EF-TVRENLLvFGR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 689 TFDAQLyKEVLEACALNDDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRC 768
Cdd:PRK13536 141 YFGMST-REIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWER 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217363546 769 ILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13536 215 LRSLLARgKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
620-764 |
2.30e-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: 54.38 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAvrglskgfglatqepWIQFATIrdnilfgktfdaqlykevl 699
Cdd:cd03221 20 SLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------------WGSTVKI------------------- 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217363546 700 eacalnddlSILPagdQtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLaavdadvaNHL 764
Cdd:cd03221 66 ---------GYFE---Q---------LSGGEKMRLALAKLLLENPNLLLLDEPT--------NHL 101
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
621-806 |
3.09e-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: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLvGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS---------KGFGLATQEP-WIQFATIRD-----NIL 685
Cdd:cd03264 21 LTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvlkqpqklrRRIGYLPQEFgVYPNFTVREfldyiAWL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 686 FG---KTFDAQLyKEVLEACALNDdlsilpagdqtEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVdaDVAN 762
Cdd:cd03264 100 KGipsKEVKARV-DEVLELVNLGD-----------RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL--DPEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217363546 763 HLLHRCILGMLSYT-TRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 806
Cdd:cd03264 166 RIRFRNLLSELGEDrIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
631-811 |
3.70e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.81 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 631 IVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----LSKGFGLATQEPWI----QFA------TIRDNILFG-KTFDAQL 694
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPPEKRRIgyvfQDArlfphyKVRGNLRYGmAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 695 YKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS 774
Cdd:PRK11144 109 FDKIVALLGIEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP--YLERLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217363546 775 YTTR---LLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11144 176 REINipiLYVSHSlDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
621-803 |
4.33e-08 |
|
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: 55.42 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfglatqePW---IQFATiRDNILFG-KTfdaQLYK 696
Cdd:cd03267 42 FTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV---------PWkrrKKFLR-RIGVVFGqKT---QLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 697 E--VLEACALNDDLSILPAG-------------DQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdV 760
Cdd:cd03267 109 DlpVIDSFYLLAAIYDLPPArfkkrldelsellDLEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV-V 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217363546 761 ANHLLHRCI--LGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLI 803
Cdd:cd03267 188 AQENIRNFLkeYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
620-798 |
4.45e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 54.08 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLAtQEPWIQFATIRDNIlfgktfdaqlykevl 699
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLP-QRPYLPLGTLREQL--------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 700 eacalnddlsILPAGDqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCilgmlsytTRL 779
Cdd:cd03223 85 ----------IYPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL--------KEL 137
|
170 180
....*....|....*....|....
gi 2217363546 780 LCT-----HRTEYLERADAVLLME 798
Cdd:cd03223 138 GITvisvgHRPSLWKFHDRVLDLD 161
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
621-812 |
4.51e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.53 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAI---------------------------AGELHRLRGHVAVrgLSKGFGLATQEp 673
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirvgditidtarslsqqKGLIRQLRQHVGF--VFQNFNLFPHR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 674 wiqfaTIRDNILFGKTFDAQLYKEvlEACALNDDL--SILPAGDQTEVGEKgvtLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:PRK11264 101 -----TVLENIIEGPVIVKGEPKE--EATARARELlaKVGLAGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 752 PLAAVDADVANHLLHrCILGMLSYT-TRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK11264 171 PTSALDPELVGEVLN-TIRQLAQEKrTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
621-821 |
5.51e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.78 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG------------LSKGFGLATQEP--WIQFATIRDNILF 686
Cdd:PRK13638 22 LDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpldyskrgllaLRQQVATVFQDPeqQIFYTDIDSDIAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 G----KTFDAQLYKEVLEACALNDDLSILPAGDQTevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN 762
Cdd:PRK13638 102 SlrnlGVPEAEITRRVDEALTLVDAQHFRHQPIQC--------LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217363546 763 HLLH--RCILGMLSYTtrLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEILPLVQAVPKA 821
Cdd:PRK13638 174 QMIAiiRRIVAQGNHV--IISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEAMEQA 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
621-790 |
6.16e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.43 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIaGELHRLRGHVAVRGLSKGFGLATQEPWIQFATIRDNI--LFGKT--FDAQLYK 696
Cdd:PRK14258 28 MEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYERRVNLNRLRRQVsmVHPKPnlFPMSVYD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 697 EVLEACALN--------DDL--SILPAGD-----QTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 761
Cdd:PRK14258 107 NVAYGVKIVgwrpkleiDDIveSALKDADlwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAS 186
|
170 180 190
....*....|....*....|....*....|..
gi 2217363546 762 ---NHLLHRciLGMLSYTTRLLCTHRTEYLER 790
Cdd:PRK14258 187 mkvESLIQS--LRLRSELTMVIVSHNLHQVSR 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
962-1233 |
7.71e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 56.71 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 962 SDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVA----CADD 1037
Cdd:COG1132 58 SALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDaveqFLAH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1038 SLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRlgslTLSPLYSHLADTLAGLSVL 1117
Cdd:COG1132 138 GLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQE----ALAELNGRLQESLSGIRVV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 1118 RATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYALSLTGL 1197
Cdd:COG1132 214 KAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGP 293
|
250 260 270
....*....|....*....|....*....|....*.
gi 2217363546 1198 LSGLVSSFTQTEAMLVSVERLEEYTcDLPQEPQGQP 1233
Cdd:COG1132 294 LRQLANVLNQLQRALASAERIFELL-DEPPEIPDPP 328
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
584-757 |
8.08e-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: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 584 AYYSPDPPAEPSTVLELHGalFSWDPVGTSletfIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-- 661
Cdd:COG1129 243 DLFPKRAAAPGEVVLEVEG--LSVGGVVRD----VS-FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkp 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 662 ---------LSKGFGLAT----QEPWIQFATIRDNI---LFGKTFDAQLY---KEVLEACALNDDLSILPAGDQTEVGek 722
Cdd:COG1129 316 vrirsprdaIRAGIAYVPedrkGEGLVLDLSIRENItlaSLDRLSRGGLLdrrRERALAEEYIKRLRIKTPSPEQPVG-- 393
|
170 180 190
....*....|....*....|....*....|....*
gi 2217363546 723 gvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:COG1129 394 --NLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
561-802 |
8.33e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 561 LLEAKVSLDRIQLFlDLpnhnpqAYYSPD---PPAEPS-TVLELHGALFSWDPVGTSLETFisHLEVKKGMLVGIVGKVG 636
Cdd:PRK10522 289 LLSAQVAFNKLNKL-AL------APYKAEfprPQAFPDwQTLELRNVTFAYQDNGFSVGPI--NLTIKRGELLFLIGGNG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 637 CGKSSLLAAIAGELHRLRGHVAVRGlsKGFGLATQEPWIQ-FATI-RDNILFGKTFDAQlyKEVLEACALNDDLSILPAG 714
Cdd:PRK10522 360 SGKSTLAMLLTGLYQPQSGEILLDG--KPVTAEQPEDYRKlFSAVfTDFHLFDQLLGPE--GKPANPALVEKWLERLKMA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 715 DQTEVGEKGVT---LSGGQRARIALARAVYQEKELYLLDDplAAVDAD-VANHLLHRCILGMLSYT--TRLLCTHRTEYL 788
Cdd:PRK10522 436 HKLELEDGRISnlkLSKGQKKRLALLLALAEERDILLLDE--WAADQDpHFRREFYQVLLPLLQEMgkTIFAISHDDHYF 513
|
250
....*....|....
gi 2217363546 789 ERADAVLLMEAGRL 802
Cdd:PRK10522 514 IHADRLLEMRNGQL 527
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
621-809 |
8.44e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.13 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFGK 688
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGrevnaenekwVRSKVGLVFQDPDDQVfsSTVWDDVAFGP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 689 TFDAQLYKEVLEAcaLNDDLSILpagDQTEVGEKG-VTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLlhR 767
Cdd:PRK13647 106 VNMGLDKDEVERR--VEEALKAV---RMWDFRDKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL--M 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217363546 768 CILGMLSY--TTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPS 809
Cdd:PRK13647 179 EILDRLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKS 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
629-832 |
9.39e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.81 E-value: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 629 VGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFGKT---FDAQ 693
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenireVRKFVGLVFQNPDDQIfsPTVEQDIAFGPInlgLDEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 694 LYK----EVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcI 769
Cdd:PRK13652 113 TVAhrvsSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID--F 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 770 LGMLSYT---TRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPPSEI-------------LPLVQAVPKAWAENGQESDSA 832
Cdd:PRK13652 180 LNDLPETygmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIflqpdllarvhldLPSLPKLIRSLQAQGIAIDMA 259
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
938-1045 |
1.13e-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: 54.86 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 938 LLLFSPGNLYIPVFP---LPKAAPNGS-SDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPV 1013
Cdd:cd18572 5 LVVAALSELAIPHYTgavIDAVVADGSrEAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDI 84
|
90 100 110
....*....|....*....|....*....|..
gi 2217363546 1014 TFFNATPTGRILNRFSSDVACADDSLPFILNI 1045
Cdd:cd18572 85 AFFDATKTGELTSRLTSDCQKVSDPLSTNLNV 116
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
715-812 |
1.13e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.59 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 715 DQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSY--TTRLLCTHRTEYLERAD 792
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEegKTMVVVTHEMGFARHVS 219
|
90 100
....*....|....*....|.
gi 2217363546 793 A-VLLMEAGRLIRAGPPSEIL 812
Cdd:PRK10619 220 ShVIFLHQGKIEEEGAPEQLF 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
621-811 |
2.02e-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: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLaaiagelHRLRG-------------HVA-------VRGLSK--------GFGLATQE 672
Cdd:TIGR03269 21 FTIEEGEVLGILGRSGAGKSVLM-------HVLRGmdqyeptsgriiyHVAlcekcgyVERPSKvgepcpvcGGTLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 673 P--WIQFATIRDN------ILFGKTFdaQLYKE--VLEAC--ALND-----DLSILPAGD---QTEVGEK----GVTLSG 728
Cdd:TIGR03269 94 VdfWNLSDKLRRRirkriaIMLQRTF--ALYGDdtVLDNVleALEEigyegKEAVGRAVDlieMVQLSHRithiARDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 729 GQRARIALARAVYQEKELYLLDDPLAAVDADVANhLLHRCILGML--SYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRA 805
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLENGEIKEE 250
|
....*.
gi 2217363546 806 GPPSEI 811
Cdd:TIGR03269 251 GTPDEV 256
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
621-758 |
2.34e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH------RLRGhVAVRGLSKGFGLATQE----PWiqfATIRDNILFGKTF 690
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDG-KPVEGPGAERGVVFQNegllPW---RNVQDNVAFGLQL 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217363546 691 dAQLYKEVLEACALnddlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:PRK11248 98 -AGVEKMQRLEIAH----QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
623-806 |
2.47e-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: 52.55 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 623 VKKGMLVGIVGKVGCGKSSLLAAIAGEL--HRLRGHVAVRG-------LSKGFGLATQEPwIQFA--TIRDNILFGktfd 691
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGrpldkrsFRKIIGYVPQDD-ILHPtlTVRETLMFA---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 692 AQLykevleacalnddlsilpagdqtevgeKGvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILG 771
Cdd:cd03213 107 AKL---------------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS--LLR 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217363546 772 MLSYTTR-LLCT-H--RTEYLERADAVLLMEAGRLIRAG 806
Cdd:cd03213 156 RLADTGRtIICSiHqpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
629-803 |
3.44e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 629 VGIVGKVGCGKSSLLAAIAGELHRLRGHVavrglskgfglatqepwiqfatirdnilfgKTFDAQLYKEVLEACALNddl 708
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGV------------------------------IYIDGEDILEEVLDQLLL--- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 709 silpagdqTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGML-----SYTTRLLCTH 783
Cdd:smart00382 52 --------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllksEKNLTVILTT 123
|
170 180
....*....|....*....|
gi 2217363546 784 RTEYLERADAVLLMEAGRLI 803
Cdd:smart00382 124 NDEKDLGPALLRRRFDRRIV 143
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
621-761 |
3.61e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.09 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAG--------ELH-RLRGHVA------VRGLSKGFG----LATQEPWIQFATIR 681
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksaGSHiELLGRTVqregrlARDIRKSRAntgyIFQQFNLVNRLSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 682 DNILFGKTFDAQLYKEVLEACALNDDLSILPAgdQTEVG------EKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK09984 105 ENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
....*.
gi 2217363546 756 VDADVA 761
Cdd:PRK09984 183 LDPESA 188
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
608-812 |
4.83e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.50 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 608 DPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGfglATQEPWIQFATIRDNILFG 687
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIA---KISDAELREVRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 KTFDAQLYKEVLEACALNDDLSILPAGDQTE--------VGEKGVT------LSGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:PRK10070 113 QSFALMPHMTVLDNTAFGMELAGINAEERREkaldalrqVGLENYAhsypdeLSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217363546 754 AAVDADVANHLLHRCI-LGMLSYTTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK10070 193 SALDPLIRTEMQDELVkLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
621-812 |
5.41e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------------LSKGFGLATQEP-WIQFATIRDN 683
Cdd:PRK14246 31 IKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyfgkdifqidaikLRKEVGMVFQQPnPFPHLSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 684 ILF----GKTFDAQLYKEVLEACalnddlsILPAGDQTEVGEK----GVTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK14246 111 IAYplksHGIKEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 756 VDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK14246 184 IDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
631-795 |
6.45e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.64 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 631 IVGKVGCGKSSLLAAIAGELHRLRGHVAVRG-----LS-----KGFGLATQEPWIQFATIRDNILfgktFDAQLYKEVLE 700
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistLKpeiyrQQVSYCAQTPTLFGDTVYDNLI----FPWQIRNQQPD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 701 ACALNDDLSI--LPagdqTEVGEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDAD---VANHLLHRcilgmls 774
Cdd:PRK10247 114 PAIFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESnkhNVNEIIHR------- 182
|
170 180
....*....|....*....|....*.
gi 2217363546 775 YTTR-----LLCTHRTEYLERADAVL 795
Cdd:PRK10247 183 YVREqniavLWVTHDKDEINHADKVI 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
620-759 |
7.70e-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: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGFGLATQE-PWIQFA-------TIRDNILFGKT 689
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtpLAEQRDEPHENiLYLGHLpglkpelSALENLHFWAA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 690 F--DAQLY-KEVLEACALNDdLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:TIGR01189 100 IhgGAQRTiEDALAAVGLTG-FEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
621-812 |
9.59e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.75 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELH--------RLRGHVAVRG----------LSKGFGLATQEPWIQFA-TIR 681
Cdd:PRK13547 22 LRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGeplaaidaprLARLRAVLPQAAQPAFAfSAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 682 DNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQ---------EKELYLLDDP 752
Cdd:PRK13547 102 EIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217363546 753 LAAVDadvanhllhrcilgmLSYTTRLLCTHRTEYLE-----------------RADAVLLMEAGRLIRAGPPSEIL 812
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 ... |
626-758 |
9.60e-07 |
|
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: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 626 GMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVavrgLSKGFGLATQEPWIQfatirDNILFGKTFDAqlYKEVLEA---- 701
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----LLNGGPLDFQRDSIA-----RGLLYLGHAPG--IKTTLSVlenl 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 702 ---CALNDDLSILPAGDQteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:cd03231 95 rfwHADHSDEQVEEALAR--VGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
594-812 |
1.01e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.77 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 594 PSTVLELHGALFSWdPVGTSLETFIShLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG------------ 661
Cdd:PRK13636 2 EDYILKVEELNYNY-SDGTHALKGIN-INIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 662 LSKGFGLATQEPwiqfatirDNILFgktfDAQLYKEVlEACALNDDLSilpagdQTEVGEK--------GVT-------- 725
Cdd:PRK13636 80 LRESVGMVFQDP--------DNQLF----SASVYQDV-SFGAVNLKLP------EDEVRKRvdnalkrtGIEhlkdkpth 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 726 -LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhRCILGMLSYT--TRLLCTHRTEYLE-RADAVLLMEAGR 801
Cdd:PRK13636 141 cLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM-KLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGR 219
|
250
....*....|.
gi 2217363546 802 LIRAGPPSEIL 812
Cdd:PRK13636 220 VILQGNPKEVF 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
621-757 |
1.25e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.42 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGL----------ATQEPWIQFATIRDNILFG--- 687
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALqknlvayvpqSEEVDWSFPVLVEDVVMMGryg 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 688 --------KTFDAQLYKEVLEACALNDDlsilpagDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:PRK15056 108 hmgwlrraKKRDRQIVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
622-759 |
1.37e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.26 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 622 EVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFG--------LATQEPWIQFATIRDNILFGKTFDAQ 693
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPdvaeachyLGHRNAMKPALTVAENLEFWAAFLGG 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 694 LYKEVLEA-CALN-DDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 759
Cdd:PRK13539 104 EELDIAAAlEAVGlAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
623-811 |
1.58e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.27 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 623 VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWIQF--ATIRDNILFG--- 687
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdIRHKIGMVFQNPDNQFvgATVEDDVAFGlen 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 KTFDAQLYKE-VLEACALnddlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLH 766
Cdd:PRK13650 110 KGIPHEEMKErVNEALEL--------VGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217363546 767 -----RCILGMlsytTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13650 182 tikgiRDDYQM----TVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
621-812 |
1.69e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 51.34 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGFGLATQEPWI--QFA------TIRDNIL-FGKT 689
Cdd:PRK13537 28 FHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepVPSRARHARQRVGVvpQFDnldpdfTVRENLLvFGRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 690 F---DAQLYKEV---LEacalnddLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANH 763
Cdd:PRK13537 108 FglsAAAARALVpplLE-------FAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217363546 764 LLHRCILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13537 176 LMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
621-812 |
2.30e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.76 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV----------AVRGLSKGFGLATQEPWIQF-ATIRDNILFGKT 689
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyASKEVARRIGLLAQNATTPGdITVQELVARGRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 690 FDAQLY----KEVLEACAlnddlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL 764
Cdd:PRK10253 108 PHQPLFtrwrKEDEEAVT-----KAMQATGITHLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217363546 765 LHrcILGMLS----YTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK10253 183 LE--LLSELNrekgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
620-757 |
2.69e-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: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGML-----VGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFglATQEPWIQFATIRDNILFGKTFD--- 691
Cdd:cd03237 14 TLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY--KPQYIKADYEGTVRDLLSSITKDfyt 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217363546 692 -AQLYKEVLeacalnDDLSILPAGDQtEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:cd03237 92 hPYFKTEIA------KPLQIEQILDR-EVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
621-812 |
2.89e-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: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAG---------------------ELHRLRGHVavrglskgfGLATQepwiQF-- 677
Cdd:COG1126 22 LDVEKGEVVVIIGPSGSGKSTLLRCINLleepdsgtitvdgedltdskkDINKLRRKV---------GMVFQ----QFnl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 678 ---ATIRDNILFGKTFDAQLYKEVLEACALNddlsILpagDQTEVGEKG----VTLSGGQRARIALARAVYQEKELYLLD 750
Cdd:COG1126 89 fphLTVLENVTLAPIKVKKMSKAEAEERAME----LL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217363546 751 DPLAAVD-------ADVANHLLHRcilGMlsytTRLLCTH-----RteylERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG1126 162 EPTSALDpelvgevLDVMRDLAKE---GM----TMVVVTHemgfaR----EVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
621-757 |
3.29e-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: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLL------------AAIAGELhRLRGH---------VAVRglsKGFGLATQEPwIQFA- 678
Cdd:COG1117 32 LDIPENKVTALIGPSGCGKSTLLrclnrmndlipgARVEGEI-LLDGEdiydpdvdvVELR---RRVGMVFQKP-NPFPk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 679 TIRDNILFG--------KTFDAQLYKEVLEACALNDdlsilpagdqtEV----GEKGVTLSGGQRARIALARAVYQEKEL 746
Cdd:COG1117 107 SIYDNVAYGlrlhgiksKSELDEIVEESLRKAALWD-----------EVkdrlKKSALGLSGGQQQRLCIARALAVEPEV 175
|
170
....*....|.
gi 2217363546 747 YLLDDPLAAVD 757
Cdd:COG1117 176 LLMDEPTSALD 186
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
625-792 |
3.34e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 625 KGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPWIQFA----------TIRDNILFGKTFDAQL 694
Cdd:PRK13540 26 AGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVghrsginpylTLRENCLYDIHFSPGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 695 YkEVLEACALN--DDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLL-----HR 767
Cdd:PRK13540 106 V-GITELCRLFslEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIItkiqeHR 174
|
170 180
....*....|....*....|....*
gi 2217363546 768 CILGMLsyttrLLCTHRTEYLERAD 792
Cdd:PRK13540 175 AKGGAV-----LLTSHQDLPLNKAD 194
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
623-862 |
3.36e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 623 VKKGMLVGIVGKVGCGKSSLLA------------AIAGELHRLRgHVAVRGLSKGFGLATQEPWIQFATIRDNILFG--- 687
Cdd:PTZ00265 408 LTEGKTYAFVGESGCGKSTILKlierlydptegdIIINDSHNLK-DINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlys 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 -------------KTFDAQLYKEVLEACA------------------------------------------LNDDLSILP 712
Cdd:PTZ00265 487 lkdlealsnyyneDGNDSQENKNKRNSCRakcagdlndmsnttdsneliemrknyqtikdsevvdvskkvlIHDFVSALP 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 713 AGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDaDVANHLLHRCILGMLSYTTR--LLCTHRTEYLER 790
Cdd:PTZ00265 567 DKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRitIIIAHRLSTIRY 645
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 791 ADAVLLMeAGRliRAGPPSEILPLVQAVPKAWAENGQESDSATAQSVQNPEKTKEGLEE----EQSTSGRLLQEES 862
Cdd:PTZ00265 646 ANTIFVL-SNR--ERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGsyiiEQGTHDALMKNKN 718
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
621-812 |
4.88e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.63 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG----------LSKGFGLATQEPWI-QFATIRDNILFGKT 689
Cdd:PRK11231 23 LSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqLARRLALLPQHHLTpEGITVRELVAYGRS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 690 FDAQLYKEVleacALNDDLSILPAGDQTEV---GEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDadvANH-- 763
Cdd:PRK11231 103 PWLSLWGRL----SAEDNARVNQAMEQTRInhlADRRLTdLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD---INHqv 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 764 -LLHrcILGMLSYTTRLLCT--HRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK11231 176 eLMR--LMRELNTQGKTVVTvlHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
621-820 |
5.04e-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: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAI------AGE-------LHRLRGHvAVRGLSKGFGLATQEPwiqFA------TIR 681
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLGLALlrlipsEGEirfdgqdLDGLSRR-ALRPLRRRMQVVFQDP---FGslsprmTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 682 D------NILFGKTFDAQLYKEVLEACAlnddlsilpagdqtEVGEKGVTL-------SGGQRARIALARAVYQEKELYL 748
Cdd:COG4172 383 QiiaeglRVHGPGLSAAERRARVAEALE--------------EVGLDPAARhryphefSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 749 LDDPLAAVDADVANHLL---------HRcilgmLSYttrLLCTH-----RteYLerADAVLLMEAGRLIRAGPPSEIL-- 812
Cdd:COG4172 449 LDEPTSALDVSVQAQILdllrdlqreHG-----LAY---LFISHdlavvR--AL--AHRVMVMKDGKVVEQGPTEQVFda 516
|
250
....*....|....*
gi 2217363546 813 P-------LVQAVPK 820
Cdd:COG4172 517 PqhpytraLLAAAPL 531
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
623-813 |
7.15e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 49.41 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 623 VKKGMLVGIVGKVGCGKSSLLAAIAGEL---HRLRGHVAVRGLSKG----------FGLATQEPWIQF--ATIRDNILFG 687
Cdd:PRK13640 30 IPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTaktvwdirekVGIVFQNPDNQFvgATVGDDVAFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 KTFDA-------QLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADV 760
Cdd:PRK13640 110 LENRAvprpemiKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217363546 761 ANHLLHRCI-LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILP 813
Cdd:PRK13640 179 KEQILKLIRkLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
621-811 |
9.97e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.54 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGEL----HRLRGHVAVRGLS------KGFGLAT--QEPWIQF---ATIRDNIL 685
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPvapcalRGRKIATimQNPRSAFnplHTMHTHAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 686 -----FGKTFDAQLYKEVLEACALNDDLSILPAgdqtevgeKGVTLSGG--QRARIALarAVYQEKELYLLDDPLAAVDA 758
Cdd:PRK10418 104 etclaLGKPADDATLTAALEAVGLENAARVLKL--------YPFEMSGGmlQRMMIAL--ALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217363546 759 DVANH---LLHRCI----LGMlsyttrLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK10418 174 VAQARildLLESIVqkraLGM------LLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
622-802 |
1.17e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.89 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 622 EVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSKGFGLATQE------PWI-QFA------TIRDNI-- 684
Cdd:PRK11629 31 SIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpMSKLSSAAKAElrnqklGFIyQFHhllpdfTALENVam 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 685 --LFGKTFDAQLYKEVLEACAlnddlsilPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN 762
Cdd:PRK11629 111 plLIGKKKPAEINSRALEMLA--------AVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217363546 763 HLLHrcILGMLSY---TTRLLCTHRTEYLERADAVLLMEAGRL 802
Cdd:PRK11629 183 SIFQ--LLGELNRlqgTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
621-812 |
1.75e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.60 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAG--ELH---RLRGHVAVRG----------LSKGFGLATQEP-WIQFATIRDNI 684
Cdd:PRK14247 24 LEIPDNTITALMGPSGSGKSTLLRVFNRliELYpeaRVSGEVYLDGqdifkmdvieLRRRVQMVFQIPnPIPNLSIFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 685 LFGKTFD---------AQLYKEVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK14247 104 ALGLKLNrlvkskkelQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 756 VDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK14247 177 LDP-ENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVF 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
624-814 |
1.84e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.89 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 624 KKGMLVGIVGKVGCGKSSLLAAIAgelHRLRGHVAVRGLSKGFGLATQEPWIQ----FA----------TIRDNILFGKT 689
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALA---FRSPKGVKGSGSVLLNGMPIDAKEMRaisaYVqqddlfiptlTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 690 F--DAQLYKE--VLEACALNDDLSILPAGDqTEVGEKGVT--LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH 763
Cdd:TIGR00955 126 LrmPRRVTKKekRERVDEVLQALGLRKCAN-TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217363546 764 LLhRCILGMLSYTTRLLCT-HR--TEYLERADAVLLMEAGRLIRAGPPSEILPL 814
Cdd:TIGR00955 205 VV-QVLKGLAQKGKTIICTiHQpsSELFELFDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
961-1045 |
2.40e-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: 47.56 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 961 SSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLP 1040
Cdd:cd18557 32 LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVT 111
|
....*
gi 2217363546 1041 FILNI 1045
Cdd:cd18557 112 DNLSQ 116
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
610-812 |
2.57e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.23 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 610 VGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAG---------------------ELHRLRGHvavrgLSKGFGL 668
Cdd:PRK03695 8 VSTRLGPL--SAEVRAGEILHLVGPNGAGKSTLLARMAGllpgsgsiqfagqpleawsaaELARHRAY-----LSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 669 ATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSilpagdqTEVGekgvTLSGGQRARIALARAVYQ------ 742
Cdd:PRK03695 81 PFAMPVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLG-------RSVN----QLSGGEWQRVRLAAVVLQvwpdin 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 743 -EKELYLLDDPLAAVD-ADVA--NHLLHR-CILGMlsytTRLLCTH---RTeyLERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK03695 150 pAGQLLLLDEPMNSLDvAQQAalDRLLSElCQQGI----AVVMSSHdlnHT--LRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
974-1031 |
2.66e-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: 2.66e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 974 IAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSD 1031
Cdd:cd18780 51 VVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSD 108
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
621-812 |
3.25e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.39 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSS-------LLAAIAGELH---------------------------RLRGHVAVRGLSKGF 666
Cdd:PRK13651 28 VEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGTIEwifkdeknkkktkekekvleklviqktRFKKIKKIKEIRRRV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 667 GLATQEPWIQF--ATIRDNILFG-------KTFDAQLYKEVLEACALndDLSILPagdqtevgEKGVTLSGGQRARIALA 737
Cdd:PRK13651 108 GVVFQFAEYQLfeQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQ--------RSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 738 RAVYQEKELYLLDDPLAAVDADVANHLLHrcILGML--SYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLnkQGKTIILVTHDLDNvLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
622-811 |
3.72e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 622 EVKKGMLVGIVGKVGCGKSSL---LAAI----AGELhRLRG-------HVAVRGLSKGFGLATQEPwiqFATI--Rdnil 685
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLarlLTMIetptGGEL-YYQGqdllkadPEAQKLLRQKIQIVFQNP---YGSLnpR---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 686 fgKTFDAQLYkevlEACALNDDLSILPAGDQTEVGEKGVTL------------SGGQRARIALARAVYQEKELYLLDDPL 753
Cdd:PRK11308 109 --KKVGQILE----EPLLINTSLSAAERREKALAMMAKVGLrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 754 AAVDADVANHLLHrciLGM-------LSYttrLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11308 183 SALDVSVQAQVLN---LMMdlqqelgLSY---VFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
629-764 |
3.74e-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: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 629 VGIVGKVGCGKSSLLAAIAGELHRLRGHVAvrgLSKGF--GLATQEPWI-QFATIRDNILFG--------KTFDA----- 692
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKDFNGEAR---PQPGIkvGYLPQEPQLdPTKTVRENVEEGvaeikdalDRFNEisaky 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 693 --------QLYKE------VLEACA---LNDDLSI------LPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLL 749
Cdd:TIGR03719 111 aepdadfdKLAAEqaelqeIIDAADawdLDSQLEIamdalrCPPWDA-----DVTKLSGGERRRVALCRLLLSKPDMLLL 185
|
170
....*....|....*....
gi 2217363546 750 DDPLAAVDAD-VA---NHL 764
Cdd:TIGR03719 186 DEPTNHLDAEsVAwleRHL 204
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
620-768 |
5.20e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.57 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSkgfgLATQEPwiQFAtirdnilfgktfDAQLY---- 695
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP----IRRQRD--EYH------------QDLLYlghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 696 ---KEVLEA-------CALNDDLS---ILPAGDQteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAV 756
Cdd:PRK13538 83 pgiKTELTAlenlrfyQRLHGPGDdeaLWEALAQ--VGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170
....*....|....*.
gi 2217363546 757 D----ADVANHLLHRC 768
Cdd:PRK13538 161 DkqgvARLEALLAQHA 176
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
629-811 |
5.72e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 629 VGIVGKVGCGKSSLLAAI-------AGELH---RLRGHVAVRGLSKGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYKe 697
Cdd:PTZ00243 1339 VGIVGRTGSGKSTLLLTFmrmvevcGGEIRvngREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVdPFLEASSAEVWA- 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 698 VLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELY-LLDDPLAAVDadvanHLLHRCI----LGM 772
Cdd:PTZ00243 1418 ALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFiLMDEATANID-----PALDRQIqatvMSA 1492
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217363546 773 LSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI 811
Cdd:PTZ00243 1493 FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
620-811 |
5.95e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 46.31 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 620 HLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLS--------------KGFGLATQEPWIQF--ATIRDN 683
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyirpvrKRIGMVFQFPESQLfeDTVERE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 684 ILFG-KTFDAQL-------YKEVLEACALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:PRK13646 107 IIFGpKNFKMNLdevknyaHRLLMDLGFSRDVMSQSP-----------FQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217363546 756 VDADvANHLLHRCI--LGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13646 176 LDPQ-SKRQVMRLLksLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
626-818 |
7.31e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 626 GMLVGIVGKVGCGKSSLLAAIAGELH--RLRGHVAVRG------LSKGFGLATQEPWI-QFATIRDNILF------GKTF 690
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNrkptkqILKRTGFVTQDDILyPHLTVRETLVFcsllrlPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 691 DAQlyKEVLEACALNDDLSILPAGDqTEVGEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcI 769
Cdd:PLN03211 174 TKQ--EKILVAESVISELGLTKCEN-TIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL--T 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 770 LGMLSYTTRLLCTHRTEYLERA----DAVLLMEAGRLIRAGPPSEILPLVQAV 818
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQPSSRVyqmfDSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
629-764 |
8.00e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 629 VGIVGKVGCGKSSLLAAIAGELHRLRGHVAvrgLSKGF--GLATQEPwiQF---ATIRDNIL--FGKTFDAQ-LYKEVLE 700
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEGEAR---PAPGIkvGYLPQEP--QLdpeKTVRENVEegVAEVKAALdRFNEIYA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 701 ACALNDDLS------------ILPAGD------QTEV---------GEKGVT-LSGGQRARIALARAVYQEKELYLLDDP 752
Cdd:PRK11819 111 AYAEPDADFdalaaeqgelqeIIDAADawdldsQLEIamdalrcppWDAKVTkLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
170
....*....|..
gi 2217363546 753 laavdadvANHL 764
Cdd:PRK11819 191 --------TNHL 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
621-820 |
8.38e-05 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 46.20 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGeLHRLRGHVA--------------------VRGlsKGFGLATQEPwiqFA-- 678
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGITSgeilfdgedllklsekelrkIRG--REIQMIFQDP---MTsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 679 ----TIRDNI-----LFGKTFDAQLYK---EVLEACALNDDLSIL---PagdqtevGEkgvtLSGGQRARIALARAVYQE 743
Cdd:COG0444 100 npvmTVGDQIaeplrIHGGLSKAEAREraiELLERVGLPDPERRLdryP-------HE----LSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 744 KELYLLDDPLAAVD----ADVANHL--LHRcILGMlSYttrLLCTH-----RteylERADAVLLMEAGRLIRAGPPSEIL 812
Cdd:COG0444 169 PKLLIADEPTTALDvtiqAQILNLLkdLQR-ELGL-AI---LFITHdlgvvA----EIADRVAVMYAGRIVEEGPVEELF 239
|
250
....*....|....*..
gi 2217363546 813 -----P----LVQAVPK 820
Cdd:COG0444 240 enprhPytraLLSSIPR 256
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
286-571 |
8.95e-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: 45.96 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 286 LALGLLKLVGTMLGFSGPLLLSLLV-GFLEEGQEPLSHGLL--YALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNI 362
Cdd:cd18563 2 ILGFLLMLLGTALGLVPPYLTKILIdDVLIQLGPGGNTSLLllLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 363 LYCKALQLGPS---RPPTGEALNLLGTDSERLLNFAgsfheAWGLPlqlaitlYLLYQQVGVAFVGGLI------LALL- 432
Cdd:cd18563 82 LYEHLQRLSLSffdKRQTGSLMSRVTSDTDRLQDFL-----SDGLP-------DFLTNILMIIGIGVVLfslnwkLALLv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 433 LVPVNKVIAT-----RIMASNQEMLQHKDARVK-LVTELLSGIRVIKFCGWEQalgarveacraRELGRLRVI--KYLDA 504
Cdd:cd18563 150 LIPVPLVVWGsyffwKKIRRLFHRQWRRWSRLNsVLNDTLPGIRVVKAFGQEK-----------REIKRFDEAnqELLDA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 505 --ACVYLWAALPVVISIVIFITYVLM----GHQLTATK----VFTA-LALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18563 219 niRAEKLWATFFPLLTFLTSLGTLIVwyfgGRQVLSGTmtlgTLVAfLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
725-788 |
1.10e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217363546 725 TLSGGQRARIALARAVYQEKELYLLDDPlaavdadvANHLLHRCILGMLSYTTR-----LLCTHRTEYL 788
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEP--------TNHLDLHAVLWLETYLLKwpktfIVVSHAREFL 404
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
621-811 |
2.19e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.79 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGeLHR-LRGHVAVRG-----LS-KGFGLATQEPWIQFA--------TIRDNIL 685
Cdd:PRK11153 26 LHIPAGEIFGVIGASGAGKSTLIRCINL-LERpTSGRVLVDGqdltaLSeKELRKARRQIGMIFQhfnllssrTVFDNVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 686 F----GKTFDAQLYK---EVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 758
Cdd:PRK11153 105 LplelAGTPKAEIKArvtELLELVGLSDKADRYPA-----------QLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 759 DVAnhllhRCILGMLSYTTR------LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK11153 174 ATT-----RSILELLKDINRelgltiVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEV 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
601-821 |
3.13e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 43.91 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 601 HGALFSWDPVGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG--LSK--GFGLATQEPWIQ 676
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNV--SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGepLAKlnRAQRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 677 FA------------TIRDNI------LFGKTFDAQLYK--EVLEACALND-DLSILPAgdqtevgekgvTLSGGQRARIA 735
Cdd:PRK10419 93 MVfqdsisavnprkTVREIIreplrhLLSLDKAERLARasEMLRAVDLDDsVLDKRPP-----------QLSGGQLQRVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 736 LARAVYQEKELYLLDDPLAAVDAdvanhLLHRCILGML------SYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPP 808
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDL-----VLQAGVIRLLkklqqqFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPV 236
|
250
....*....|...
gi 2217363546 809 SEILPLVQAVPKA 821
Cdd:PRK10419 237 GDKLTFSSPAGRV 249
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
628-812 |
4.20e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.55 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 628 LVGIVGKVGCGKSSLLAA-------IAGelHRLRGHVAVRGLS-----------KGFGLATQEPWIQFATIRDNILFG-- 687
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTlnrmndkVSG--YRYSGDVLLGGRSifnyrdvlefrRRVGMLFQRPNPFPMSIMDNVLAGvr 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 688 --KTFDAQLYKEVLEAC--------ALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:PRK14271 127 ahKLVPRKEFRGVAQARltevglwdAVKDRLSDSP-----------FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 758 ADVANHlLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 812
Cdd:PRK14271 196 PTTTEK-IEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
623-811 |
6.84e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.82 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 623 VKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHV----------AVRGLSKGFGLATQEPWIQF--ATIRDNILFGKTF 690
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddNFEKLRKHIGIVFQNPDNQFvgSIVKYDVAFGLEN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 691 DAQLYKEVLE--ACALNDDLSILPAGDQTEvgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLL--- 765
Cdd:PRK13648 112 HAVPYDEMHRrvSEALKQVDMLERADYEPN------ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLdlv 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217363546 766 HRciLGMLSYTTRLLCTHR-TEYLErADAVLLMEAGRLIRAGPPSEI 811
Cdd:PRK13648 186 RK--VKSEHNITIISITHDlSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
957-1039 |
8.60e-04 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 42.89 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 957 APNGSSDIRFYLTVyATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACAD 1036
Cdd:cd18573 34 EIFGLSLKTFALAL-LGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVG 112
|
...
gi 2217363546 1037 DSL 1039
Cdd:cd18573 113 KSL 115
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
621-765 |
9.63e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.08 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG---------LSKGFGLAT--QE----PWIqfaTIRDNIL 685
Cdd:COG1129 25 LELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvrfrsprDAQAAGIAIihQElnlvPNL---SVAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 686 FGK------TFD-AQLYKEVLEACA-LndDLSILPAgdqTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVD 757
Cdd:COG1129 102 LGReprrggLIDwRAMRRRARELLArL--GLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
....*...
gi 2217363546 758 ADVANHLL 765
Cdd:COG1129 173 EREVERLF 180
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
628-808 |
1.06e-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: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 628 LVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRG---------LSKGFGLATQEPWI-QFATIRDNILFGKTFDAQLYKE 697
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldaVRQSLGMCPQHNILfHHLTVAEHILFYAQLKGRSWEE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 698 V-LEACALNDDlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYT 776
Cdd:TIGR01257 1038 AqLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP-YSRRSIWDLLLKYRSGR 1111
|
170 180 190
....*....|....*....|....*....|...
gi 2217363546 777 TRLLCTHRTEYLE-RADAVLLMEAGRLIRAGPP 808
Cdd:TIGR01257 1112 TIIMSTHHMDEADlLGDRIAIISQGRLYCSGTP 1144
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
621-757 |
1.07e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 42.80 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSS-------LLAAIAGELH-------RLRGHvAVRGLSKGFGLATQEPwiqFA------TI 680
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTlgrlllrLEEPTSGEILfdgqditGLSGR-ELRPLRRRMQMVFQDP---YAslnprmTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 681 RDNI-----LFGKTFDAQLYKEV---LEACALN-DDLSILPagdqtevGEkgvtLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:COG4608 115 GDIIaeplrIHGLASKAERRERVaelLELVGLRpEHADRYP-------HE----FSGGQRQRIGIARALALNPKLIVCDE 183
|
....*.
gi 2217363546 752 PLAAVD 757
Cdd:COG4608 184 PVSALD 189
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
427-571 |
1.56e-03 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 42.01 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 427 LILALLLVPVNKVIATRIMASnQEMLQHKDARVKlvtELLSGIRVIKFCGWEQALGARVEAcRARELGR--LRVIKylda 504
Cdd:cd18541 151 PLLALLVYRLGKKIHKRFRKV-QEAFSDLSDRVQ---ESFSGIRVIKAFVQEEAEIERFDK-LNEEYVEknLRLAR---- 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363546 505 acvyLWAALPVVISIVIFITYVL---MGHQLTATKVFTALALV------RMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18541 222 ----VDALFFPLIGLLIGLSFLIvlwYGGRLVIRGTITLGDLVafnsylGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
727-788 |
1.69e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217363546 727 SGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHllhrcILGMLSyttRLLCTHRTEYL 788
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQ-----ILALLK---SLQQKHQLAYL 480
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
589-812 |
2.62e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 41.31 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 589 DPPAEPSTVLELHGALFSWdPVGTSLETFisHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGL------ 662
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRV-PGRTLLHPL--SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplesws 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 663 SKGFG-----LATQEPWIQFATIRDNILFGK--------TFDAQLYKEVLEACALnddlsilpagdqteVGEKGV----- 724
Cdd:PRK10575 80 SKAFArkvayLPQQLPAAEGMTVRELVAIGRypwhgalgRFGAADREKVEEAISL--------------VGLKPLahrlv 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 725 -TLSGGQRARIALARAVYQEKELYLLDDPLAAVD----ADVANhLLHRciLGMLSYTTRLLCTHRTEYLER-ADAVLLME 798
Cdd:PRK10575 146 dSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLA-LVHR--LSQERGLTVIAVLHDINMAARyCDYLVALR 222
|
250
....*....|....
gi 2217363546 799 AGRLIRAGPPSEIL 812
Cdd:PRK10575 223 GGEMIAQGTPAELM 236
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
967-1033 |
3.76e-03 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 41.00 E-value: 3.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217363546 967 YLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVA 1033
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVD 107
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
324-571 |
5.23e-03 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 40.49 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 324 LLYALGLAGGAVLGAVLQnqYGYEVY------KVTLQARgavlNILYCKaLQLGP----SRPPTGEALNLLGTDSERLLN 393
Cdd:cd18542 39 WLLALLILGVALLRGVFR--YLQGYLaekasqKVAYDLR----NDLYDH-LQRLSfsfhDKARTGDLMSRCTSDVDTIRR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 394 FAGsfheaWGLPLQLAITLYllyqqvgvaFVGGLI-----------LALLLVPVNKVIATRIMASNQEM---LQHKDARV 459
Cdd:cd18542 112 FLA-----FGLVELVRAVLL---------FIGALIimfsinwkltlISLAIIPFIALFSYVFFKKVRPAfeeIREQEGEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 460 -KLVTELLSGIRVIK-FcgweqalgARveacRARELGRLRVI--KYLDAAC--VYLWA----------ALPVVISIVIFI 523
Cdd:cd18542 178 nTVLQENLTGVRVVKaF--------AR----EDYEIEKFDKEneEYRDLNIklAKLLAkywplmdflsGLQIVLVLWVGG 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2217363546 524 TYVLMGhQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRI 571
Cdd:cd18542 246 YLVING-EITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
621-765 |
7.26e-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: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 621 LEVKKGMLVGIVGKVGCGKSSLLAAIA---------GELHRLRGHVAVRGLS----KGFGLATQE-PWIQFATIRDNILF 686
Cdd:TIGR02633 22 LEVRPGECVGLCGENGAGKSTLMKILSgvyphgtwdGEIYWSGSPLKASNIRdterAGIVIIHQElTLVPELSVAENIFL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 687 G--------KTFDAQLY---KEVLEACALNDDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAA 755
Cdd:TIGR02633 102 GneitlpggRMAYNAMYlraKNLLRELQLDADNVTRPVGD----------YGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170
....*....|
gi 2217363546 756 VDADVANHLL 765
Cdd:TIGR02633 172 LTEKETEILL 181
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
631-751 |
7.30e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363546 631 IVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGfglATQEPWIQF----------ATIRDNILFGKTF--DAQLYKEV 698
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN---NIAKPYCTYighnlglkleMTVFENLKFWSEIynSAETLYAA 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2217363546 699 LEACALNDDLSilpagdqtevgEKGVTLSGGQRARIALARAVYQEKELYLLDD 751
Cdd:PRK13541 108 IHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
724-797 |
9.76e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.11 E-value: 9.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363546 724 VTLSGGQRARIALARAV----YQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLM 797
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| |
