|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
61-1386 |
0e+00 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 847.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 61 PVDNAGFFSFMTLQWLSPLAWRAHKDScLKMEDVWGLSCHEASETNCQRLEWLWHEELKRRGKDGA-------------- 126
Cdd:TIGR00957 203 PESSASFLSRITFWWITGMAVYGYRQP-LEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPVsavygkkdpskpkg 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 127 ------------------------SLSRVFWRFCQTRMLVAIFSLLITMVAGFVGPALLiRALLEFSQCSEVKLLYGLAL 182
Cdd:TIGR00957 282 ssqldaneevealivksphkprkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQIL-SLLIRFVNDPMAPDWQGYFY 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 183 VAGIFLMELTRSWSLAFMWAINYRTAARLRGAALTFAFQKILRLRSTKDVSS--GELVNICASDGQRLYEAVSVGCLLAG 260
Cdd:TIGR00957 361 TGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSStvGEIVNLMSVDAQRFMDLATYINMIWS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 261 GPLVGMLGLTYTTYFLGPTALVGSAIFIIFYPTMMLASRMTAYFRKKCVAVTDRRVRLMNEILGCMKFIKMYCWETPFAN 340
Cdd:TIGR00957 441 APLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLD 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 341 NIQKVRSEERRNLEWAG---CVQSLTLGVAPVVVviaSVCTFTLHMALGYD--LTAAQAFTVVAVFNSMTFALKVTPLAV 415
Cdd:TIGR00957 521 KVEGIRQEELKVLKKSAylhAVGTFTWVCTPFLV---ALITFAVYVTVDENniLDAEKAFVSLALFNILRFPLNILPMVI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 416 RALSEGSVAVKRFQKLFMMEDRELISVKtedpynvvefkdatlawektcgsqtkksRTQLKRGGMkrvlrreklslYIIT 495
Cdd:TIGR00957 598 SSIVQASVSLKRLRIFLSHEELEPDSIE----------------------------RRTIKPGEG-----------NSIT 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 496 EENkgkieepnaehllthmeqespqSTISSTQSIRPplhkTLHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMTLLG 575
Cdd:TIGR00957 639 VHN----------------------ATFTWARDLPP----TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 576 GSVSVNGGFAYVAQQAWILNDSLRENILFGKKYNEEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLA 655
Cdd:TIGR00957 693 GHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLA 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 656 RALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAA--KGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKG 733
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRD 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 734 RDYAAL---FNSVQQENLVRKNLKNKEKAE-KESSP----------------------------QTLHVSNPPK-PDTES 780
Cdd:TIGR00957 853 GAFAEFlrtYAPDEQQGHLEDSWTALVSGEgKEAKLiengmlvtdvvgkqlqrqlsasssdsgdQSRHHGSSAElQKAEA 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 781 KKTD-QLMQAEEKGSGAVAWPVYAAYIKAAGGPLAFIVtILLFLFTTGSIAFSNWWLSYWIRQGSGNSslllgneTAESD 859
Cdd:TIGR00957 933 KEETwKLMEADKAQTGQVELSVYWDYMKAIGLFITFLS-IFLFVCNHVSALASNYWLSLWTDDPMVNG-------TQNNT 1004
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 860 SMRLNphiqyysrVYV---LSMGAALFLKTirgLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMD 936
Cdd:TIGR00957 1005 SLRLS--------VYGalgILQGFAVFGYS---MAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELD 1073
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 937 EVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFSIIPLGAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQG 1016
Cdd:TIGR00957 1074 TVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLG 1153
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1017 LSTIYAYGRGADFIHRYQALLDTNQACQFLFSCAMRWLAVRLDLISISLITTVALLIVLMHGHISPAYAGLALSYAVQLT 1096
Cdd:TIGR00957 1154 VSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVT 1233
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1097 GLFQFTVRLLSETEARFTSVERINHYIKNlESEGPRQITGCpTSSSSWPAEGQITFQDVEMRYRDGLPLVLKNLCFSILP 1176
Cdd:TIGR00957 1234 FYLNWLVRMSSEMETNIVAVERLKEYSET-EKEAPWQIQET-APPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHG 1311
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1177 EETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNLDPWDQYTDAQI 1256
Cdd:TIGR00957 1312 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEV 1391
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1257 WEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGC 1336
Cdd:TIGR00957 1392 WWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC 1471
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1337 TTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTdENSRFHAMMEAA 1386
Cdd:TIGR00957 1472 TVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ-QRGIFYSMAKDA 1520
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
61-1385 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 805.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 61 PVDNAGFFSFMTLQWLSPLAWRAHKDScLKMEDVWGLSCHEASETNCQRLEWLWHEELKR------RGKDgASLSRVFWr 134
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRP-LTEKDVWKLDTWDQTETLYRSFQKCWDEELKKpkpwllRALN-NSLGGRFW- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 135 fcqtrmLVAIFSLLiTMVAGFVGPALLIRaLLEFSQCSE---VKLLYGLALVAGIFLMELTRSWSLAFMwainYRTAARL 211
Cdd:PLN03130 305 ------LGGFFKIG-NDLSQFVGPLLLNL-LLESMQNGEpawIGYIYAFSIFVGVVLGVLCEAQYFQNV----MRVGFRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 212 RGAALTFAFQKILRL--RSTKDVSSGELVNICASDGQRLYEAVSVGCLLAGGPLVGMLGLTYTTYFLGPTALVGSAIFII 289
Cdd:PLN03130 373 RSTLVAAVFRKSLRLthEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 290 FYPTM-MLASRMTaYFRKKCVAVTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEER---RNLEWAGCVQSLTLG 365
Cdd:PLN03130 453 MFPIQtFIISKMQ-KLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELswfRKAQLLSAFNSFILN 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 366 VAPVVVVIASVCTFTLhmaLGYDLTAAQAFTVVAVFNSMTFALKVTPLAVRALSEGSVAVKRFQKLFMMEDRELI---SV 442
Cdd:PLN03130 532 SIPVLVTVVSFGVFTL---LGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLpnpPL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 443 KTEDPynVVEFKDATLAWEKtcgsqtkksrtqlkrggmkrvlrreklslyiiteenkgKIEEPnaehllthmeqespqst 522
Cdd:PLN03130 609 EPGLP--AISIKNGYFSWDS--------------------------------------KAERP----------------- 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 523 isstqsirpplhkTLHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQM-TLLGGSVSVNGGFAYVAQQAWILNDSLREN 601
Cdd:PLN03130 632 -------------TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIRGTVAYVPQVSWIFNATVRDN 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 602 ILFGKKYNEEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSR 681
Cdd:PLN03130 699 ILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQ 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 682 LFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALF-NSVQQENLVRKNlkNKEKAE 760
Cdd:PLN03130 779 VFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMeNAGKMEEYVEEN--GEEEDD 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 761 KESSPQTLHVSNPPKPDTESKKTDQ------LMQAEEKGSGAVAWPVYAAYIKAAGGplAFIVTILlFLFTTGSIAF--- 831
Cdd:PLN03130 857 QTSSKPVANGNANNLKKDSSSKKKSkegksvLIKQEERETGVVSWKVLERYKNALGG--AWVVMIL-FLCYVLTEVFrvs 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 832 SNWWLSYWIRQGSGNSSLLLgnetaesdsmrlnphiqYYSRVY-VLSMGAALfLKTIRGLVFVKCTVRAASVLHDKLFKT 910
Cdd:PLN03130 934 SSTWLSEWTDQGTPKTHGPL-----------------FYNLIYaLLSFGQVL-VTLLNSYWLIMSSLYAAKRLHDAMLGS 995
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 911 LLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFSIIPL-----GAFLFIVN 985
Cdd:PLN03130 996 ILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLlvlfyGAYLYYQS 1075
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 986 RIsrvliRELKRLENISQSPFTSHITSSLQGLSTIYAY---GRGADFIHRYqalLDTNQACQFLFSCAMRWLAVRLDLIS 1062
Cdd:PLN03130 1076 TA-----REVKRLDSITRSPVYAQFGEALNGLSTIRAYkayDRMAEINGRS---MDNNIRFTLVNMSSNRWLAIRLETLG 1147
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1063 ISLITTVALLIVLMHGHIS--PAYA---GLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHYIkNLESEGPRQITGc 1137
Cdd:PLN03130 1148 GLMIWLTASFAVMQNGRAEnqAAFAstmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYI-DLPSEAPLVIEN- 1225
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1138 PTSSSSWPAEGQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAH 1217
Cdd:PLN03130 1226 NRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISK 1305
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1218 IGLEDLRSKLSVIPQEPVLFIGTVRSNLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCV 1297
Cdd:PLN03130 1306 FGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSL 1385
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1298 ARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTDENS 1377
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
....*...
gi 1207190976 1378 RFHAMMEA 1385
Cdd:PLN03130 1466 AFSKMVQS 1473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
61-1385 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 768.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 61 PVDNAGFFSFMTLQWLSPLAWRAHKDScLKMEDVWGLSCHEASETNCQRLEWLWHEElKRRGKD------GASLSRVFWr 134
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKP-ITEKDVWQLDQWDQTETLIKRFQRCWTEE-SRRPKPwllralNNSLGGRFW- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 135 fcqtrmLVAIFSLLITMvAGFVGPAL---LIRALLEfSQCSEVKLLYGLALVAGIFLMELTRSWSLAFMWainyRTAARL 211
Cdd:PLN03232 305 ------LGGIFKIGHDL-SQFVGPVIlshLLQSMQE-GDPAWVGYVYAFLIFFGVTFGVLCESQYFQNVG----RVGFRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 212 RGAALTFAFQKILRL--RSTKDVSSGELVNICASDGQRLYEAVSVGCLLAGGPLVGMLGLTYTTYFLGPTALVGSAIFII 289
Cdd:PLN03232 373 RSTLVAAIFHKSLRLthEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 290 FYPTMMLASRMTAYFRKKCVAVTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEER---RNLEWAGCVQSLTLGV 366
Cdd:PLN03232 453 LIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELswfRKAQLLSAFNSFILNS 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 367 APVVVVIASVCTFTLhmaLGYDLTAAQAFTVVAVFNSMTFALKVTPLAVRALSEGSVAVKRFQKLFMMEDRELISVKTED 446
Cdd:PLN03232 533 IPVVVTLVSFGVFVL---LGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQ 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 447 P-YNVVEFKDATLAWEKtcgsqtkksrtqlkrggmkrvlrreklslyiiteenkgKIEEPnaehllthmeqespqstiss 525
Cdd:PLN03232 610 PgAPAISIKNGYFSWDS--------------------------------------KTSKP-------------------- 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 526 tqsirpplhkTLHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMTLL-GGSVSVNGGFAYVAQQAWILNDSLRENILF 604
Cdd:PLN03232 632 ----------TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQVSWIFNATVRENILF 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 605 GKKYNEEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFH 684
Cdd:PLN03232 702 GSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 685 SAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFNSVQQENLVRKNLKNKEKAEKESS 764
Cdd:PLN03232 782 SCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDENILKLGP 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 765 PQTLHVSNPPKPDTESKKTDQ--LMQAEEKGSGAVAWPVYAAYIKAAGGPLAFIVTILLFLFTTGSIAFSNWWLSYWirq 842
Cdd:PLN03232 862 TVTIDVSERNLGSTKQGKRGRsvLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIW--- 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 843 gsgnsslllgneTAESDSMRLNPhiQYYSRVYVLSMGAALFLKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTT 922
Cdd:PLN03232 939 ------------TDQSTPKSYSP--GFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTN 1004
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 923 PLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFSIIPLGAFLFIVNRISRVLIRELKRLENIS 1002
Cdd:PLN03232 1005 PTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVT 1084
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1003 QSPFTSHITSSLQGLSTIYAYgRGADFIHRYQA-LLDTNQACQFLFSCAMRWLAVRLDLISISLITTVALLIVLMHGHIS 1081
Cdd:PLN03232 1085 RSPIYAQFGEALNGLSSIRAY-KAYDRMAKINGkSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAE 1163
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1082 -----PAYAGLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHYIkNLESEGPrQITGCPTSSSSWPAEGQITFQDVE 1156
Cdd:PLN03232 1164 nqagfASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYI-DLPSEAT-AIIENNRPVSGWPSRGSIKFEDVH 1241
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1157 MRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVL 1236
Cdd:PLN03232 1242 LRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVL 1321
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1237 FIGTVRSNLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAA 1316
Cdd:PLN03232 1322 FSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1317 IDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTDENSRFHAMMEA 1385
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
178-1385 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 679.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 178 YGLALVAGIFLMELTRSWSLAFMWAINYRTAARLRGAALTFAFQKIL----RLRSTKDVSSGELVNICASDGQRLYEAVS 253
Cdd:PTZ00243 283 RGLGLVLTLFLTQLIQSVCLHRFYYISIRCGLQYRSALNALIFEKCFtissKSLAQPDMNTGRIINMMSTDVERINSFMQ 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 254 VGCLLAGGPLVGMLGLTYTTYFLGPTALVGSAIFIIFYPTMMLASRMTAYFRKKCVAVTDRRVRLMNEILGCMKFIKMYC 333
Cdd:PTZ00243 363 YCMYLWSSPMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 334 WETPFANNIQKVRSEE---RRNLEWAGCVQSLTLGVAPVVVvIASVctFTLHMALGYDLTAAQAFTVVAVFNSMTFALKV 410
Cdd:PTZ00243 443 WEPCFVANIEDKRARElryLRDVQLARVATSFVNNATPTLM-IAVV--FTVYYLLGHELTPEVVFPTIALLGVLRMPFFM 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 411 TPLAVRALSEGSVAVKRFQKLFMMEDRELISVKtedpyNVVEFKDATLAWEKTCGS------------------QTKKSR 472
Cdd:PTZ00243 520 IPWVFTTVLQFLVSIKRISTFLECDNATCSTVQ-----DMEEYWREQREHSTACQLaavlenvdvtafvpvklpRAPKVK 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 473 TQLkrggMKRVLRReklslyIITEENKGKIEEPNAEHLLTHMEQESPQSTI----------------SSTQSIRPPLHKT 536
Cdd:PTZ00243 595 TSL----LSRALRM------LCCEQCRPTKRHPSPSVVVEDTDYGSPSSASrhiveggtgggheatpTSERSAKTPKMKT 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 537 -----------LHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMTLLGGSVSVNGGFAYVAQQAWILNDSLRENILFG 605
Cdd:PTZ00243 665 ddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFF 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 606 KKYNEEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHS 685
Cdd:PTZ00243 745 DEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEE 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 686 AIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRdYAALFNSVQQENLVRKNLKNKEKAEKESSP 765
Cdd:PTZ00243 825 CFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTSL-YATLAAELKENKDSKEGDADAEVAEVDAAP 903
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 766 Q--TLHVSNPPKPDTESKKTD---------QLMQAEEKGSGAVAWPVYAAYIKAAGGPLAFIVTILLFLFTTGSIAFSNW 834
Cdd:PTZ00243 904 GgaVDHEPPVAKQEGNAEGGDgaaldaaagRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGV 983
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 835 WLSYWI--RQGSGNSSLLLgnetaesdsmrlnphiqyysrVYVLSMGAALFLKTIRGLVFVKCTVRAASVLHDKLFKTLL 912
Cdd:PTZ00243 984 WLSMWStrSFKLSAATYLY---------------------VYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVS 1042
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 913 LSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFSIIPLGAFLFIVNRISRVLI 992
Cdd:PTZ00243 1043 RGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSAN 1122
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 993 RELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLFSCAMRWLAVRLDLISISLITTVALL 1072
Cdd:PTZ00243 1123 REIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALI 1202
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1073 IV----LMHGHISPAYAGLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHYIKNLESEG-----------------P 1131
Cdd:PTZ00243 1203 GVigtmLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEDmpeldeevdalerrtgmA 1282
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1132 RQITGC-------PTSSSSWPAE-GQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAEL 1203
Cdd:PTZ00243 1283 ADVTGTvviepasPTSAAPHPVQaGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV 1362
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1204 SRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDN 1283
Cdd:PTZ00243 1363 CGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEG 1442
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1284 GENFSVGERQLLCVARALL-RHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQI 1362
Cdd:PTZ00243 1443 GSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAV 1522
|
1290 1300
....*....|....*....|...
gi 1207190976 1363 LEFDTPSNLLTDENSRFHAMMEA 1385
Cdd:PTZ00243 1523 AEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
811-1123 |
2.32e-157 |
|
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: 476.28 E-value: 2.32e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 811 GPLAFIVTILLFLFTTGSIAFSNWWLSYWIRQGSGNSSLLLGNETAESDSMRLNPHIQYYSRVYVLSMGAALFLKTIRGL 890
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 891 VFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWF 970
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 971 LFSIIPLGAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLFSCA 1050
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1051 MRWLAVRLDLISISLITTVALLIVLMHGHISPAYAGLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHYI 1123
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
61-1387 |
1.48e-138 |
|
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: 462.07 E-value: 1.48e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 61 PVDNAGFFSFMTLQWLSPLAWRAHKDScLKMEDVWGLSCHEASETNCQRLEWLWHEEL---KRRGKDGASLSRVF-WRFc 136
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQK-LELSDIYQIPSFDSADNLSERLEREWDRELasaKKNPKLLNALRRCFfWRF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 137 qtrMLVAIFsLLITMVAGFVGPALLIRALLEFS--QCSEVKLLYGLALvaGIFLMELTRSWSLAFMWAINYRTAARLRGA 214
Cdd:TIGR01271 83 ---VFYGIL-LYFGEATKAVQPLLLGRIIASYDpfNAPEREIAYYLAL--GLCLLFIVRTLLLHPAIFGLHHLGMQMRIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 215 ALTFAFQKILRL--RSTKDVSSGELVNICASDGQRLYEAVSVGCLLAGGPL--VGMLGLTYTtyFLGPTALVGSAIFIIF 290
Cdd:TIGR01271 157 LFSLIYKKTLKLssRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLqvILLMGLIWE--LLEVNGFCGLGFLILL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 291 YPTMMLASRMTAYFRKKCVAVTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEERRNLEWAGCVQ---SLTLGVA 367
Cdd:TIGR01271 235 ALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRyfySSAFFFS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 368 PVVVVIASVCTFtlhmALGYDLTAAQAFTVVAVfnSMTFALKVT---PLAVRALSEGSVAVKRFQKLFMMEDRELISvkt 444
Cdd:TIGR01271 315 GFFVVFLSVVPY----ALIKGIILRRIFTTISY--CIVLRMTVTrqfPGAIQTWYDSLGAITKIQDFLCKEEYKTLE--- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 445 edpYNV----VEFKDATLAWEKTCGSQTKKsrtqlkrggmkrvlrreklslyiITEENKGKiEEPNAEHLLTHmeqespq 520
Cdd:TIGR01271 386 ---YNLttteVEMVNVTASWDEGIGELFEK-----------------------IKQNNKAR-KQPNGDDGLFF------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 521 STISstqsirppLHKT--LHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMTLLGGSVSVNGGFAYVAQQAWILNDSL 598
Cdd:TIGR01271 432 SNFS--------LYVTpvLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTI 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 599 RENILFGKKYNEEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARV 678
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 679 GSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALF--------------NSVQ 744
Cdd:TIGR01271 584 EKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerrNSIL 663
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 745 QENLVRKNLKNK-------------------EKAEKESSPQTLHVSNP-------------PKPDTESKKTD-------- 784
Cdd:TIGR01271 664 TETLRRVSIDGDstvfsgpetikqsfkqpppEFAEKRKQSIILNPIASarkfsfvqmgpqkAQATTIEDAVRepserkfs 743
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 785 ---------------------------------QLMQAEEKGSG------------------------------------ 795
Cdd:TIGR01271 744 lvpedeqgeeslprgnqyhhglqhqaqrrqsvlQLMTHSNRGENrreqlqtsfrkkssitqqnelaseldiysrrlskds 823
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 796 --------------------------AVAWPVYAAYIkAAGGPLAFiVTILLFLFTTGSIAFSnwWLSYWIRQGSGNSSL 849
Cdd:TIGR01271 824 vyeiseeineedlkecfaderenvfeTTTWNTYLRYI-TTNRNLVF-VLIFCLVIFLAEVAAS--LLGLWLITDNPSAPN 899
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 850 LLGNETAESDSMR------LNPHIQYYS-RVYVLSMGAALFLKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTT 922
Cdd:TIGR01271 900 YVDQQHANASSPDvqkpviITPTSAYYIfYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTM 979
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 923 PLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFSIIPLgAFLFIVNRISRVLI-RELKRLENI 1001
Cdd:TIGR01271 980 KAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPV-AVIFIMLRAYFLRTsQQLKQLESE 1058
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1002 SQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLFSCAMRWLAVRLDLISISLITTVALLIVLMHGhIS 1081
Cdd:TIGR01271 1059 ARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQ-DG 1137
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1082 PAYAGLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHYIkNLESEGPRQITGC-------------PTSSSSWPAEG 1148
Cdd:TIGR01271 1138 EGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFI-DLPQEEPRPSGGGgkyqlstvlvienPHAQKCWPSGG 1216
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1149 QITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAElSRGSIIIDGVNIAHIGLEDLRSKLS 1228
Cdd:TIGR01271 1217 QMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFG 1295
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1229 VIPQEPVLFIGTVRSNLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKIL 1308
Cdd:TIGR01271 1296 VIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1309 LLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTdENSRFHAMMEAAE 1387
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLN-ETSLFKQAMSAAD 1453
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
142-428 |
1.66e-138 |
|
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: 425.44 E-value: 1.66e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 142 VAIFSLLITMVAGFVGPALLIRALLEFSQCSEVKLLYGLALVAGIFLMELTRSWSLAFMWAINYRTAARLRGAALTFAFQ 221
Cdd:cd18592 1 FSILLLLISLIFGFIGPTILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 222 KILRLRSTKDVSSGELVNICASDGQRLYEAVSVGCLLAGGPLVGMLGLTYTTYFLGPTALVGSAIFIIFYPTMMLASRMT 301
Cdd:cd18592 81 KILRLRSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 302 AYFRKKCVAVTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEERRNLEWAGCVQSLTLGVAPVVVVIASVCTFTL 381
Cdd:cd18592 161 GKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1207190976 382 HMALGYDLTAAQAFTVVAVFNSMTFALKVTPLAVRALSEGSVAVKRF 428
Cdd:cd18592 241 HVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1148-1368 |
6.71e-129 |
|
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: 396.86 E-value: 6.71e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1148 GQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKL 1227
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPVLFIGTVRSNLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKI 1307
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1308 LLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTP 1368
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
873-1385 |
7.21e-107 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 351.00 E-value: 7.21e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 873 VYVLSMGAALFLKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQN 952
Cdd:COG1132 66 LLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 953 VTLVLFCLGVVGAVFPWF-LFSIIPLGAFLFIVNRISRvLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIH 1031
Cdd:COG1132 146 VVTLIGALVVLFVIDWRLaLIVLLVLPLLLLVLRLFGR-RLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1032 RYQALLDTNQACQFLFSCAMRWLAVRLDLISISLITTVALLIVLM--HGHISPAYAGLALSYAVQLTGLFQFTVRLLSET 1109
Cdd:COG1132 225 RFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLvlSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1110 EARFTSVERINHYIknlesEGPRQITGCPTSSSSWPAEGQITFQDVEMRYRDGLPlVLKNLCFSILPEETIGIVGRTGSG 1189
Cdd:COG1132 305 QRALASAERIFELL-----DEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1190 KSSLgVALF-RLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNL---DPwdQYTDAQIWEALEKTHI 1265
Cdd:COG1132 379 KSTL-VNLLlRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQA 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1266 KDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRL 1345
Cdd:COG1132 456 HEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRL 535
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1207190976 1346 NTVLGCNRIMVLDQGQILEFDTPSNLLtDENSRFHAMMEA 1385
Cdd:COG1132 536 STIRNADRILVLDDGRIVEQGTHEELL-ARGGLYARLYRL 574
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
815-1123 |
8.41e-100 |
|
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: 320.99 E-value: 8.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 815 FIVTILLFLFTTGSIAFSNWWLSYWIRQGSGNSSLLLGnetaesdsmrlnphiQYYSRVYVLSMGAALFLKTIRGLVFVK 894
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSG---------------YYLGVYAALLVLASVLLVLLRWLLFVL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 895 CTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFSI 974
Cdd:cd18580 66 AGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 975 IPLGAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLFSCAMRWL 1054
Cdd:cd18580 146 PPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1055 AVRLDLISISLITTVALLIVLMHGHISPAYAGLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHYI 1123
Cdd:cd18580 226 GLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
874-1372 |
2.30e-95 |
|
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: 323.32 E-value: 2.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 874 YVLSMGAALF------LKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSkDMDEVDVRLAMQAE 947
Cdd:COG2274 196 WVLAIGLLLAllfeglLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 948 MLLQNVTLVLFCLGVVGAVFPWF----LFSIIPLGAFLFIVNRISRVLIRELKRLENISQSpftsHITSSLQGLSTIYAY 1023
Cdd:COG2274 275 TALLDLLFVLIFLIVLFFYSPPLalvvLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQS----LLVETLRGIETIKAL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1024 GRGADFIHRYQALLDTNQACQFlfscAMRWLAVRLDLIS--ISLITTVALLIV----LMHGHISP-------AYAGLALS 1090
Cdd:COG2274 351 GAESRFRRRWENLLAKYLNARF----KLRRLSNLLSTLSglLQQLATVALLWLgaylVIDGQLTLgqliafnILSGRFLA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1091 YAVQLTGLFQftvRLLsetEARfTSVERINHyIKNLESEGPRQITGCPTSssswPAEGQITFQDVEMRYRDGLPLVLKNL 1170
Cdd:COG2274 427 PVAQLIGLLQ---RFQ---DAK-IALERLDD-ILDLPPEREEGRSKLSLP----RLKGDIELENVSFRYPGDSPPVLDNI 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1171 CFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNLDPWD- 1249
Cdd:COG2274 495 SLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDp 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1250 QYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTI 1329
Cdd:COG2274 575 DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL 654
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1207190976 1330 RSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLL 1372
Cdd:COG2274 655 RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1144-1368 |
1.23e-92 |
|
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: 297.40 E-value: 1.23e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1144 WPAEGQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDL 1223
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1224 RSKLSVIPQEPVLFIGTVRSNLDPWDQYTDAQIWEALekthikdmvsqlpnslhsEVTDNGENFSVGERQLLCVARALLR 1303
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1304 HSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTP 1368
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
560-719 |
5.29e-91 |
|
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: 292.84 E-value: 5.29e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGGFAYVAQQAWILNDSLRENILFGKKYNEEKYNAVLEACCLFPDIIELPYGDMTEIGE 639
Cdd:cd03250 44 KSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 640 RGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPA-AKGKTVIFVTHQLQYLPECDDVVLMKDG 718
Cdd:cd03250 124 KGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLlLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
.
gi 1207190976 719 Q 719
Cdd:cd03250 204 R 204
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
815-1122 |
2.39e-86 |
|
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: 283.60 E-value: 2.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 815 FIVTILLFLFTTGSIAFSNWWLSYWIrqgsgNSSLLLGNETAESDSMRLNphiqyysrVY-VLSMGAALFLkTIRGLVFV 893
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWS-----DDPALNGTQDTEQRDYRLG--------VYgALGLGQAIFV-FLGSLALA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 894 KCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFS 973
Cdd:cd18603 67 LGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 974 IIPLGAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLFSCAMRW 1053
Cdd:cd18603 147 IIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRW 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1054 LAVRLDLISISLITTVALLIVLMHGHISPAYAGLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHY 1122
Cdd:cd18603 227 LAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
815-1122 |
5.99e-83 |
|
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: 273.58 E-value: 5.99e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 815 FIVTILLFLFTTGSIAFSNWWLSYWIRQGSGNSSlllgnetaesdsmrlnphiQYYSRVYV-LSMGAALFLkTIRGLVFV 893
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLSQ-------------------GFYIGIYAgLGVLQAIFL-FLFGLLLA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 894 KCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFS 973
Cdd:cd18606 61 YLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 974 IIPLGAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLFSCAMRW 1053
Cdd:cd18606 141 LPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRW 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1054 LAVRLDLISISLITTVALLIVLMHGHISPAYAGLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHY 1122
Cdd:cd18606 221 LAIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
815-1123 |
1.82e-78 |
|
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: 261.25 E-value: 1.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 815 FIVTILLFLFTTGSIAFSNWWLSYWIRQGSGNSSLLLGNetaesdsmrlnPHIQYYSRVYVLSMGAALFLKTIRGLVFVK 894
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSE-----------VSVLYYLGIYALISLLSVLLGTLRYLLFFF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 895 CTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFSI 974
Cdd:cd18604 70 GSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 975 IPLGAFLFivnRISRVLI---RELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLFSCAM 1051
Cdd:cd18604 150 VVLAALYV---YIGRLYLrasRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 1052 RWLAVRLDLISiSLITTVALLIVLMHGHISPAYAGLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHYI 1123
Cdd:cd18604 227 RWLSVRIDLLG-ALFSFATAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1148-1385 |
1.37e-76 |
|
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: 254.45 E-value: 1.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1148 GQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKL 1227
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPVLFIGTVRSNLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKI 1307
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 1308 LLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTDENSRFHAMMEA 1385
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRT 255
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
815-1123 |
4.77e-75 |
|
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: 251.68 E-value: 4.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 815 FIVTILLFLFTTGSIAFSNWWLSYWIrqgsgnsslllgNETAESDSMRLNPHIQYYSRVYVLSMGAALFLKTIRGLVFVK 894
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWV------------SHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 895 CTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFSI 974
Cdd:cd18605 69 GGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 975 IPLGAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLFSCAMRWL 1054
Cdd:cd18605 149 LPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 1055 AVRLDLISISLITTVALLIVLMH---GHISPAYAGLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHYI 1123
Cdd:cd18605 229 SIRLQLLGVLIVTFVALTAVVQHffgLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
815-1122 |
8.71e-74 |
|
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: 248.29 E-value: 8.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 815 FIVTILLFLFTTGSIAFSNWWLSYWIRQGSGNSSLLLGNEtaeSDSMRLNPHIqYYSRVYVLSMGAALFLKTIRGLVFVK 894
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNIT---SSSLEDDEVS-YYISVYAGLSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 895 CTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFSI 974
Cdd:cd18602 77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 975 IPLGAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLFSCAMRWL 1054
Cdd:cd18602 157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1055 AVRLDLIS--ISLITTVALLIVLMHGHISPAYAGLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHY 1122
Cdd:cd18602 237 GIRLDYLGavIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
804-1372 |
1.35e-71 |
|
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: 250.83 E-value: 1.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 804 AYIKAAGGPLAfiVTILLFLFTTGSIAFSNWWLSYWIrqgsgnSSLLLGNETAESdsmrlnphiqyySRVYVLSMGAALF 883
Cdd:COG4988 10 RLARGARRWLA--LAVLLGLLSGLLIIAQAWLLASLL------AGLIIGGAPLSA------------LLPLLGLLLAVLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 884 LKTI----RGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFskdMDEVDvrlAMQ---AEMLLQNVTLV 956
Cdd:COG4988 70 LRALlawlRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLL---TEGVE---ALDgyfARYLPQLFLAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 957 LFCLGVVGAVFP--W-----FLFSI--IPLgaFLFIVNRISRVLIRE-LKRLENISqspftSHITSSLQGLSTIYAYGRG 1026
Cdd:COG4988 144 LVPLLILVAVFPldWlsgliLLVTAplIPL--FMILVGKGAAKASRRqWRALARLS-----GHFLDRLRGLTTLKLFGRA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1027 adfiHRYQALLdtNQACQFLFSCAMRWLavRLDLISIS---LITT--VALLIVlmhghispaYAGLALSYAvQLTgLFQ- 1100
Cdd:COG4988 217 ----KAEAERI--AEASEDFRKRTMKVL--RVAFLSSAvleFFASlsIALVAV---------YIGFRLLGG-SLT-LFAa 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1101 FTVRLLSeTE-------------ARFTSV---ERINHYiknLESEGPRQITGcpTSSSSWPAEGQITFQDVEMRYRDGLP 1164
Cdd:COG4988 278 LFVLLLA-PEfflplrdlgsfyhARANGIaaaEKIFAL---LDAPEPAAPAG--TAPLPAAGPPSIELEDVSFSYPGGRP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1165 lVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSN 1244
Cdd:COG4988 352 -ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIREN 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1245 L---DPwdQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTET 1321
Cdd:COG4988 431 LrlgRP--DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAET 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1322 DRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLL 1372
Cdd:COG4988 509 EAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
811-1122 |
5.00e-71 |
|
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: 240.69 E-value: 5.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 811 GPLAFIVTILLFLFTTGSIAFSNWWLSYW---IRQGSGNSSLLLGNETAESDSMRLNphIQYYSRVYVLSMGAALFLKTI 887
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWanlEEKLNDTTDRVQGENSTNVDIEDLD--RDFNLGIYAGLTAATFVFGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 888 RGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVF 967
Cdd:cd18601 79 RSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 968 PWFLFSIIPLGAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLF 1047
Cdd:cd18601 159 PWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLF 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1048 SCAMRWLAVRLDLISISLITTVALLIVLMHGHISPAYAGLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHY 1122
Cdd:cd18601 239 LATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
896-1384 |
4.51e-70 |
|
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: 246.60 E-value: 4.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 896 TVRAASVLHDKLFKTLL-LSPMRF--FDTtplGRILNRFSKDMDEVD---VRLAMQAemllqnVTLVLFCLGVVGAVFpW 969
Cdd:COG4987 83 TLRLLADLRVRLYRRLEpLAPAGLarLRS---GDLLNRLVADVDALDnlyLRVLLPL------LVALLVILAAVAFLA-F 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 970 FLFSI-IPLGAFLF--------IVNRISRVLIRELKRLENIsqspFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTN 1040
Cdd:COG4987 153 FSPALaLVLALGLLlaglllplLAARLGRRAGRRLAAARAA----LRARLTDLLQGAAELAAYGALDRALARLDAAEARL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1041 QACQflfSCAMRWLAVRLDLIS-ISLITTVALLIVLM----HGHISPAYAG------LALSYAVQ-LTGLFQFTVRLLSe 1108
Cdd:COG4987 229 AAAQ---RRLARLSALAQALLQlAAGLAVVAVLWLAAplvaAGALSGPLLAllvlaaLALFEALApLPAAAQHLGRVRA- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1109 tearftSVERINhyikNLESEGPRQITgcPTSSSSWPAEGQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGS 1188
Cdd:COG4987 305 ------AARRLN----ELLDAPPAVTE--PAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1189 GKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNL---DPwdQYTDAQIWEALEKTHI 1265
Cdd:COG4987 373 GKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1266 KDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRL 1345
Cdd:COG4987 451 GDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRL 530
|
490 500 510
....*....|....*....|....*....|....*....
gi 1207190976 1346 NTVLGCNRIMVLDQGQILEFDTPSNLLtDENSRFHAMME 1384
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGTHEELL-AQNGRYRQLYQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1148-1372 |
1.66e-69 |
|
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: 232.89 E-value: 1.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1148 GQITFQDVEMRYRDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKL 1227
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPVLFIGTVRSNLDPWDQY-TDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSK 1306
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 1307 ILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLL 1372
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
899-1382 |
1.45e-66 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 236.54 E-value: 1.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 899 AASVLHD---KLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVdVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFSII 975
Cdd:TIGR02203 82 SNKVVRDirvRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQV-ASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 976 ----PLGAFLfiVNRISRVLIRELKRLENiSQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLFSCAM 1051
Cdd:TIGR02203 161 vvmlPVLSIL--MRRVSKRLRRISKEIQN-SMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1052 RWLAVRLDLIsISLITTVALLIVLMHGHISPAYAGLALSYAVQLTGLFQfTVRLLSETEARFTSVERINHYIKNLESEGP 1131
Cdd:TIGR02203 238 SISSPITQLI-ASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIR-PLKSLTNVNAPMQRGLAAAESLFTLLDSPP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1132 RQITGcptSSSSWPAEGQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIID 1211
Cdd:TIGR02203 316 EKDTG---TRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1212 GVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNL---DPwDQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFS 1288
Cdd:TIGR02203 393 GHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLS 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1289 VGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTP 1368
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTH 551
|
490
....*....|....*.
gi 1207190976 1369 SNLLTDEN--SRFHAM 1382
Cdd:TIGR02203 552 NELLARNGlyAQLHNM 567
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
142-427 |
1.71e-65 |
|
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: 223.90 E-value: 1.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 142 VAIFSLLITMVAGFVGPaLLIRALLEF-SQCSEVKLLYGLALVAGIFLMELTRSWSLAFMWAINYRTAARLRGAALTFAF 220
Cdd:cd18579 1 LAGLLKLLEDLLSLAQP-LLLGLLISYlSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 221 QKILRLRST--KDVSSGELVNICASDGQRLYEAVSVGCLLAGGPLVGMLGLTYTTYFLGPTALVGSAIFIIFYPTMMLAS 298
Cdd:cd18579 80 RKALRLSSSarQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 299 RMTAYFRKKCVAVTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEERRNLEWAGCVQSLTLGVAPVVVVIASVCT 378
Cdd:cd18579 160 KLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLAT 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1207190976 379 FTLHMALGYDLTAAQAFTVVAVFNSMTFALKVTPLAVRALSEGSVAVKR 427
Cdd:cd18579 240 FATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKR 288
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1150-1385 |
2.52e-64 |
|
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: 218.25 E-value: 2.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSV 1229
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFIGTVRSNLdpwdQY-----TDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRH 1304
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1305 SKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLtDENSRFHAMME 1384
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMWK 234
|
.
gi 1207190976 1385 A 1385
Cdd:cd03253 235 A 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1150-1375 |
2.43e-61 |
|
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: 209.78 E-value: 2.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSV 1229
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFIGTVRSNLdpwdQY-----TDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRH 1304
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1305 SKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTDE 1375
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1150-1361 |
4.88e-61 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 206.08 E-value: 4.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSV 1229
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFIGTVRSNLdpwdqytdaqiwealekthikdmvsqlpnslhsevtdngenFSVGERQLLCVARALLRHSKILL 1309
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 1310 LDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQ 1361
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1150-1386 |
3.49e-58 |
|
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: 200.84 E-value: 3.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRY--RDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKL 1227
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPVLFIGTVRSNL-----DPwdqyTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALL 1302
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1303 RHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTdENSRFHAM 1382
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKL 234
|
....
gi 1207190976 1383 MEAA 1386
Cdd:cd03249 235 VKAQ 238
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1148-1387 |
2.80e-56 |
|
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: 196.61 E-value: 2.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1148 GQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAElSRGSIIIDGVNIAHIGLEDLRSKL 1227
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPVLFIGTVRSNLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKI 1307
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1308 LLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLtDENSRFHAMMEAAE 1387
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL-NEKSHFKQAISPSD 238
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
123-742 |
5.17e-56 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 205.40 E-value: 5.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 123 KDGASLSRVFWRFCQT---RMLVAIFSLLITMVAGFVGPALLIRALLEFSQCSEVKLL--YGLALVAGIFLMELTRSWSL 197
Cdd:COG1132 3 KSPRKLLRRLLRYLRPyrgLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALllLLLLLLGLALLRALLSYLQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 198 AFMWAINYRTAARLRGAAltfaFQKILRLRST--KDVSSGELVNICASDGQRLYEAVSVGCLLAGGPLVGMLGLTYTTYF 275
Cdd:COG1132 83 YLLARLAQRVVADLRRDL----FEHLLRLPLSffDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 276 LGP--TALVGSAIFIIFYPTMMLASRMTAYFRKkcvaVTDRRVRL---MNEILGCMKFIKMYCWETPFANNIQKVRSEER 350
Cdd:COG1132 159 IDWrlALIVLLVLPLLLLVLRLFGRRLRKLFRR----VQEALAELngrLQESLSGIRVVKAFGREERELERFREANEELR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 351 RNLEWAGCVQSLTLGVAPVV--VVIASVCTFTLHMALGYDLTAAQAFTVVAVFNSMTFALKVTPLAVRALSEGSVAVKRF 428
Cdd:COG1132 235 RANLRAARLSALFFPLMELLgnLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 429 QKLfMMEDRELISVKTEDPYNV----VEFKDATLAwektcgsqtkksrtqlkrggmkrvlrreklslYiiteenkgkiee 504
Cdd:COG1132 315 FEL-LDEPPEIPDPPGAVPLPPvrgeIEFENVSFS--------------------------------Y------------ 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 505 pnaehllthmeqespqstisstqsirPPLHKTLHRIDLCIQKgslvgvcggvgsgKSSLLSALLGQMTLLGGSVSVNG-- 582
Cdd:COG1132 350 --------------------------PGDRPVLKDISLTIPPgetvalvgpsgsgKSTLVNLLLRFYDPTSGRILIDGvd 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 583 -----------GFAYVAQQAWILNDSLRENILFGKK-YNEEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQ 650
Cdd:COG1132 404 irdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 651 RVSLARALYSERPILLLDDPLSAVDARVGSRLFHsAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLM 730
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQE-ALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL 562
|
650
....*....|..
gi 1207190976 731 EKGRDYAALFNS 742
Cdd:COG1132 563 ARGGLYARLYRL 574
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1147-1364 |
6.17e-56 |
|
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: 205.82 E-value: 6.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1147 EGQITFQDVEMRYRDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSK 1226
Cdd:COG5265 355 GGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1227 LSVIPQEPVLFIGTVRSNLdpwdQY-----TDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARAL 1301
Cdd:COG5265 434 IGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1302 LRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILE 1364
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
866-1364 |
1.27e-55 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 207.10 E-value: 1.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 866 HIQYYSRVYVLSMGAAL----FLKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDmDEVDVR 941
Cdd:TIGR03796 188 GRQDWLRPLLLGMGLTAllqgVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEF 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 942 LAMQ-AEMLLQNVTLVLFclGVVGAVFPWFL------FSIIPLGAFLFIVNRI---SRVLIRELKRLENISqspftshiT 1011
Cdd:TIGR03796 267 LSGQlATTALDAVMLVFY--ALLMLLYDPVLtligiaFAAINVLALQLVSRRRvdaNRRLQQDAGKLTGVA--------I 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1012 SSLQGLSTIYAYGRGADFIHR---YQA-LLDTNQACQFLfscamrwlAVRLDLI--SISLITTVALLIV----LMHGHIS 1081
Cdd:TIGR03796 337 SGLQSIETLKASGLESDFFSRwagYQAkLLNAQQELGVL--------TQILGVLptLLTSLNSALILVVgglrVMEGQLT 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1082 ----PAYAGLALSYAVQLTGLFQFTVRLlSETEArftSVERINHYIKN-LESEGPRQITGCPTSSSSWPAEGQITFQDVE 1156
Cdd:TIGR03796 409 igmlVAFQSLMSSFLEPVNNLVGFGGTL-QELEG---DLNRLDDVLRNpVDPLLEEPEGSAATSEPPRRLSGYVELRNIT 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1157 MRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVL 1236
Cdd:TIGR03796 485 FGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFL 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1237 FIGTVRSNLDPWDQ-YTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATA 1315
Cdd:TIGR03796 565 FEGTVRDNLTLWDPtIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATS 644
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1207190976 1316 AIDTETDRLIQDTIRSSfsGCTTLVIAHRLNTVLGCNRIMVLDQGQILE 1364
Cdd:TIGR03796 645 ALDPETEKIIDDNLRRR--GCTCIIVAHRLSTIRDCDEIIVLERGKVVQ 691
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1150-1379 |
6.98e-53 |
|
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: 185.77 E-value: 6.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSV 1229
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFIGTVRSNLDPWDQYTDAQ-IWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKIL 1308
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMErVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1309 LLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLtDENSRF 1379
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL-AENGLY 230
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
142-427 |
1.64e-52 |
|
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: 186.50 E-value: 1.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 142 VAIFSLLITMVAGFVGPaLLIRALLEFSQCSEV-----KLLYGLALVAGIFLMELTRSWSLAFMWAINYRTAARLRGAAL 216
Cdd:cd18597 1 LAGLLKLLADVLQVLSP-LLLKYLINFVEDAYLggpppSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 217 TFAFQKILRL--RSTKDVSSGELVNICASDGQRLYEAVSVGCLLAGGPLVGMLGLTYTTYFLGPTALVGSAIFIIFYPTM 294
Cdd:cd18597 80 KAIYRKSLRLsgKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 295 MLASRMTAYFRKKCVAVTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEERRNLEWAGCVQSLTLGVAPVVVVIA 374
Cdd:cd18597 160 GFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 375 SVCTFTLHMALGYDLTAAQAFTVVAVFNSMTFALKVTPLAVRALSEGSVAVKR 427
Cdd:cd18597 240 SMLSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKR 292
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1148-1362 |
6.17e-52 |
|
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: 182.02 E-value: 6.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1148 GQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKL 1227
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPVLFIGTVRSNLDPWDQY-TDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSK 1306
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 1307 ILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQI 1362
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
906-1372 |
1.39e-50 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 189.46 E-value: 1.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 906 KLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVdvrlAMQAEMLLqnVTLVLFCLGVVGAVFPWFLFSIiPLGAFLFIVN 985
Cdd:PRK11176 103 RLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQV----ASSSSGAL--ITVVREGASIIGLFIMMFYYSW-QLSLILIVIA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 986 RISRVLIREL-KRLENISQSPFTS--HITSS----LQGLSTIYAYGRGADFIHRYQALldtnqacqflfSCAMRWLAVRL 1058
Cdd:PRK11176 176 PIVSIAIRVVsKRFRNISKNMQNTmgQVTTSaeqmLKGHKEVLIFGGQEVETKRFDKV-----------SNRMRQQGMKM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1059 ---DLIS---ISLITTVALLIVLMHGHISPAYAGL-ALSYAVQLTGLFQFTVRLLSETE--ARF--------TSVErinh 1121
Cdd:PRK11176 245 vsaSSISdpiIQLIASLALAFVLYAASFPSVMDTLtAGTITVVFSSMIALMRPLKSLTNvnAQFqrgmaacqTLFA---- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1122 yIKNLESE---GPRQITgcptsssswPAEGQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALF 1198
Cdd:PRK11176 321 -ILDLEQEkdeGKRVIE---------RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1199 RLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNLD--PWDQYTDAQIWEALEKTHIKDMVSQLPNSL 1276
Cdd:PRK11176 391 RFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1277 HSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMV 1356
Cdd:PRK11176 471 DTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILV 550
|
490
....*....|....*.
gi 1207190976 1357 LDQGQILEFDTPSNLL 1372
Cdd:PRK11176 551 VEDGEIVERGTHAELL 566
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
560-718 |
9.15e-50 |
|
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: 175.98 E-value: 9.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVN-----------------GGFAYVAQQAWILNDSLRENILFGKKYNEEKYNAVLEACCL 622
Cdd:cd03290 40 KSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 623 FPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKG--KTVIFVT 700
Cdd:cd03290 120 QPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVT 199
|
170
....*....|....*...
gi 1207190976 701 HQLQYLPECDDVVLMKDG 718
Cdd:cd03290 200 HKLQYLPHADWIIAMKDG 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
560-733 |
4.70e-48 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 181.49 E-value: 4.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGK-KYNEEKYNAVLEACCLFPD 625
Cdd:COG4988 376 KSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEF 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 626 IIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHsAIRPAAKGKTVIFVTHQLQY 705
Cdd:COG4988 456 VAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQ-ALRRLAKGRTVILITHRLAL 534
|
170 180
....*....|....*....|....*...
gi 1207190976 706 LPECDDVVLMKDGQIAEHGTHTQLMEKG 733
Cdd:COG4988 535 LAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
874-1382 |
1.94e-46 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 177.22 E-value: 1.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 874 YVLSMGAALFLKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNV 953
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 954 TLV------LFCLG-----VVGAVFPWFLfsiiplgAFLFIVNRISRVLIRELKR-LENISQSpFTSHITsslqGLSTIY 1021
Cdd:PRK10790 151 ALIgamlvaMFSLDwrmalVAIMIFPAVL-------VVMVIYQRYSTPIVRRVRAyLADINDG-FNEVIN----GMSVIQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1022 AYGRGADFIHRyqaLLDTNQAcQFLfscaMRWLAVRLD--LIS--ISLITTVALLIVLM-HGHISPAYAGLALSYAV--Q 1094
Cdd:PRK10790 219 QFRQQARFGER---MGEASRS-HYM----ARMQTLRLDgfLLRplLSLFSALILCGLLMlFGFSASGTIEVGVLYAFisY 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1095 LTGLFQFTVRLLSETEARFTSV---ERINHYIknlesEGPRQITGcptsSSSWP-AEGQITFQDVEMRYRDGLPlVLKNL 1170
Cdd:PRK10790 291 LGRLNEPLIELTTQQSMLQQAVvagERVFELM-----DGPRQQYG----NDDRPlQSGRIDIDNVSFAYRDDNL-VLQNI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1171 CFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNLDPWDQ 1250
Cdd:PRK10790 361 NLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1251 YTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIR 1330
Cdd:PRK10790 441 ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALA 520
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 1331 SSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTdENSRFHAM 1382
Cdd:PRK10790 521 AVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA-AQGRYWQM 571
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
875-1380 |
6.67e-46 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 177.99 E-value: 6.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 875 VLSMGAALFlKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVT 954
Cdd:TIGR00958 209 LLSIASSVS-AGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLV 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 955 LVLFCLGVVGAVFPWF----LFSIIPLGAFLFIVNRISRVLIRELKrlENISQSpfTSHITSSLQGLSTIYAYGRGADFI 1030
Cdd:TIGR00958 288 MLLGLLGFMLWLSPRLtmvtLINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKA--NQVAEEALSGMRTVRSFAAEEGEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1031 HRY-QALLDTNQACQflfscaMRWLAVRLDLISISLITTVALLIVLMHG-HI---SPAYAGLALS---YAVQLTGLFQFT 1102
Cdd:TIGR00958 364 SRFkEALEETLQLNK------RKALAYAGYLWTTSVLGMLIQVLVLYYGgQLvltGKVSSGNLVSfllYQEQLGEAVRVL 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1103 VRLLSETEARFTSVERINHYIK---NLESEGprqiTGCPTsssswPAEGQITFQDVEMRY--RDGLPlVLKNLCFSILPE 1177
Cdd:TIGR00958 438 SYVYSGMMQAVGASEKVFEYLDrkpNIPLTG----TLAPL-----NLEGLIEFQDVSFSYpnRPDVP-VLKGLTFTLHPG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1178 ETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNLD-PWDQYTDAQI 1256
Cdd:TIGR00958 508 EVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEI 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1257 WEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTirSSFSGC 1336
Cdd:TIGR00958 588 MAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASR 665
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1207190976 1337 TTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTDENSRFH 1380
Cdd:TIGR00958 666 TVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
902-1345 |
8.12e-46 |
|
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: 174.09 E-value: 8.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 902 VLHDKLFKTLLLSPMRFFD----TTPLGR-------ILNRFSKDMDEV-DVRLAMQAEMLLQNVTLVLFCLGVvgAVFPW 969
Cdd:TIGR02868 76 VGHDAALRSLGALRVRVYErlarQALAGRrrlrrgdLLGRLGADVDALqDLYVRVIVPAGVALVVGAAAVAAI--AVLSV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 970 FLFSIIPLGA--FLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQallDTNQACQFLF 1047
Cdd:TIGR02868 154 PAALILAAGLllAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVE---EADRELTRAE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1048 SCAMRWLAVRLDLISISLITTVALLIVL-----MHGHISPAYAG------LALSYAVQ-LTGLFQftvrllSETEARfTS 1115
Cdd:TIGR02868 231 RRAAAATALGAALTLLAAGLAVLGALWAggpavADGRLAPVTLAvlvllpLAAFEAFAaLPAAAQ------QLTRVR-AA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1116 VERINHYiknLESEGPRQITGCPTSSSSWPAEGQITFQDVEMRYrDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGV 1195
Cdd:TIGR02868 304 AERIVEV---LDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1196 ALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNL---DPwdQYTDAQIWEALEKTHIKDMVSQL 1272
Cdd:TIGR02868 380 TLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGLADWLRAL 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1273 PNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRL 1345
Cdd:TIGR02868 458 PDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1147-1385 |
1.04e-44 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 172.07 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1147 EGQITFQDVEMRYrDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSK 1226
Cdd:PRK13657 332 KGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1227 LSVIPQEPVLFIGTVRSNL-----DPwdqyTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARAL 1301
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1302 LRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILE---FDTpsnlLTDENSR 1378
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFDE----LVARGGR 562
|
....*..
gi 1207190976 1379 FHAMMEA 1385
Cdd:PRK13657 563 FAALLRA 569
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1147-1362 |
3.26e-44 |
|
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: 160.33 E-value: 3.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1147 EGQITFQDVEMRYRDgLP--LVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLR 1224
Cdd:cd03248 9 KGIVKFQNVTFAYPT-RPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1225 SKLSVIPQEPVLFIGTVRSNLD-PWDQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLR 1303
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1304 HSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQI 1362
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1126-1388 |
1.39e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 168.48 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1126 LESEGPRQITGCPTSSSSWPAEgqITFQDVEMRYRDGLPLvLKNLCFSILPEETIGIVGRTGSGKSSLGVALfrLAELS- 1204
Cdd:PRK11174 328 LETPLAHPQQGEKELASNDPVT--IEAEDLEILSPDGKTL-AGPLNFTLPAGQRIALVGPSGAGKTSLLNAL--LGFLPy 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1205 RGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNL---DPwdQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVT 1281
Cdd:PRK11174 403 QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1282 DNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQ 1361
Cdd:PRK11174 481 DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQ 560
|
250 260 270
....*....|....*....|....*....|
gi 1207190976 1362 ILE---FDTpsnlLTDENSRFHAMMEAAEE 1388
Cdd:PRK11174 561 IVQqgdYAE----LSQAGGLFATLLAHRQE 586
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
560-741 |
1.61e-43 |
|
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: 170.40 E-value: 1.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGKKY-NEEKYNAVLEACCLFPD 625
Cdd:COG2274 514 KSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDF 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 626 IIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRPAAKGKTVIFVTHQLQY 705
Cdd:COG2274 594 IEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAE-TEAIILENLRRLLKGRTVIIIAHRLST 672
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207190976 706 LPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFN 741
Cdd:COG2274 673 IRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1138-1357 |
1.28e-42 |
|
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: 164.38 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1138 PTSSSSWPAEGQITFQDVEMRYRDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAH 1217
Cdd:TIGR02857 310 GKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1218 IGLEDLRSKLSVIPQEPVLFIGTVRSNLDPWDQY-TDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLC 1296
Cdd:TIGR02857 389 ADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1297 VARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVL 1357
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
144-427 |
2.44e-42 |
|
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: 157.66 E-value: 2.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 144 IFSLLITMVAGFVGPaLLIRALLEFSQC-SEVKLLYGLALVAGIFLMELTRSWSLAFMWAINYRTAARLRgAALTFA-FQ 221
Cdd:cd18596 3 ALLAVLSSVLSFAPP-FFLNRLLRYLEDpGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLR-AILTQLiFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 222 KILRLRSTKDVSS---------------------GELVNICASDGQRLYEAVSVGCLLAGGPLVGMLGLTYTTYFLGPTA 280
Cdd:cd18596 81 KALRRRDKSGSSKsseskkkdkeededekssasvGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 281 LVGSAIFIIFYP-TMMLASRMTAYFRKKcVAVTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEE---RRNLEWA 356
Cdd:cd18596 161 LVGLAVMVLLLPlNGYLAKRYSRAQKEL-MKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEElkwLRKRFLL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 357 GCVQSLTLGVAPVVVVIASVCTFTLHMalGYDLTAAQAFTVVAVFNSMTFALKVTPLAVRALSEGSVAVKR 427
Cdd:cd18596 240 DLLLSLLWFLIPILVTVVTFATYTLVM--GQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDR 308
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
142-427 |
1.06e-41 |
|
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: 155.32 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 142 VAIFSLLITMVAGFVGPALLiRALLEFSQCSEVKLLYGLALVAGIFLMELTRSWSLAFMWAINYRTAARLRgAALTFA-F 220
Cdd:cd18595 1 LAALLKLLSDILLFASPQLL-KLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIR-TALTSAiY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 221 QKILRLRST--KDVSSGELVNICASDGQRLYEAVSVGCLLAGGPLVGMLGLTYTTYFLGPTALVGSAIFIIFYPTMMLAS 298
Cdd:cd18595 79 RKALRLSNSarKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 299 RMTAYFRKKCVAVTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEERRNLEWAG---CVQSLTLGVAPVVVVIAS 375
Cdd:cd18595 159 RKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAylnAVSSFLWTCAPFLVSLAT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 376 VCTFTLhMALGYDLTAAQAFTVVAVFNSMTFALKVTPLAVRALSEGSVAVKR 427
Cdd:cd18595 239 FATYVL-SDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKR 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
560-741 |
1.25e-41 |
|
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: 162.24 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGKKY-NEEKYNAVLEACCLFPD 625
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLARPDaTDEELWAALERVGLGDW 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 626 IIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHsAIRPAAKGKTVIFVTHQLQY 705
Cdd:COG4987 454 LAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLA-DLLEALAGRTVLLITHRLAG 532
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207190976 706 LPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFN 741
Cdd:COG4987 533 LERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1114-1384 |
6.93e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 157.29 E-value: 6.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1114 TSVERINHYIknlesEGPRQITgCPTSSSSWPAEGQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSL 1193
Cdd:PRK11160 309 ASARRINEIT-----EQKPEVT-FPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1194 GVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNL---DPwdQYTDAQIWEALEKTHIKDMVS 1270
Cdd:PRK11160 383 LQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1271 QlPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLG 1350
Cdd:PRK11160 461 D-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQ 539
|
250 260 270
....*....|....*....|....*....|....
gi 1207190976 1351 CNRIMVLDQGQILEFDTPSNLLTDENsRFHAMME 1384
Cdd:PRK11160 540 FDRICVMDNGQIIEQGTHQELLAQQG-RYYQLKQ 572
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
584-740 |
3.31e-38 |
|
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: 143.14 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 584 FAYVAQQAWILNDSLRENILFGKK-YNEEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSER 662
Cdd:cd03251 78 IGLVSQDVFLFNDTVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 663 PILLLDDPLSAVDARvGSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALF 740
Cdd:cd03251 158 PILILDEATSALDTE-SERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
147-429 |
5.80e-38 |
|
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: 144.31 E-value: 5.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 147 LLITMVAGFVGPALLIRALLEFSQCSEVK----LLYGLALVAGIFLMELTRSWslAFMwaINYRTAARLRGAALTFAFQK 222
Cdd:cd18594 6 LFLEESLKIVQPLLLGRLVAYFVPDSTVTkteaYLYALGLSLCAFLRVLLHHP--YFF--GLHRYGMQLRIALSSLIYKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 223 ILRLRST--KDVSSGELVNICASDGQRLYEAVSVGCLLAGGPLVGMLGLTYTTYFLGPTALVGSAIFIIFYPTMMLASRM 300
Cdd:cd18594 82 TLKLSSSalSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 301 TAYFRKKCVAVTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEERRNLEWAGCVQSLTLG---VAPVVVVIASVC 377
Cdd:cd18594 162 FAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAfffFSPTLVSFATFV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 378 TFTLhmaLGYDLTAAQAFTVVAVFNS--MTFALKVtPLAVRALSEGSVAVKRFQ 429
Cdd:cd18594 242 PYVL---TGNTLTARKVFTVISLLNAlrMTITRFF-PESIQTLSESRVSLKRIQ 291
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
799-1123 |
1.20e-37 |
|
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: 144.56 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 799 WPVYAAYIkAAGGPLAFIVTILLFLFTTgSIAFSNWWLsyWIRQgsgnsSLLLGNETAESDSMRLNPHI-------QYYS 871
Cdd:cd18600 3 WNTYLRYI-TSHKSLIFVLILCLVIFAI-EVAASLVGL--WLLR-----SQADRVNTTRPESSSNTYAVivtftssYYVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 872 RVYVLSMGAALFLKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQ 951
Cdd:cd18600 74 YIYVGVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 952 NVTLVLFCLGVVGAVFPWFLFSIIPLGAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIH 1031
Cdd:cd18600 154 LFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1032 RYQALLDTNQACQFLFSCAMRWLAVRLDLISISLITTVALLIVLMHGHiSPAYAGLALSYAVQLTGLFQFTVRLLSETEA 1111
Cdd:cd18600 234 LFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDS 312
|
330
....*....|..
gi 1207190976 1112 RFTSVERINHYI 1123
Cdd:cd18600 313 LMRSVSRIFKFI 324
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1150-1362 |
2.51e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.87 E-value: 2.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVemRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSV 1229
Cdd:COG4619 1 LELEGL--SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFIGTVRSNLDPWDQYTDaqiwEALEKTHIKDMVSQL---PNSLHSEVtdngENFSVGERQLLCVARALLRHSK 1306
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLRE----RKFDRERALELLERLglpPDILDKPV----ERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1307 ILLLDEATAAIDTETDRLIQDTIRSSF--SGCTTLVIAH------RLntvlgCNRIMVLDQGQI 1362
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
1008-1386 |
4.47e-36 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 145.80 E-value: 4.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1008 SHITSSLQGLSTIYAYGRgadFIHRYQALldtNQACQFLFSC---AMRWLAVRLDLISISliTTVALLIVLMHGHISPAY 1084
Cdd:TIGR01192 196 KHVSDSISNVSVVHSYNR---IEAETSAL---KQFTNNLLSAqypVLDWWALASGLNRMA--STISMMCILVIGTVLVIK 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1085 AGLALSYAVQLTGLFQFTVRLLSETEARFTSVERINHYIKNL-ESEGPRQITGCPTSSSSWP-AEGQITFQDVEMRYRDG 1162
Cdd:TIGR01192 268 GELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFfDLEDSVFQREEPADAPELPnVKGAVEFRHITFEFANS 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1163 LPLVlKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVR 1242
Cdd:TIGR01192 348 SQGV-FDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIR 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1243 SNLD-PWDQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTET 1321
Cdd:TIGR01192 427 ENIRlGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVET 506
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1322 DRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNlLTDENSRFHAMMEAA 1386
Cdd:TIGR01192 507 EARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQE-LIQKDGRFYKLLRRS 570
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
585-742 |
4.64e-36 |
|
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: 136.98 E-value: 4.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 585 AYVAQQAWILNDSLRENILFGK--KYNEEKYNAVlEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSER 662
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRpdATDEEVIEAA-KAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 663 PILLLDDPLSAVDArVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFNS 742
Cdd:cd03253 157 PILLLDEATSALDT-HTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
560-715 |
5.22e-36 |
|
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: 144.74 E-value: 5.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG-------------FAYVAQQAWILNDSLRENILFGKKY-NEEKYNAVLEACCLFPD 625
Cdd:TIGR02857 361 KSTLLNLLLGFVDPTEGSIAVNGVpladadadswrdqIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEF 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 626 IIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRPAAKGKTVIFVTHQLQY 705
Cdd:TIGR02857 441 VAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL-EALRALAQGRTVLLVTHRLAL 519
|
170
....*....|
gi 1207190976 706 LPECDDVVLM 715
Cdd:TIGR02857 520 AALADRIVVL 529
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
141-427 |
6.46e-36 |
|
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: 138.51 E-value: 6.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 141 LVAIFSLLITMVagFVGPALLIRALLEF--SQCSEVKLLYGLALVAGIFLmeltrswsLAFMWAINY--------RTAAR 210
Cdd:cd18593 1 LLGIFLFLEEAI--RVVQPIFLGKLIRYfeGNGSSISLTEAYLYAGGVSL--------CSFLFIITHhpyffgmqRIGMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 211 LRGAALTFAFQKILRLRST--KDVSSGELVNICASDGQRLYEAVSVGCLLAGGPLvGMLGLTYTTYF-LGPTALVGSAIF 287
Cdd:cd18593 71 LRVACSSLIYRKALRLSQAalGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPL-QLIAVIYILWFeIGWSCLAGLAVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 288 IIFYPTMMLASRMTAYFRKKCVAVTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEERRNLEWAGCVQSLTLGVA 367
Cdd:cd18593 150 LILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 368 PVVVVIASVCTFTLHMALGYDLTAAQAFTVVAVFNS----MTFALkvtPLAVRALSEGSVAVKR 427
Cdd:cd18593 230 FVSSKLILFLTFLAYILLGNILTAERVFVTMALYNAvrltMTLFF---PFAIQFGSELSVSIRR 290
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1150-1362 |
1.04e-35 |
|
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: 133.88 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSV 1229
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFIGTVRSNLdpwdqytdaqiwealekthikdmvsqlpnslhsevtdngenFSVGERQLLCVARALLRHSKILL 1309
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1310 LDEATAAIDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLGCNRIMVLDQGQI 1362
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
532-752 |
1.46e-34 |
|
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: 134.21 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 532 PLHKT--LHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMTLLGGSVSVNGGFAYVAQQAWILNDSLRENILFGKKYN 609
Cdd:cd03291 46 CLVGApvLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 610 EEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRP 689
Cdd:cd03291 126 EYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 690 AAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAAL---FNSVQQENLVRKN 752
Cdd:cd03291 206 LMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKlmgYDTFDQFSAERRN 271
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
960-1365 |
3.77e-34 |
|
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: 139.50 E-value: 3.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 960 LGVVGAVFPWF----LFSIIPLGAFLFIVNRISRVLIRELKRLENISQSpftsHITSSLQGLSTIYAYGRGADFIHRYQA 1035
Cdd:COG4618 147 LAVLFLFHPLLgllaLVGALVLVALALLNERLTRKPLKEANEAAIRANA----FAEAALRNAEVIEAMGMLPALRRRWQR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1036 LLDTNQACQFLFSCAMRWLA-----VRLdLISISLITTVALLIVlmHGHISPA-------YAGLALSYAVQLTGLFQFTV 1103
Cdd:COG4618 223 ANARALALQARASDRAGGFSalskfLRL-LLQSAVLGLGAYLVI--QGEITPGamiaasiLMGRALAPIEQAIGGWKQFV 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1104 RllseteARfTSVERINHYIKNLESEGPRqitgcptssSSWPA-EGQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGI 1182
Cdd:COG4618 300 S------AR-QAYRRLNELLAAVPAEPER---------MPLPRpKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1183 VGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNLDPWDQYTDAQIWEALEK 1262
Cdd:COG4618 364 IGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKL 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1263 THIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRS-SFSGCTTLVI 1341
Cdd:COG4618 444 AGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVVVI 523
|
410 420
....*....|....*....|....
gi 1207190976 1342 AHRLNTVLGCNRIMVLDQGQILEF 1365
Cdd:COG4618 524 THRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
584-739 |
1.29e-32 |
|
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: 127.27 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 584 FAYVAQQAWILNDSLRENILFGKKYNEEKynAVLEACCL-----FpdIIELPYGDMTEIGERGANLSGGQRQRVSLARAL 658
Cdd:cd03249 79 IGLVSQEPVLFDGTIAENIRYGKPDATDE--EVEEAAKKanihdF--IMSLPDGYDTLVGERGSQLSGGQKQRIAIARAL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 659 YSERPILLLDDPLSAVDARVgSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAA 738
Cdd:cd03249 155 LRNPKILLLDEATSALDAES-EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAK 233
|
.
gi 1207190976 739 L 739
Cdd:cd03249 234 L 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
560-733 |
2.20e-32 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 126.19 E-value: 2.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGKKYN-EEKYNAVLEACCLFPD 625
Cdd:cd03254 42 KTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKEAGAHDF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 626 IIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLfHSAIRPAAKGKTVIFVTHQLQY 705
Cdd:cd03254 122 IMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLI-QEALEKLMKGRTSIIIAHRLST 200
|
170 180
....*....|....*....|....*...
gi 1207190976 706 LPECDDVVLMKDGQIAEHGTHTQLMEKG 733
Cdd:cd03254 201 IKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
560-719 |
2.58e-32 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 124.03 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG-------------FAYVAQQAWILNDSLRENILfgkkyneekynavleacclfpdi 626
Cdd:cd03228 41 KSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknIAYVPQDPFLFSGTIRENIL----------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 627 ielpygdmteigerganlSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRPAAKGKTVIFVTHQLQYL 706
Cdd:cd03228 98 ------------------SGGQRQRIAIARALLRDPPILILDEATSALDP-ETEALILEALRALAKGKTVIVIAHRLSTI 158
|
170
....*....|...
gi 1207190976 707 PECDDVVLMKDGQ 719
Cdd:cd03228 159 RDADRIIVLDDGR 171
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
560-746 |
2.71e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 134.20 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLlGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGKK-YNEEKYNAVLEACCLFPD 625
Cdd:PRK11174 389 KTSLLNALLGFLPY-QGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEF 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 626 IIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRPAAKGKTVIFVTHQLQY 705
Cdd:PRK11174 468 LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH-SEQLVMQALNAASRRQTTLMVTHQLED 546
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207190976 706 LPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFNSVQQE 746
Cdd:PRK11174 547 LAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1150-1364 |
6.96e-32 |
|
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: 123.19 E-value: 6.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGlEDLRSKLSV 1229
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFIGTVRSNLdpwdqytdaqiwealekthikdmvsqlpnslhsevtdnGENFSVGERQLLCVARALLRHSKILL 1309
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1310 LDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILE 1364
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
148-428 |
9.87e-32 |
|
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: 126.13 E-value: 9.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 148 LITMVAGFVGPaLLIRALLEF-----SQCSEVkLLYGLALVAGIFLMELTRSwslAFMWAINyRTAARLRGAALTFAFQK 222
Cdd:cd18598 7 LLADVLGFAGP-LLLNKLVEFledssEPLSDG-YLYALGLVLSSLLGALLSS---HYNFQMN-KVSLKVRAALVTAVYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 223 ILRLRSTKDV--SSGELVNICASDGQRLyeAVSVGCL--LAGGPL-VGM-LGLTYTTyfLGPTALVGSAIFIIFYP-TMM 295
Cdd:cd18598 81 ALRVRSSSLSkfSTGEIVNLMSTDADRI--VNFCPSFhdLWSLPLqIIVaLYLLYQQ--VGVAFLAGLVFALVLIPiNKW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 296 LASRMTAYFRKKcVAVTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEERRNLEW-----AGCV---QSLtlgva 367
Cdd:cd18598 157 IAKRIGALSEKM-MKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGrkyldALCVyfwATT----- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 368 PVVVviaSVCTFTLHMALGYDLTAAQAFTVVAVFNSMTFALKVTPLAVRALSEGSVAVKRF 428
Cdd:cd18598 231 PVLI---SILTFATYVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
629-1358 |
1.48e-31 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 135.16 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 629 LPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDAR----------------------VGSRLfhSA 686
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseylvqktinnlkgnenritiiIAHRL--ST 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 687 IRPAakgkTVIFVTHQLQYLPECDDVVLMKDGQ--------------------------------IAEHGTHTQLME-KG 733
Cdd:PTZ00265 643 IRYA----NTIFVLSNRERGSTVDVDIIGEDPTkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKnKN 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 734 RDYAALFNSVQQENLVRKNLKNKEKAEKESS----------PQTLHVSNPPKPDTESKKTDQLMQAEEKGSgavawpvya 803
Cdd:PTZ00265 719 GIYYTMINNQKVSSKKSSNNDNDKDSDMKSSaykdsergydPDEMNGNSKHENESASNKKSCKMSDENASE--------- 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 804 ayiKAAGGPLAF----------------------------IVTILLFLFTTGSI--AFSNWWLSYwirqgsgnSSLLLGN 853
Cdd:PTZ00265 790 ---NNAGGKLPFlrnlfkrkpkapnnlrivyreifsykkdVTIIALSILVAGGLypVFALLYAKY--------VSTLFDF 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 854 ETAESDSMRlnphiqyYSrVYVLSMGAALFL-KTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDT---TP--LGRI 927
Cdd:PTZ00265 859 ANLEANSNK-------YS-LYILVIAIAMFIsETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAPglLSAH 930
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 928 LNRfskdmdevDVRLAMQAemLLQNVTL-----VLFclgVVGAVFPWFLFSIIP--LGAFLFIVNRISRVLIR------- 993
Cdd:PTZ00265 931 INR--------DVHLLKTG--LVNNIVIfthfiVLF---LVSMVMSFYFCPIVAavLTGTYFIFMRVFAIRARltankdv 997
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 994 ELKRLeNISQSPFTSH------------ITSSLQGLSTIYAYG----------RGADFIHRYQ--------ALLDTNQAC 1043
Cdd:PTZ00265 998 EKKEI-NQPGTVFAYNsddeifkdpsflIQEAFYNMNTVIIYGledyfcnlieKAIDYSNKGQkrktlvnsMLWGFSQSA 1076
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1044 QFLFSCAMRWLAVRLdlISISLITTVALLIVLMHGHISPAYAGLALSyavqltglfqftvrLLSETEARFTSVERINHYI 1123
Cdd:PTZ00265 1077 QLFINSFAYWFGSFL--IRRGTILVDDFMKSLFTFLFTGSYAGKLMS--------------LKGDSENAKLSFEKYYPLI 1140
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1124 KNLESEGPRQITGCPTSSSSwPAEGQITFQDVEMRY--RDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLA 1201
Cdd:PTZ00265 1141 IRKSNIDVRDNGGIRIKNKN-DIKGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFY 1218
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1202 EL------------------------------------------------------SRGSIIIDGVNIAHIGLEDLRSKL 1227
Cdd:PTZ00265 1219 DLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLF 1298
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPVLFIGTVRSNLD-PWDQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSK 1306
Cdd:PTZ00265 1299 SIVSQEPMLFNMSIYENIKfGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1307 ILLLDEATAAIDTETDRLIQDTIR--SSFSGCTTLVIAHRLNTVLGCNRIMVLD 1358
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIKRSDKIVVFN 1432
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
560-720 |
1.52e-31 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 123.47 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGKKY-NEEKYNAVLEACCLFPD 625
Cdd:cd03245 43 KSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 626 IIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHsAIRPAAKGKTVIFVTHQLQY 705
Cdd:cd03245 123 VNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKE-RLRQLLGDKTLIIITHRPSL 201
|
170
....*....|....*
gi 1207190976 706 LPECDDVVLMKDGQI 720
Cdd:cd03245 202 LDLVDRIIVMDSGRI 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1150-1376 |
1.55e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 124.77 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLplVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSV 1229
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFIG-TVR-----------SNLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCV 1297
Cdd:COG1120 80 VPQEPPAPFGlTVRelvalgryphlGLFGRPSAEDREAVEEALERTGLEHLADRPVDEL-----------SGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1298 ARALLRHSKILLLDEATAAID----TETDRLIQDTIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLL 1372
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARE--RGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVL 226
|
....
gi 1207190976 1373 TDEN 1376
Cdd:COG1120 227 TPEL 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1150-1365 |
1.95e-31 |
|
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: 123.38 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLV--LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIG---LEDLR 1224
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1225 SKLSVIPQEPvlfigtvRSNLDPWdqYT-DAQIWEALEKtHIKDMVSQLPNSLHSEVTDNGEN-----------FSVGER 1292
Cdd:cd03257 82 KEIQMVFQDP-------MSSLNPR--MTiGEQIAEPLRI-HGKLSKKEARKEAVLLLLVGVGLpeevlnrypheLSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 1293 QLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIR--SSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEF 1365
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
584-741 |
6.01e-31 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 129.84 E-value: 6.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 584 FAYVAQQAWILNDSLRENILFGK--KYNEEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSE 661
Cdd:TIGR02203 408 VALVSQDVVLFNDTIANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKD 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 662 RPILLLDDPLSAVDARvGSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFN 741
Cdd:TIGR02203 488 APILILDEATSALDNE-SERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHN 566
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1167-1315 |
6.07e-31 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 119.29 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIG-TVRSNL 1245
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 1246 -------DPWDQYTDAQIWEALEKTHIKDMvsqlpnsLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATA 1315
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
178-427 |
7.43e-31 |
|
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: 124.27 E-value: 7.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 178 YGLALVagIFLMELTRSwslAFMWA---INYRTAARLRGAALTFAFQKILRLRS----TKDVSSGELVNICASDGQRLYE 250
Cdd:cd18591 56 YVLAVI--LFLALLLQA---TFSQAsyhIVIREGIRLKTALQAMIYEKALRLSSwnlsSGSMTIGQITNHMSEDANNIMF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 251 AVSVGCLLAGGPL--VGMLGLTYttYFLGPTALVGSAIFIIFYPTMMLASRMTAYFRKKCVAVTDRRVRLMNEILGCMKF 328
Cdd:cd18591 131 FFWLIHYLWAIPLkiIVGLILLY--LKLGVSALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 329 IKMYCWETPFANNIQKVRSEERRNLeWAGCVQ-SLTLGVAPVVVVIASVCTFTLHMAL-GYDLTAAQAFTVVAVFNSMTF 406
Cdd:cd18591 209 LKLYAWENIFLDKIQEARRKELKLL-LKDAVYwSLMTFLTQASPILVTLVTFGLYPYLeGEPLTAAKAFSSLALFNQLTV 287
|
250 260
....*....|....*....|.
gi 1207190976 407 ALKVTPLAVRALSEGSVAVKR 427
Cdd:cd18591 288 PLFIFPVVIPILINAVVSTRR 308
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1123-1364 |
9.97e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 129.45 E-value: 9.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1123 IKNLESEGPRQITGcptsSSSWPAE-GQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLA 1201
Cdd:PRK10789 290 IRAMLAEAPVVKDG----SEPVPEGrGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1202 ELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIGTVRSNL---DPwdQYTDAQIWEALEKTHIKDMVSQLPNSLHS 1278
Cdd:PRK10789 366 DVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDT 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1279 EVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLGCNRIMVLD 1358
Cdd:PRK10789 444 EVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQ 523
|
....*.
gi 1207190976 1359 QGQILE 1364
Cdd:PRK10789 524 HGHIAQ 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
560-725 |
8.62e-30 |
|
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: 118.36 E-value: 8.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGKKYNEEKYNAVLEACCLFPDI 626
Cdd:cd03244 43 KSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 627 IELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRPAAKGKTVIFVTHQLQYL 706
Cdd:cd03244 123 ESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPE-TDALIQKTIREAFKDCTVLTIAHRLDTI 201
|
170
....*....|....*....
gi 1207190976 707 PECDDVVLMKDGQIAEHGT 725
Cdd:cd03244 202 IDSDRILVLDKGRVVEFDS 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
585-739 |
1.93e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 126.76 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 585 AYVAQQAWILNDSLRENILFG-KKYNEEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERP 663
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 664 ILLLDDPLSAVDARVGSRLFHSairPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAAL 739
Cdd:TIGR00958 638 VLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
560-746 |
3.54e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 124.44 E-value: 3.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSV-------------SVNGGFAYVAQQAWILNDSLRENILFGK-KYNEEKYNAVLEACCLFPD 625
Cdd:PRK10789 354 KSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 626 IIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSaIRPAAKGKTVIFVTHQLQY 705
Cdd:PRK10789 434 ILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN-LRQWGEGRTVIISAHRLSA 512
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207190976 706 LPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFNSVQQE 746
Cdd:PRK10789 513 LTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLE 553
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
815-1099 |
3.69e-29 |
|
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: 118.51 E-value: 3.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 815 FIVTILLFLFTTGSIAFSNWWLSYWIRQGSGNSSlllgnetaeSDSMRLNphiqYYSRVYVLSMGAALFLKTIRGLVFVK 894
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGD---------PETQALN----VYSLALLLLGLAQFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 895 CTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWFLFSI 974
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 975 IPLGAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLFSCAMRWL 1054
Cdd:pfam00664 148 LAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLS 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1207190976 1055 AVRLDLISiSLITTVALLIV---LMHGHISPAYAGLALSYAVQLTGLF 1099
Cdd:pfam00664 228 FGITQFIG-YLSYALALWFGaylVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1150-1374 |
5.57e-29 |
|
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: 123.09 E-value: 5.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELS---RGSIIIDGVNIAHIGLEDLRSK 1226
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1227 LSVIPQEPvlfigtvRSNLDPW---DQYTDA-------------QIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVG 1290
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVtvgDQIAEAlenlglsraearaRVLELLEAVGLERRLDRYPHQL-----------SGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1291 ERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRS--SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDT 1367
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGP 226
|
....*..
gi 1207190976 1368 PSNLLTD 1374
Cdd:COG1123 227 PEEILAA 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1150-1393 |
5.97e-29 |
|
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: 116.83 E-value: 5.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGL--PLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKL 1227
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPvlfigtvRSNLDPwdQYT-----------------DAQIWEALEKTHI-KDMVSQLPNSLhsevtdngenfSV 1289
Cdd:COG1124 82 QMVFQDP-------YASLHP--RHTvdrilaeplrihglpdrEERIAELLEQVGLpPSFLDRYPHQL-----------SG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1290 GERQLLCVARALLRHSKILLLDEATAAID----TETDRLIQDTIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILE 1364
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDvsvqAEILNLLKDLREE--RGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVE 219
|
250 260
....*....|....*....|....*....
gi 1207190976 1365 FDTPSNLLTDENSRFHAMMEAAEETFSRP 1393
Cdd:COG1124 220 ELTVADLLAGPKHPYTRELLAASLAFERA 248
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1151-1361 |
3.27e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 111.57 E-value: 3.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1151 TFQDVEMRYRDGLplVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVI 1230
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1231 PQepvlfigtvrsnldpwdqytdaqiwealekthikdmvsqlpnslhsevtdngenFSVGERQLLCVARALLRHSKILLL 1310
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1311 DEATAAIDTETDRLIQDTIRSSF-SGCTTLVIAHRLNTV-LGCNRIMVLDQGQ 1361
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1150-1374 |
8.61e-28 |
|
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: 119.62 E-value: 8.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLP---LVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIG---LEDL 1223
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1224 RSKLSVIPQEPVLFI---GTVRSNL-DPWDQY---TDAQIW----EALEKTHI-KDMVSQLPNSlhsevtdngenFSVGE 1291
Cdd:COG1123 341 RRRVQMVFQDPYSSLnprMTVGDIIaEPLRLHgllSRAERRervaELLERVGLpPDLADRYPHE-----------LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1292 RQLLCVARALLRHSKILLLDEATAAIDTETD----RLIQDtIRSSFsGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFD 1366
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQaqilNLLRD-LQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
....*...
gi 1207190976 1367 TPSNLLTD 1374
Cdd:COG1123 488 PTEEVFAN 495
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1153-1363 |
6.36e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 108.68 E-value: 6.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1153 QDVEMRYRDGLplVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQ 1232
Cdd:cd03214 3 ENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1233 epvlfigtvrsnldpwdqytdaqiweALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDE 1312
Cdd:cd03214 81 --------------------------ALELLGLAHLADRPFNEL-----------SGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 1313 ATAAID----TETDRLIQDTIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQIL 1363
Cdd:cd03214 124 PTSHLDiahqIELLELLRRLARE--RGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
587-740 |
8.12e-27 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 118.31 E-value: 8.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 587 VAQQAWILNDSLRENILFGK-KYNEEK--YNAVLEACCLFpdIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERP 663
Cdd:TIGR01846 536 VLQENVLFSRSIRDNIALCNpGAPFEHviHAAKLAGAHDF--ISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPR 613
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 664 ILLLDDPLSAVDARvGSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALF 740
Cdd:TIGR01846 614 ILIFDEATSALDYE-SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLW 689
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
560-703 |
1.42e-26 |
|
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: 115.92 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGGFA-------------YVAQQAWILNDSLRENILFGKK-YNEEKYNAVLEACCLFPD 625
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVTLDGVPVssldqdevrrrvsVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADW 453
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 626 IIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHsAIRPAAKGKTVIFVTHQL 703
Cdd:TIGR02868 454 LRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLE-DLLAALSGRTVVLITHHL 530
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1111-1344 |
1.82e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.06 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1111 ARFTS-VERINHYIKNLE-SEGPRQITGCPTSSsswpAEGQITFQDVEMRYRDGLPLVlKNLCFSILPEETIGIVGRTGS 1188
Cdd:COG4178 326 AEWRAtVDRLAGFEEALEaADALPEAASRIETS----EDGALALEDLTLRTPDGRPLL-EDLSLSLKPGERLLITGPSGS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1189 GKSSLgvalFR-LAEL---SRGSIII-DGVNIAhigledlrsklsVIPQEPVLFIGTVRSNL---DPWDQYTDAQIWEAL 1260
Cdd:COG4178 401 GKSTL----LRaIAGLwpyGSGRIARpAGARVL------------FLPQRPYLPLGTLREALlypATAEAFSDAELREAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1261 EKTHIKDMVSQLpnslhSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLV 1340
Cdd:COG4178 465 EAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVIS 539
|
....
gi 1207190976 1341 IAHR 1344
Cdd:COG4178 540 VGHR 543
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1152-1361 |
2.45e-26 |
|
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: 108.32 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1152 FQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIP 1231
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1232 QEP--VLFIGTVRS-------NLdPWDQYTDAQ-IWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARAL 1301
Cdd:cd03225 82 QNPddQFFGPTVEEevafgleNL-GLPEEEIEErVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 1302 LRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIA-HRLNTVLG-CNRIMVLDQGQ 1361
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
584-739 |
3.03e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 115.50 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 584 FAYVAQQAWILNDSLRENILF--GKKYNEEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSE 661
Cdd:PRK11176 419 VALVSQNVHLFNDTIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 662 RPILLLDDPLSAVDARvGSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAAL 739
Cdd:PRK11176 499 SPILILDEATSALDTE-SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
560-724 |
1.09e-25 |
|
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: 106.46 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG--------FAYVAQQAWILND---SLRENIL--------FGKKYNEEKYNAVLEAc 620
Cdd:cd03235 38 KSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRSIDRDfpiSVRDVVLmglyghkgLFRRLSKADKAKVDEA- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 621 clfpdiieLPYGDMTEIGERG-ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRP-AAKGKTVIF 698
Cdd:cd03235 117 --------LERVGLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK-TQEDIYELLRElRREGMTILV 187
|
170 180
....*....|....*....|....*..
gi 1207190976 699 VTHQLQYLPE-CDDVVLMKDGQIAeHG 724
Cdd:cd03235 188 VTHDLGLVLEyFDRVLLLNRTVVA-SG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1150-1364 |
2.36e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 105.90 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGlPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHI---GLEDLRSK 1226
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1227 LSVIPQ-----------EPVLF----IGTVRSNLdpwdqytDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGE 1291
Cdd:COG2884 81 IGVVFQdfrllpdrtvyENVALplrvTGKSRKEI-------RRRVREVLDLVGLSDKAKALPHEL-----------SGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 1292 RQLLCVARALLRHSKILLLDEATAAIDTET-DRLIQ--DTIRSsfSGcTTLVIA-HRLNTVLGCN-RIMVLDQGQILE 1364
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETsWEIMEllEEINR--RG-TTVLIAtHDLELVDRMPkRVLELEDGRLVR 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
560-725 |
2.44e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.33 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG--------FAYVAQQAWILND---SLRENILFG--------KKYNEEKYNAVLEAc 620
Cdd:COG1121 45 KSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQRAEVDWDfpiTVRDVVLMGrygrrglfRRPSRADREAVDEA- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 621 clfpdiIELpyGDMTE-----IGErganLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRP-AAKGK 694
Cdd:COG1121 124 ------LER--VGLEDladrpIGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA-TEEALYELLRElRREGK 190
|
170 180 190
....*....|....*....|....*....|..
gi 1207190976 695 TVIFVTHQLQYLPE-CDDVVLMKDGQIAeHGT 725
Cdd:COG1121 191 TILVVTHDLGAVREyFDRVLLLNRGLVA-HGP 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
586-740 |
2.47e-25 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 106.03 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 586 YVAQQAWILNDSLRENILF---GKKYNEEKYNAVLEACCLFpdIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSER 662
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALadpGMSMERVIEAAKLAGAHDF--ISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 663 PILLLDDPLSAVDARvGSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALF 740
Cdd:cd03252 158 RILIFDEATSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
560-732 |
2.50e-25 |
|
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: 112.53 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG-------------FAYVAQQAWILNDSLRENI-LFGKKyNEEKynaVLEACCL--- 622
Cdd:COG4618 371 KSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQDVELFDGTIAENIaRFGDA-DPEK---VVAAAKLagv 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 623 --FpdIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRPA-AKGKTVIFV 699
Cdd:COG4618 447 heM--ILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDE-GEAALAAAIRALkARGATVVVI 523
|
170 180 190
....*....|....*....|....*....|...
gi 1207190976 700 THQLQYLPECDDVVLMKDGQIAEHGTHTQLMEK 732
Cdd:COG4618 524 THRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
595-746 |
4.26e-25 |
|
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: 112.22 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 595 NDSLRENILFGK-KYNEEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSA 673
Cdd:COG5265 445 NDTIAYNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 674 VDARVgSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFNSVQQE 746
Cdd:COG5265 525 LDSRT-ERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEE 596
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
560-743 |
4.39e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.84 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGK-KYNEEKYNAVLEACCLfPD 625
Cdd:PRK11160 379 KSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAISVVSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGL-EK 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 626 IIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRPAAKGKTVIFVTHQLQY 705
Cdd:PRK11160 458 LLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIL-ELLAEHAQNKTVLMITHRLTG 536
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207190976 706 LPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFNSV 743
Cdd:PRK11160 537 LEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
560-732 |
5.25e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 105.15 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG------------FAYVAQQAWILND-SLRENILF-------GKKYNEEKYNAVLEA 619
Cdd:COG1131 39 KTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALYPDlTVRENLRFfarlyglPRKEARERIDELLEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 620 CclfpdiielpygDMTE-IGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRP-AAKGKTVI 697
Cdd:COG1131 119 F------------GLTDaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP-EARRELWELLRElAAEGKTVL 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207190976 698 FVTHqlqYLPE----CDDVVLMKDGQIAEHGTHTQLMEK 732
Cdd:COG1131 186 LSTH---YLEEaerlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1150-1376 |
8.21e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 104.79 E-value: 8.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDglPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHigledLRSKLSV 1229
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQE-------PVLFIGTVRSNLDP----WDQYTDAQ---IWEALEKTHIKDM----VSQLpnslhsevtdngenfSVGE 1291
Cdd:COG1121 80 VPQRaevdwdfPITVRDVVLMGRYGrrglFRRPSRADreaVDEALERVGLEDLadrpIGEL---------------SGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1292 RQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQIlEFDTPS 1369
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLV-AHGPPE 223
|
....*..
gi 1207190976 1370 NLLTDEN 1376
Cdd:COG1121 224 EVLTPEN 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1150-1372 |
1.12e-24 |
|
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: 104.20 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLV--LKNLCFSILPEETIGIVGRTGSGKSSLgVALFRLAEL-SRGSIIIDGVNIAHI---GLEDL 1223
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLERpTSGSVLVDGTDLTLLsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1224 RSKLSVIPQEPVLFIG-TVRSN------LDPWDQ-YTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLL 1295
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENvalpleIAGVPKaEIEERVLELLELVGLEDKADAYPAQL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1296 CVARALLRHSKILLLDEATAAIDTETDR----LIQDtIRSSFsGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSN 1370
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQsilaLLRD-INREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
..
gi 1207190976 1371 LL 1372
Cdd:cd03258 228 VF 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1150-1362 |
3.00e-24 |
|
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: 102.57 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLP--LVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDL---- 1223
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1224 RSKLSVIPQE----PVLfigTVRSNL--------DPWDQYtDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGE 1291
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVelplllagVPKKER-RERAEELLERVGLGDRLNHYPSEL-----------SGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1292 RQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRS--SFSGCTTLVIAHRLNTVLGCNRIMVLDQGQI 1362
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1149-1357 |
3.41e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 110.89 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1149 QITFQDVEMRY--RDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIII-DGVNIAHIGLEDLRS 1225
Cdd:PTZ00265 382 KIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1226 KLSVIPQEPVLFIGTVRSNL-------------------DPWDQYT---------------------------------- 1252
Cdd:PTZ00265 461 KIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrkn 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1253 -----DAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQD 1327
Cdd:PTZ00265 541 yqtikDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260 270
....*....|....*....|....*....|...
gi 1207190976 1328 TIrSSFSGC---TTLVIAHRLNTVLGCNRIMVL 1357
Cdd:PTZ00265 621 TI-NNLKGNenrITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1150-1369 |
4.35e-24 |
|
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: 102.26 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLplVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAEL-----SRGSIIIDGVNIAHIG--LED 1222
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDvdVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1223 LRSKLSVIPQEPVLFIGTVRSNLD--PWDQ------YTDAQIWEALEKTHIKDMVSQLPNSLHsevtdngenFSVGERQL 1294
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAygLRLHgiklkeELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 1295 LCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRsSFSGCTTLVIA-HRLNTVLGC-NRIMVLDQGQILEFDTPS 1369
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIA-ELKKEYTIVIVtHNMQQAARVaDRTAFLLNGRLVEFGPTE 225
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
535-741 |
5.47e-24 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 109.06 E-value: 5.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 535 KTLHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLREN 601
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhtlrqFINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 602 ILFGKKYN--EEKYNAVLEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVG 679
Cdd:TIGR01193 568 LLLGAKENvsQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 680 SRLFHSAIRpaAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFN 741
Cdd:TIGR01193 648 KKIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1150-1361 |
5.80e-24 |
|
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: 100.34 E-value: 5.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYrdGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIG--LEDLRSKL 1227
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPVLFIG-TVRSNLdpwdqytdaqiwealekthikdmvsqlpnslhsevtdnGENFSVGERQLLCVARALLRHSK 1306
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI--------------------------------------ALGLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 1307 ILLLDEATAAIDTETDRLIQDTIRSSF--SGCTTLVIAHRLNTVLG-CNRIMVLDQGQ 1361
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQaqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1150-1361 |
2.20e-23 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 99.47 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDG---LPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALfrLAELSR--GSIIIDGvniahigledlr 1224
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEKlsGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1225 sKLSVIPQEPVLFIGTVRSNL---DPWDQ--YtdaqiWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVAR 1299
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENIlfgKPFDEerY-----EKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1300 ALLRHSKILLLDEATAAIDTET-DRLIQDTIRSSFSGCTTLVIA-HRLNTVLGCNRIMVLDQGQ 1361
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNKTRILVtHQLQLLPHADQIVVLDNGR 204
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
513-732 |
2.43e-23 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 106.28 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 513 HMEQESPQSTISSTQ-SIRPPL--HKTLHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMTLLGGSVSVNGG------ 583
Cdd:TIGR01842 307 AMPLPEPEGHLSVENvTIVPPGgkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAdlkqwd 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 584 -------FAYVAQQAWILNDSLRENIL-FGKKYNEEKynaVLEACCL---FPDIIELPYGDMTEIGERGANLSGGQRQRV 652
Cdd:TIGR01842 387 retfgkhIGYLPQDVELFPGTVAENIArFGENADPEK---IIEAAKLagvHELILRLPDGYDTVIGPGGATLSGGQRQRI 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 653 SLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRPA-AKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLME 731
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDE-EGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
.
gi 1207190976 732 K 732
Cdd:TIGR01842 543 K 543
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1150-1379 |
2.53e-22 |
|
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: 97.76 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLVlKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSV 1229
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLF--------IGTVRSnLDPWDQYT-DAQIWEALEkthikdMVSQLPNSLHSEVTDngeNFSVGERQLLCVARA 1300
Cdd:cd03295 80 VIQQIGLFphmtveenIALVPK-LLKWPKEKiRERADELLA------LVGLDPAEFADRYPH---ELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1301 LLRHSKILLLDEATAAIDTETDRLIQDTIR--SSFSGCTTLVIAHRLNT--VLGcNRIMVLDQGQILEFDTPSNLLTDEN 1376
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEafRLA-DRIAIMKNGEIVQVGTPDEILRSPA 228
|
...
gi 1207190976 1377 SRF 1379
Cdd:cd03295 229 NDF 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
560-714 |
3.26e-22 |
|
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: 96.01 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG------------FAYVAQQ-AWILNDSLRENILF-----GKKYNEEKYNAVLEACC 621
Cdd:COG4133 41 KTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLGHAdGLKPELTVRENLRFwaalyGLRADREAIDEALEAVG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 622 LfPDIIELPYGdmteigergaNLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIR-PAAKGKTVIFVT 700
Cdd:COG4133 121 L-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-GVALLAELIAaHLARGGAVLLTT 188
|
170
....*....|....
gi 1207190976 701 HQLQYLPECDDVVL 714
Cdd:COG4133 189 HQPLELAAARVLDL 202
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
584-739 |
4.27e-22 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 103.10 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 584 FAYVAQQAWILNDSLRENI-LFGKKYNEEkynAVLEAC---CLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLARALY 659
Cdd:TIGR03796 555 VAMVDQDIFLFEGTVRDNLtLWDPTIPDA---DLVRACkdaAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALV 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 660 SERPILLLDDPLSAVDARVGSRLFHSAIRpaaKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAAL 739
Cdd:TIGR03796 632 RNPSILILDEATSALDPETEKIIDDNLRR---RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1150-1378 |
4.82e-22 |
|
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: 96.42 E-value: 4.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLplVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAH---IGLEDLRSK 1226
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1227 LSVIPQEPVLFIG-TVRSNLD-PWDQYT---DAQIWE-ALEKTH---IKDMVSQLPNSLhsevtdngenfSVGERQLLCV 1297
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfPLREHTrlsEEEIREiVLEKLEavgLRGAEDLYPAEL-----------SGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1298 ARALLRHSKILLLDEATAAID----TETDRLIQDTIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLL 1372
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKE--LGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELR 225
|
....*.
gi 1207190976 1373 TDENSR 1378
Cdd:cd03261 226 ASDDPL 231
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
868-1123 |
4.94e-22 |
|
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: 98.06 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 868 QYYSRVYVLSMGAALFLKTI----RGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDvRLA 943
Cdd:cd18559 34 QEHGQVYLSVLGALAILQGItvfqYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVD-SMA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 944 MQAEML----LQNV-TLVLFCLGVVGAVFpwflfSIIPLGAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLS 1018
Cdd:cd18559 113 PQVIKMwmgpLQNViGLYLLILLAGPMAA-----VGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGIS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1019 TIYAYGRGADFIHRYQALLDtNQACQFLFSCAMRWLAVRLDLISISLITTVALLIVLMHGHISpAYAGLALSYAVQLTGL 1098
Cdd:cd18559 188 VIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLA-GLVALKVFYSLALTTY 265
|
250 260
....*....|....*....|....*
gi 1207190976 1099 FQFTVRLLSETEARFTSVERINHYI 1123
Cdd:cd18559 266 LNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
560-725 |
6.16e-22 |
|
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: 96.65 E-value: 6.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG-------------FAYVAQQAwILNDSL--RENILFG--------KKYNEEKYNAV 616
Cdd:COG1120 40 KSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAYVPQEP-PAPFGLtvRELVALGryphlglfGRPSAEDREAV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 617 LEACCLFpdiielpygDMTEIGERGAN-LSGGQRQRVSLARALYSERPILLLDDPLSAVD----ARVGSRLFHSAirpAA 691
Cdd:COG1120 119 EEALERT---------GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLA---RE 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207190976 692 KGKTVIFVTHQL----QYlpeCDDVVLMKDGQIAEHGT 725
Cdd:COG1120 187 RGRTVVMVLHDLnlaaRY---ADRLVLLKDGRIVAQGP 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1150-1366 |
6.32e-22 |
|
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: 95.66 E-value: 6.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLplVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEdlRSKLSV 1229
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFIG-TVRSNL--------DPWDQyTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARA 1300
Cdd:cd03259 77 VFQDYALFPHlTVAENIafglklrgVPKAE-IRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1301 LLRHSKILLLDEATAAIDTETDRLIQDTIRSSFS--GCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFD 1366
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1152-1360 |
6.82e-22 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 95.29 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1152 FQDVEMRYRDglPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIahiglEDLRSKLSVIP 1231
Cdd:cd03235 2 VEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1232 QE-------PVLFIGTVRSNLDP----WDQYTDAQ---IWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCV 1297
Cdd:cd03235 75 QRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSELADRQIGEL-----------SGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1298 ARALLRHSKILLLDEATAAIDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQG 1360
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
560-724 |
7.43e-22 |
|
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: 94.42 E-value: 7.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSvnggfayvaqqawilndslreniLFGKKYNEEKYNAVLEACCLFPDIIELPygDMTEIGE 639
Cdd:cd03214 38 KSTLLKTLAGLLKPSSGEIL-----------------------LDGKDLASLSPKELARKIAYVPQALELL--GLAHLAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 640 RGAN-LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAA-KGKTVIFVTHQL----QYlpeCDDVV 713
Cdd:cd03214 93 RPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLnlaaRY---ADRVI 169
|
170
....*....|.
gi 1207190976 714 LMKDGQIAEHG 724
Cdd:cd03214 170 LLKDGRIVAQG 180
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1150-1378 |
9.31e-22 |
|
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: 95.82 E-value: 9.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDglPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIG---LEDLRSK 1226
Cdd:COG1127 6 IEVRNLTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1227 LSVIPQEPVLFIG-TVRSNLD-PWDQYTD---AQI----WEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCV 1297
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAfPLREHTDlseAEIrelvLEKLELVGLPGAADKMPSEL-----------SGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1298 ARALLRHSKILLLDEATAAID----TETDRLIQDtIRSSFsGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLL 1372
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDpitsAVIDELIRE-LRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELL 230
|
....*.
gi 1207190976 1373 TDENSR 1378
Cdd:COG1127 231 ASDDPW 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
560-747 |
9.36e-22 |
|
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: 96.08 E-value: 9.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGgFAYVAQQAWILND--------------SLRENILFgkkYNEEKYNAVLEACCLFPD 625
Cdd:COG4555 40 KTTLLRMLAGLLKPDSGSILIDG-EDVRKEPREARRQigvlpderglydrlTVRENIRY---FAELYGLFDEELKKRIEE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 626 IIELPygDMTEIGERGA-NLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRPAAK-GKTVIFVTHQL 703
Cdd:COG4555 116 LIELL--GLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM-ARRLLREILRALKKeGKTVLFSSHIM 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207190976 704 QYLPE-CDDVVLMKDGQIAEHGTHTQLMEKGRD---YAALFNSVQQEN 747
Cdd:COG4555 193 QEVEAlCDRVVILHKGKVVAQGSLDELREEIGEenlEDAFVALIGSEE 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
560-720 |
1.37e-21 |
|
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: 93.23 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGgfayvaQQAWILNDSLRENIlfgkkyneekynavleacCLFPDIIELpYGDMTeiGE 639
Cdd:cd03230 39 KTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRI------------------GYLPEEPSL-YENLT--VR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 640 RGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRP-AAKGKTVIFVTHQLQYLPE-CDDVVLMKD 717
Cdd:cd03230 92 ENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNN 170
|
...
gi 1207190976 718 GQI 720
Cdd:cd03230 171 GRI 173
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1150-1376 |
2.49e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 95.44 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSV 1229
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEP-VLFIG-TVRS---------NLDPwdQYTDAQIWEALEKTHIKDMVSQLPnslhsevtdngENFSVGERQLLCVA 1298
Cdd:PRK13632 88 IFQNPdNQFIGaTVEDdiafglenkKVPP--KKMKDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1299 RALLRHSKILLLDEATAAIDTETDRLIQDTIRS-SFSGCTTLV-IAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTDEN 1376
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlRKTRKKTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
560-736 |
5.89e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 99.02 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGKKYNEEKYNAVLEACCLFPDI 626
Cdd:PRK10790 380 KSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 627 IELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDArvGS-RLFHSAIRPAAKGKTVIFVTHQLQY 705
Cdd:PRK10790 460 RSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDS--GTeQAIQQALAAVREHTTLVVIAHRLST 537
|
170 180 190
....*....|....*....|....*....|..
gi 1207190976 706 LPECDDVVLMKDGQIAEHGTHTQLME-KGRDY 736
Cdd:PRK10790 538 IVEADTILVLHRGQAVEQGTHQQLLAaQGRYW 569
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
560-724 |
6.86e-21 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 92.58 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-----------GFAYVAQQaWIL--NDSLRENILFG----KKYNEEKYNAVLEaccl 622
Cdd:cd03259 39 KTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQD-YALfpHLTVAENIAFGlklrGVPKAEIRARVRE---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 623 fpdIIELpyGDMTEIGERGAN-LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFH--SAIRpAAKGKTVIFV 699
Cdd:cd03259 114 ---LLEL--VGLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREelKELQ-RELGITTIYV 187
|
170 180
....*....|....*....|....*.
gi 1207190976 700 TH-QLQYLPECDDVVLMKDGQIAEHG 724
Cdd:cd03259 188 THdQEEALALADRIAVMNEGRIVQVG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
560-720 |
7.32e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 92.19 E-value: 7.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG-------------FAYVAQQAWILNDSLRENILF-----GKKYNEEKYNAVLEACC 621
Cdd:COG4619 39 KSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 622 LFPDIIELPYgdmteigergANLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIR--PAAKGKTVIFV 699
Cdd:COG4619 119 LPPDILDKPV----------ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP-ENTRRVEELLReyLAEEGRAVLWV 187
|
170 180
....*....|....*....|....
gi 1207190976 700 TH---QLQYLpeCDDVVLMKDGQI 720
Cdd:COG4619 188 SHdpeQIERV--ADRVLTLEAGRL 209
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
585-739 |
7.42e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.49 E-value: 7.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 585 AYVAQQAWILNDSLRENILFGKK--YNEEKYNAVLEACCLfpDIIEL-PYGDMTEIGERGANLSGGQRQRVSLARALYSE 661
Cdd:PRK13657 412 AVVFQDAGLFNRSIEDNIRVGRPdaTDEEMRAAAERAQAH--DFIERkPDGYDTVVGERGRQLSGGERQRLAIARALLKD 489
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 662 RPILLLDDPLSAVDARVGSRLfHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAAL 739
Cdd:PRK13657 490 PPILILDEATSALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
599-725 |
9.36e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.60 E-value: 9.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 599 RENILFG-------KKYNEEKYNAVLEaccLFpdiielpygDMTEIGER-GANLSGGQRQRVSLARALYSERPILLLDDP 670
Cdd:COG1118 93 AENIAFGlrvrppsKAEIRARVEELLE---LV---------QLEGLADRyPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 671 LSAVDARVGSRL------FHSAIrpaakGKTVIFVTH-QLQYLPECDDVVLMKDGQIAEHGT 725
Cdd:COG1118 161 FGALDAKVRKELrrwlrrLHDEL-----GGTTVFVTHdQEEALELADRVVVMNQGRIEQVGT 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1146-1369 |
1.35e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.54 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1146 AEGQITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRS 1225
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1226 KLSVIPQEP-VLFIG-TVRSNLD--------PWDQYTDaQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLL 1295
Cdd:PRK13635 82 QVGMVFQNPdNQFVGaTVQDDVAfglenigvPREEMVE-RVDQALRQVGMEDFLNREPHRL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 1296 CVARALLRHSKILLLDEATAAIDTETDRLIQDTIR--SSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPS 1369
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
579-740 |
1.93e-20 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 97.27 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 579 SVNGGFAYVAQQAWILNDSLRENILFGKK--YNEEKYNAVlEACCLFPDIIELPYGDMTEIGERGANLSGGQRQRVSLAR 656
Cdd:TIGR01192 406 SLRKSIATVFQDAGLFNRSIRENIRLGREgaTDEEVYEAA-KAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIAR 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 657 ALYSERPILLLDDPLSAVDARVGSRLfHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDY 736
Cdd:TIGR01192 485 AILKNAPILVLDEATSALDVETEARV-KNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRF 563
|
....
gi 1207190976 737 AALF 740
Cdd:TIGR01192 564 YKLL 567
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1166-1362 |
2.32e-20 |
|
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: 91.05 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNI--AHIGLEDLRSKLSVIPQEPVLFigtvrS 1243
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLF-----P 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1244 NLDPWDQYTDAQIW--------------EALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILL 1309
Cdd:cd03262 90 HLTVLENITLAPIKvkgmskaeaeeralELLEKVGLADKADAYPAQL-----------SGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1310 LDEATAAIDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQI 1362
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1153-1375 |
2.67e-20 |
|
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: 91.34 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1153 QDVEMRYrDGLpLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGlEDLRSKLSVIP- 1231
Cdd:cd03219 4 RGLTKRF-GGL-VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIGRt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1232 -QEPVLFIG-TVRSNLD---------------PWDQYTDA--QIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGER 1292
Cdd:cd03219 81 fQIPRLFPElTVLENVMvaaqartgsglllarARREEREAreRAEELLERVGLADLADRPAGEL-----------SYGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1293 QLLCVARALLRHSKILLLDEATAAI-DTETDRLIqDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPS 1369
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLnPEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPD 228
|
....*.
gi 1207190976 1370 NLLTDE 1375
Cdd:cd03219 229 EVRNNP 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1166-1374 |
4.31e-20 |
|
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: 90.57 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLED-LRSKLSVIPQEPVLFIG-TVRS 1243
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1244 NLD-PWDQYTDAQIWEALEKthIKDMVSQLPNSLHSEvtdnGENFSVGERQLLCVARALLRHSKILLLDEATA----AID 1318
Cdd:cd03224 95 NLLlGAYARRRAKRKARLER--VYELFPRLKERRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEglapKIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 1319 TETDRLIQDtIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTD 1374
Cdd:cd03224 169 EEIFEAIRE-LRD--EGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
560-724 |
5.82e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.91 E-value: 5.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG------------FAYVAQQAWILNDSLRENIlfgkkyneekynavleacclfpdii 627
Cdd:cd03247 41 KSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTTLRNNL------------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 628 elpygdmteigerGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRPAAKGKTVIFVTHQLQYLP 707
Cdd:cd03247 96 -------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIE 161
|
170
....*....|....*..
gi 1207190976 708 ECDDVVLMKDGQIAEHG 724
Cdd:cd03247 162 HMDKILFLENGKIIMQG 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
644-719 |
7.44e-20 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 87.69 E-value: 7.44e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQ 719
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
560-722 |
7.99e-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: 90.92 E-value: 7.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG--------GFAYVAQQawilnDSL------RENILFG----KKYNEEKYNAVLEAcc 621
Cdd:COG1116 50 KSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQE-----PALlpwltvLDNVALGlelrGVPKAERRERAREL-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 622 lfpdiIELpygdmteIGERGA------NLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLfHSAIRP--AAKG 693
Cdd:COG1116 123 -----LEL-------VGLAGFedayphQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERL-QDELLRlwQETG 189
|
170 180 190
....*....|....*....|....*....|....
gi 1207190976 694 KTVIFVTHQLQ---YLpeCDDVVLMKD--GQIAE 722
Cdd:COG1116 190 KTVLFVTHDVDeavFL--ADRVVVLSArpGRIVE 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
560-720 |
3.25e-19 |
|
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: 88.30 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG-------------FAYVAQQAWILNDSLRENILFG-KKYNEEKYNAVLEACCLFPD 625
Cdd:cd03248 53 KSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQDNIAYGlQSCSFECVKEAAQKAHAHSF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 626 IIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRPAAKGKTVIFVTHQLQY 705
Cdd:cd03248 133 ISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQVQQALYDWPERRTVLVIAHRLST 211
|
170
....*....|....*
gi 1207190976 706 LPECDDVVLMKDGQI 720
Cdd:cd03248 212 VERADQILVLDGGRI 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
560-724 |
3.70e-19 |
|
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: 87.74 E-value: 3.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-----------------GFAYVAQQAWIL-NDSLRENILFG--KKYNEEKYNAVLEA 619
Cdd:cd03297 36 KSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQYALFpHLNVRENLAFGlkRKRNREDRISVDEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 620 CCLFpdiielpygDMTEIGERG-ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAK-GKTVI 697
Cdd:cd03297 116 LDLL---------GLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlNIPVI 186
|
170 180 190
....*....|....*....|....*....|
gi 1207190976 698 FVTH---QLQYLpeCDDVVLMKDGQIAEHG 724
Cdd:cd03297 187 FVTHdlsEAEYL--ADRIVVMEDGRLQYIG 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1167-1364 |
4.11e-19 |
|
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: 92.83 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAElSRGSIIIDGVNIAHIG---LEDLRSKLSVIPQEP--------- 1234
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPfgslsprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1235 ----------VLFIGtvrsnLDPWDQytDAQIWEALEKTHIKdmvsqlPNSLH---SEvtdngenFSVGERQLLCVARAL 1301
Cdd:COG4172 381 vgqiiaeglrVHGPG-----LSAAER--RARVAEALEEVGLD------PAARHrypHE-------FSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1302 LRHSKILLLDEATAAIdtetDRLIQDTIRSSFS------GCTTLVIAHRLNTV--LgCNRIMVLDQGQILE 1364
Cdd:COG4172 441 ILEPKLLVLDEPTSAL----DVSVQAQILDLLRdlqrehGLAYLFISHDLAVVraL-AHRVMVMKDGKVVE 506
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
560-724 |
6.05e-19 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 87.18 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG----------------FAYVAQQA-----------WILNDSLRenILFGKKYNEEK 612
Cdd:cd03257 44 KSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrkeIQMVFQDPmsslnprmtigEQIAEPLR--IHGKLSKKEAR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 613 YNAVLEACCLFPDiielpygdmteiGERGAN-----LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGS---RLFH 684
Cdd:cd03257 122 KEAVLLLLVGVGL------------PEEVLNrypheLSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAqilDLLK 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207190976 685 SAIRpaAKGKTVIFVTHQL---QYLpeCDDVVLMKDGQIAEHG 724
Cdd:cd03257 190 KLQE--ELGLTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
560-720 |
8.43e-19 |
|
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: 85.35 E-value: 8.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG-------------FAYVAQQAWILNDSLRENILfgkkyneekynavleacclfpdi 626
Cdd:cd03246 41 KSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAENIL----------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 627 ielpygdmteigerganlSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRPA-AKGKTVIFVTHQLQY 705
Cdd:cd03246 98 ------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVE-GERALNQAIAALkAAGATRIVIAHRPET 158
|
170
....*....|....*
gi 1207190976 706 LPECDDVVLMKDGQI 720
Cdd:cd03246 159 LASADRILVLEDGRV 173
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1166-1362 |
1.40e-18 |
|
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: 84.40 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGvniahigledlrsklsvipqEPVLFigtvrsnL 1245
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSF-------A 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1246 DPWDQyTDAQIWealekthikdMVSQLpnslhsevtdngenfSVGERQLLCVARALLRHSKILLLDEATAAI-DTETDRL 1324
Cdd:cd03216 68 SPRDA-RRAGIA----------MVYQL---------------SVGERQMVEIARALARNARLLILDEPTAALtPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1207190976 1325 IqDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQI 1362
Cdd:cd03216 122 F-KVIRRlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1172-1368 |
1.87e-18 |
|
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: 88.19 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1172 FSILPEETIGIVGRTGSGKSSLGVALFRLAE---LSRGSIIIDGVNIAHIGLEDLR----SKLSVIPQEPVlfigtvrSN 1244
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPM-------TS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1245 LDPwdQYT-DAQIWEALE----------KTHIKDMVSQ--LPNSL-------HsevtdngeNFSVGERQLLCVARALLRH 1304
Cdd:COG0444 99 LNP--VMTvGDQIAEPLRihgglskaeaRERAIELLERvgLPDPErrldrypH--------ELSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 1305 SKILLLDEATAAIDTETDR----LIQDtIRSSFsGCTTLVIAHRLNTVLG-CNRIMVLDQGQILE-------FDTP 1368
Cdd:COG0444 169 PKLLIADEPTTALDVTIQAqilnLLKD-LQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVEegpveelFENP 242
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
560-725 |
2.74e-18 |
|
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: 86.01 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQA-------WILNDSLRENI-LFGKKYNEEKYNAVLE 618
Cdd:COG1124 44 KSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrRVQMVFQDPyaslhprHTVDRILAEPLrIHGLPDREERIAELLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 619 ACCLFPDIIELpygdmteigeRGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGS---RLFHsAIRpAAKGKT 695
Cdd:COG1124 124 QVGLPPSFLDR----------YPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAeilNLLK-DLR-EERGLT 191
|
170 180 190
....*....|....*....|....*....|...
gi 1207190976 696 VIFVTHQL---QYLpeCDDVVLMKDGQIAEHGT 725
Cdd:COG1124 192 YLFVSHDLavvAHL--CDRVAVMQNGRIVEELT 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1149-1330 |
2.82e-18 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 84.84 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1149 QITFQDVEMRYRDglPLVLKNLCFSILPEETIGIVGRTGSGKSSlgvaLFR----LAELSRGSIIIDGVNIaHIGLEDLR 1224
Cdd:COG4133 2 MLEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTT----LLRilagLLPPSAGEVLWNGEPI-RDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1225 SKLSVIPQEPVLFIG-TVRSNLDPW-----DQYTDAQIWEALEK---THIKD-MVSQLpnslhsevtdngenfSVGERQL 1294
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRFWaalygLRADREAIDEALEAvglAGLADlPVRQL---------------SAGQKRR 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207190976 1295 LCVARALLRHSKILLLDEATAAIDTETDRLIQDTIR 1330
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
560-725 |
2.87e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 88.23 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-----------GFAYVAQqawilNDSL------RENILFG----KKYNEEKYNAVLE 618
Cdd:COG3842 44 KTTLLRMIAGFETPDSGRILLDGrdvtglppekrNVGMVFQ-----DYALfphltvAENVAFGlrmrGVPKAEIRARVAE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 619 ACclfpdiielpygDMTEIGERG----ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLfHSAIRP--AAK 692
Cdd:COG3842 119 LL------------ELVGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEM-REELRRlqREL 185
|
170 180 190
....*....|....*....|....*....|....
gi 1207190976 693 GKTVIFVTH-QLQYLPECDDVVLMKDGQIAEHGT 725
Cdd:COG3842 186 GITFIYVTHdQEEALALADRIAVMNDGRIEQVGT 219
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
560-739 |
3.61e-18 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 90.40 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGKKYNEEKYNAVLEACCLFPDI 626
Cdd:TIGR03797 492 KSTLLRLLLGFETPESGSVFYDGqdlagldvqavrrQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDI 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 627 IELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAkgkTVIFVTHQLQYL 706
Cdd:TIGR03797 572 RAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKV---TRIVIAHRLSTI 648
|
170 180 190
....*....|....*....|....*....|...
gi 1207190976 707 PECDDVVLMKDGQIAEHGTHTQLMEKGRDYAAL 739
Cdd:TIGR03797 649 RNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
560-725 |
5.06e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.44 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-----------GFAYVAQQaWILNDSL--RENILFG---KKYNEEKYNA-VLEACcl 622
Cdd:COG3839 42 KSTLLRMIAGLEDPTSGEILIGGrdvtdlppkdrNIAMVFQS-YALYPHMtvYENIAFPlklRKVPKAEIDRrVREAA-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 623 fpdiielpygDMTEIGE----RGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDA--RVGSRL----FHSAIrpaak 692
Cdd:COG3839 119 ----------ELLGLEDlldrKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAklRVEMRAeikrLHRRL----- 183
|
170 180 190
....*....|....*....|....*....|....
gi 1207190976 693 GKTVIFVTH-QLQYLPECDDVVLMKDGQIAEHGT 725
Cdd:COG3839 184 GTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
560-719 |
5.31e-18 |
|
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: 83.01 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGgfayvaQQAWILNDSLRENilfgkkynEEKYNAVLEACCLFP-----DIIELPygdm 634
Cdd:cd03229 39 KSTLLRCIAGLEEPDSGSILIDG------EDLTDLEDELPPL--------RRRIGMVFQDFALFPhltvlENIALG---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 635 teigerganLSGGQRQRVSLARALYSERPILLLDDPLSAVD--ARVGSRLFHSAIRpAAKGKTVIFVTHQLQYLPE-CDD 711
Cdd:cd03229 101 ---------LSGGQQQRVALARALAMDPDVLLLDEPTSALDpiTRREVRALLKSLQ-AQLGITVVLVTHDLDEAARlADR 170
|
....*...
gi 1207190976 712 VVLMKDGQ 719
Cdd:cd03229 171 VVVLRDGK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
560-722 |
6.62e-18 |
|
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: 84.06 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG--------GFAYVAQQA----WIlndSLRENILFG-------KKYNEEKYNAVLEAC 620
Cdd:cd03293 43 KSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQQDallpWL---TVLDNVALGlelqgvpKAEARERAEELLELV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 621 CL------FPdiielpygdmteigergANLSGGQRQRVSLARALYSERPILLLDDPLSAVDA--RVGSRLFHSAIRpAAK 692
Cdd:cd03293 120 GLsgfenaYP-----------------HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltREQLQEELLDIW-RET 181
|
170 180 190
....*....|....*....|....*....|....*
gi 1207190976 693 GKTVIFVTHQLQ---YLpeCDDVVLM--KDGQIAE 722
Cdd:cd03293 182 GKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVA 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
560-729 |
1.00e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 84.09 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG----------------GFAYVAQQAwILNDSL--RENILFGKKYN--------EEKY 613
Cdd:cd03261 39 KSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMGMLFQSG-ALFDSLtvFENVAFPLREHtrlseeeiREIV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 614 NAVLEACCLFPDIIELPygdmteigergANLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRP--AA 691
Cdd:cd03261 118 LEKLEAVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYDEPTAGLDP-IASGVIDDLIRSlkKE 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207190976 692 KGKTVIFVTHQLQYLPE-CDDVVLMKDGQIAEHGTHTQL 729
Cdd:cd03261 186 LGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1166-1375 |
1.22e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAElSRGSIIIDGVNIAHIG---LEDLRSKLSVIPQEPvlfigtvR 1242
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP-------N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1243 SNLDPwdQYTDAQIWEALEKTHIKDM---------------VSQLPNSLHSEVTDngenFSVGERQLLCVARALLRHSKI 1307
Cdd:PRK15134 373 SSLNP--RLNVLQIIEEGLRVHQPTLsaaqreqqviavmeeVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1308 LLLDEATAAIdtetDRLIQDTIRSSFSGCTT------LVIAHRLNTVLG-CNRIMVLDQGQILE-------FDTPSNLLT 1373
Cdd:PRK15134 447 IILDEPTSSL----DKTVQAQILALLKSLQQkhqlayLFISHDLHVVRAlCHQVIVLRQGEVVEqgdcervFAAPQQEYT 522
|
..
gi 1207190976 1374 DE 1375
Cdd:PRK15134 523 RQ 524
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1150-1344 |
1.77e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 81.43 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLVlKNLCFSILPEETIGIVGRTGSGKSSLgvalFR-LAEL---SRGSIIIDGvniahigledlRS 1225
Cdd:cd03223 1 IELENLSLATPDGRVLL-KDLSFEIKPGDRLLITGPSGTGKSSL----FRaLAGLwpwGSGRIGMPE-----------GE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1226 KLSVIPQEPVLFIGTVRSNLD-PWDQytdaqiwealekthikdmvsqlpnslhsevtdngeNFSVGERQLLCVARALLRH 1304
Cdd:cd03223 65 DLLFLPQRPYLPLGTLREQLIyPWDD-----------------------------------VLSGGEQQRLAFARLLLHK 109
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1207190976 1305 SKILLLDEATAAIDTETDRLIQDTIRSsfSGCTTLVIAHR 1344
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
560-672 |
1.88e-17 |
|
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: 80.77 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILND-SLRENILFG---KKYNEEKYNAVLEAccl 622
Cdd:pfam00005 24 KSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENLRLGlllKGLSKREKDARAEE--- 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 623 fpDIIELPYGDM--TEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLS 672
Cdd:pfam00005 101 --ALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
560-719 |
2.68e-17 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 82.13 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG-----------------FAYVAQQawILNDSLRENILFGKKY----NEEKYNAVLE 618
Cdd:cd03225 40 KSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkvglvFQNPDDQ--FFGPTVEEEVAFGLENlglpEEEIEERVEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 619 ACCLFpDIIEL----PYgdmteigergaNLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRP-AAKG 693
Cdd:cd03225 118 ALELV-GLEGLrdrsPF-----------TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPA-GRRELLELLKKlKAEG 184
|
170 180
....*....|....*....|....*..
gi 1207190976 694 KTVIFVTHQLQYLPE-CDDVVLMKDGQ 719
Cdd:cd03225 185 KTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
644-721 |
3.79e-17 |
|
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: 80.17 E-value: 3.79e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIA 721
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1150-1342 |
4.20e-17 |
|
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: 81.69 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHI---GLEDLRSK 1226
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1227 LSVIPQEPVLFigtvrSNLDPWDQ--------YTDAQIW-----EALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQ 1293
Cdd:cd03292 80 IGVVFQDFRLL-----PDRNVYENvafalevtGVPPREIrkrvpAALELVGLSHKHRALPAEL-----------SGGEQQ 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207190976 1294 LLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIA 1342
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1145-1382 |
5.06e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 82.44 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1145 PAEGQITFQDVEMRY--RDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLgvalFR----LAELSRGSIIIDGVNIAHI 1218
Cdd:COG1116 3 AAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRliagLEKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1219 GLEdlrskLSVIPQEPVLFigtvrsnldPW-----------------DQYTDAQIWEALEKTHIKDMVSQLPNSLhsevt 1281
Cdd:COG1116 79 GPD-----RGVVFQEPALL---------PWltvldnvalglelrgvpKAERRERARELLELVGLAGFEDAYPHQL----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1282 dngenfSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRS--SFSGCTTLVIAH------RLntvlgCNR 1353
Cdd:COG1116 140 ------SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADR 208
|
250 260 270
....*....|....*....|....*....|....*.
gi 1207190976 1354 IMVLDQ--GQILE-----FDTPSNLLTDENSRFHAM 1382
Cdd:COG1116 209 VVVLSArpGRIVEeidvdLPRPRDRELRTSPEFAAL 244
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1153-1375 |
5.10e-17 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 82.39 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1153 QDVEMRYrDGLpLVLKNLCFSILPEETIGIVGRTGSGKSSLgvalFRL----AELSRGSIIIDGVNI--------AHIGL 1220
Cdd:COG0411 8 RGLTKRF-GGL-VAVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLitgfYRPTSGRILFDGRDItglpphriARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1221 edLRS--------KLSVI--------PQEPVLFIGTVRSNLDPWDQYTDA--QIWEALEKTHIKDMVSQLPNSLhsevtd 1282
Cdd:COG0411 82 --ARTfqnprlfpELTVLenvlvaahARLGRGLLAALLRLPRARREEREAreRAEELLERVGLADRADEPAGNL------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1283 ngenfSVGERQLLCVARALLRHSKILLLDEATAAI-DTETDRLIqDTIRS--SFSGCTTLVIAHRLNTVLG-CNRIMVLD 1358
Cdd:COG0411 154 -----SYGQQRRLEIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRlrDERGITILLIEHDMDLVMGlADRIVVLD 227
|
250
....*....|....*..
gi 1207190976 1359 QGQILEFDTPSNLLTDE 1375
Cdd:COG0411 228 FGRVIAEGTPAEVRADP 244
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
560-720 |
5.24e-17 |
|
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: 81.38 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------------GFayVAQQAWILND-SLRENILFG-------KKYNEEK 612
Cdd:cd03255 43 KSTLLNILGGLDRPTSGEVRVDGtdisklsekelaafrrrhiGF--VFQSFNLLPDlTALENVELPlllagvpKKERRER 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 613 YNAVLEACCLfPDIIElpygdmteigERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRPAAK 692
Cdd:cd03255 121 AEELLERVGL-GDRLN----------HYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVM-ELLRELNK 188
|
170 180 190
....*....|....*....|....*....|
gi 1207190976 693 --GKTVIFVTHQLQYLPECDDVVLMKDGQI 720
Cdd:cd03255 189 eaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
560-730 |
6.18e-17 |
|
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: 84.00 E-value: 6.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-----------------GFAYVAQQAwilndSL------RENILFGKKYNEEKYNAV 616
Cdd:COG4148 38 KTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEA-----RLfphlsvRGNLLYGRKRAPRAERRI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 617 LeacclFPDIIELpygdmTEIG---ERG-ANLSGGQRQRVSLARALYSeRP-ILLLDDPLSAVDA-----------RVGS 680
Cdd:COG4148 113 S-----FDEVVEL-----LGIGhllDRRpATLSGGERQRVAIGRALLS-SPrLLLMDEPLAALDLarkaeilpyleRLRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 681 RLfhsAIrPaakgktVIFVTHQLQylpE----CDDVVLMKDGQIAEHGTHTQLM 730
Cdd:COG4148 182 EL---DI-P------ILYVSHSLD---EvarlADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
644-730 |
6.20e-17 |
|
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: 81.96 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAK-GKTVIFVTHQLQylpEC----DDVVLMKDG 718
Cdd:cd03295 136 LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDID---EAfrlaDRIAIMKNG 212
|
90
....*....|..
gi 1207190976 719 QIAEHGTHTQLM 730
Cdd:cd03295 213 EIVQVGTPDEIL 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
587-729 |
7.56e-17 |
|
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: 81.07 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 587 VAQQAWILNDSLRENILFGKKYNEEKYNAVLEAC---CLfpDIIELPygdmTEIGER--GANLSGGQRQRVSLARALYSE 661
Cdd:cd03260 86 VFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERveeAL--RKAALW----DEVKDRlhALGLSGGQQQRLCLARALANE 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 662 RPILLLDDPLSAVDaRVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPEC-DDVVLMKDGQIAEHGTHTQL 729
Cdd:cd03260 160 PEVLLLDEPTSALD-PISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
560-722 |
7.90e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 81.24 E-value: 7.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------------GFayVAQQAWILND-SLRENILF-------GKKYNEEK 612
Cdd:COG1136 47 KSTLLNILGGLDRPTSGEVLIDGqdisslserelarlrrrhiGF--VFQFFNLLPElTALENVALplllagvSRKERRER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 613 YNAVLEacclfpdiielpygdMTEIGERG----ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGS---RLFHS 685
Cdd:COG1136 125 ARELLE---------------RVGLGDRLdhrpSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEevlELLRE 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207190976 686 AIRpaAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAE 722
Cdd:COG1136 190 LNR--ELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1150-1374 |
1.48e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIG-LEDLRSKLS 1228
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1229 VIPQEP-VLFIG-TVRSNL---------DPWDqyTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCV 1297
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDLafgpenlclPPIE--IRKRVDRALAEIGLEKYRHRSPKTL-----------SGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 1298 ARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSF-SGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTD 1374
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1156-1373 |
1.67e-16 |
|
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: 81.15 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1156 EMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDL----RSKLSVIP 1231
Cdd:cd03294 29 EILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1232 QEPVLFIG-TVRSN---------LDPWDQYTDAQiwEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARAL 1301
Cdd:cd03294 109 QSFALLPHrTVLENvafglevqgVPRAEREERAA--EALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARAL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 1302 LRHSKILLLDEATAAIDTETDRLIQDTIR--SSFSGCTTLVIAHRLNTV--LGcNRIMVLDQGQILEFDTPSNLLT 1373
Cdd:cd03294 176 AVDPDILLMDEAFSALDPLIRREMQDELLrlQAELQKTIVFITHDLDEAlrLG-DRIAIMKDGRLVQVGTPEEILT 250
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
560-725 |
1.69e-16 |
|
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: 80.07 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG------GFAYVAQQAWIL---------NDSLRENILFG-------KKYNEEKYNAVL 617
Cdd:COG1122 40 KSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRKVGLVfqnpddqlfAPTVEEDVAFGpenlglpREEIRERVEEAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 618 EACclfpdiielpygDMTEIGERG-ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRP-AAKGKT 695
Cdd:COG1122 120 ELV------------GLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR-GRRELLELLKRlNKEGKT 186
|
170 180 190
....*....|....*....|....*....|.
gi 1207190976 696 VIFVTHQLQYLPE-CDDVVLMKDGQIAEHGT 725
Cdd:COG1122 187 VIIVTHDLDLVAElADRVIVLDDGRIVADGT 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
560-739 |
2.07e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.18 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG---GFAYVAQQ--AWILND-------SLRENILFGK----KYNEEKYNAVLEAcclf 623
Cdd:COG3840 38 KSTLLNLIAGFLPPDSGRILWNGqdlTALPPAERpvSMLFQEnnlfphlTVAQNIGLGLrpglKLTAEQRAQVEQA---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 624 pdiieLPYGDMTEIGER-GANLSGGQRQRVSLARALYSERPILLLDDPLSAVDarvgsrlfhsairPAAK---------- 692
Cdd:COG3840 114 -----LERVGLAGLLDRlPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD-------------PALRqemldlvdel 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 693 ----GKTVIFVTHQLQ-YLPECDDVVLMKDGQIAEHGTHTQLMEkGRDYAAL 739
Cdd:COG3840 176 crerGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLD-GEPPPAL 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1150-1374 |
2.46e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 82.05 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLV--LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHI---GLEDLR 1224
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1225 SKLSVIPQEPVLFIG-TVRSN------LDPWD-QYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLC 1296
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENvalpleIAGVPkAEIRKRVAELLELVGLSDKADAYPSQL-----------SGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1297 VARALLRHSKILLLDEATAAIDTETDR----LIQDtIRSSFsGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNL 1371
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRsildLLKD-INREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDV 228
|
...
gi 1207190976 1372 LTD 1374
Cdd:COG1135 229 FAN 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
560-731 |
2.56e-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: 83.80 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG----------------GFAYVAQQ-----------AWILNDSLRENILFGKKYNEEK 612
Cdd:COG1123 304 KSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQDpysslnprmtvGDIIAEPLRLHGLLSRAERRER 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 613 YNAVLEACCLFPDIIE-LPYGdmteigerganLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGS---RLFHSaIR 688
Cdd:COG1123 384 VAELLERVGLPPDLADrYPHE-----------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAqilNLLRD-LQ 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207190976 689 pAAKGKTVIFVTHQL---QYLpeCDDVVLMKDGQIAEHGTHTQLME 731
Cdd:COG1123 452 -RELGLTYLFISHDLavvRYI--ADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1150-1363 |
2.99e-16 |
|
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: 79.33 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRD--GLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEdLRSKL 1227
Cdd:cd03266 2 ITADALTKRFRDvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPVLFIG-TVRSNLdpwdQYTDAqiWEALEKTHIKDMVSQLPNSLHSEVTDN--GENFSVGERQLLCVARALLRH 1304
Cdd:cd03266 81 GFVSDSTGLYDRlTARENL----EYFAG--LYGLKGDELTARLEELADRLGMEELLDrrVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1305 SKILLLDEATAAIDTETDRLIQDTIRSSFS-GCTTLVIAHRLNTVLG-CNRIMVLDQGQIL 1363
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
140-427 |
3.58e-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: 80.72 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 140 MLVAIFSLLITMvaGFVGPALLiRALLEFSQCSEVKLLYGLALVAGIFLMELTRSWSLAFMWAINYRTAARLRGAALTFA 219
Cdd:cd18559 1 SFLLIKLVLCNH--VFSGPSNL-WLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 220 FQKILRL--RSTKDVSSGELVNICASDGQRLYEAVSVGCLLAGGPLVGMLGLTYTTYFLGPTALVGSAIFIIFYP-TMML 296
Cdd:cd18559 78 YHKALRSpiSFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPvNRVY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 297 ASRMTAYFRKKCVAvTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEER---RNLEWAGCVQSLTLGVAPVVVVI 373
Cdd:cd18559 158 AASSRQLKRLESVS-KDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELaylPSIVYLRALAVRLWCVGPCIVLF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 374 ASVCTFTLhMALGYDLTAAQAFTVVAVFNSMTFALKVTPLAVRALSEGSVAVKR 427
Cdd:cd18559 237 ASFFAYVS-RHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1159-1329 |
3.88e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1159 YRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFI 1238
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1239 GTVRSNLD-PWdqytdaQIW-EALEKTHIKDMVSQ--LPNSLhseVTDNGENFSVGERQLLCVARALLRHSKILLLDEAT 1314
Cdd:PRK10247 95 DTVYDNLIfPW------QIRnQQPDPAIFLDDLERfaLPDTI---LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170
....*....|....*
gi 1207190976 1315 AAIDTETDRLIQDTI 1329
Cdd:PRK10247 166 SALDESNKHNVNEII 180
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1150-1364 |
4.94e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 78.67 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLP--LVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAhigleDLRSKL 1227
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPVLFigtvrsnldPW-----------------DQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVG 1290
Cdd:cd03293 76 GYVFQQDALL---------PWltvldnvalglelqgvpKAEARERAEELLELVGLSGFENAYPHQL-----------SGG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1291 ERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFS--GCTTLVIAHRLN-TVLGCNRIMVLDQ--GQILE 1364
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1150-1376 |
7.27e-16 |
|
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: 78.97 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLplVLKNLCFSILPEETIGIVGRTGSGKSSL-GVALFRLAELSRGSIII-----DGVNI----AHIG 1219
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLfgerrGGEDVwelrKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1220 L------EDLRSKLSVIpqEPVL--FIGTVrsnlDPWDQYTDAQI---WEALEKTHIKDMVSQLPNSLhsevtdngenfS 1288
Cdd:COG1119 82 LvspalqLRFPRDETVL--DVVLsgFFDSI----GLYREPTDEQReraRELLELLGLAHLADRPFGTL-----------S 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1289 VGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRS-SFSGCTTLV-IAHRLNTVLGC-NRIMVLDQGQILEF 1365
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
250
....*....|.
gi 1207190976 1366 DTPSNLLTDEN 1376
Cdd:COG1119 225 GPKEEVLTSEN 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
644-724 |
9.03e-16 |
|
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: 77.68 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDA--RVGSRL----FHSAIrpaakGKTVIFVTH-QLQYLPECDDVVLMK 716
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAklRVQMRAelkrLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMN 205
|
....*...
gi 1207190976 717 DGQIAEHG 724
Cdd:cd03301 206 DGQIQQIG 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1159-1376 |
9.74e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.66 E-value: 9.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1159 YRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLgvalfrLAELS------RGSIIIDGVNIAHIGLEDLRSKLSVIPQ 1232
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL------LRALSgelspdSGEVRLNGRPLADWSPAELARRRAVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1233 EPVL-FIGTVRS----NLDPWDQYTDAQ---IWEALEKTHikdmVSQLPNSLHSEVtdngenfSVGERQLLCVARAL--L 1302
Cdd:PRK13548 84 HSSLsFPFTVEEvvamGRAPHGLSRAEDdalVAAALAQVD----LAHLAGRDYPQL-------SGGEQQRVQLARVLaqL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1303 RHS----KILLLDEATAAIDT----ETDRLIQDTIRSsfSGCTTLVIAHRLN-TVLGCNRIMVLDQGQILEFDTPSNLLT 1373
Cdd:PRK13548 153 WEPdgppRWLLLDEPTSALDLahqhHVLRLARQLAHE--RGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
...
gi 1207190976 1374 DEN 1376
Cdd:PRK13548 231 PET 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1150-1377 |
1.04e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.02 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSV 1229
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPV-LFIGTV---------RSNLDPWDQYTDaQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVAR 1299
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvafglENHAVPYDEMHR-RVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1300 ALLRHSKILLLDEATAAIDTETDRLIQDTIR--SSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTDENS 1377
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
597-731 |
1.09e-15 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 79.85 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 597 SLRENILFGKKY----NEEKYNAVLEACclfpdiielpygDMTEIGERGA----NLSGGQRQRVSLARALYSERPILLLD 668
Cdd:TIGR01187 58 TVEENVAFGLKMrkvpRAEIKPRVLEAL------------RLVQLEEFADrkphQLSGGQQQRVALARALVFKPKILLLD 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 669 DPLSAVDARVGSRLFHSAIRPAAK-GKTVIFVTH-QLQYLPECDDVVLMKDGQIAEHGTHTQLME 731
Cdd:TIGR01187 126 EPLSALDKKLRDQMQLELKTIQEQlGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1150-1365 |
1.36e-15 |
|
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: 77.23 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLVLKNLCFsilPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAhIGLEDLRSKLSV 1229
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL---GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFIG-TVRSNLD--PW-----DQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARAL 1301
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDyiAWlkgipSKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 1302 LRHSKILLLDEATAAIDTEtDRLIQDTIRSSFSGCTTLVIA-HRLNTVLG-CNRIMVLDQGQILEF 1365
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPE-ERIRFRNLLSELGEDRIVILStHIVEDVESlCNQVAVLNKGKLVFE 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
642-732 |
1.42e-15 |
|
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: 77.76 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRL------FHSAIrpaakGKTVIFVTH-QLQYLPECDDVVL 714
Cdd:cd03296 135 AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELrrwlrrLHDEL-----HVTTVFVTHdQEEALEVADRVVV 209
|
90
....*....|....*...
gi 1207190976 715 MKDGQIAEHGTHTQLMEK 732
Cdd:cd03296 210 MNKGRIEQVGTPDEVYDH 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1154-1381 |
1.82e-15 |
|
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: 77.38 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1154 DVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAhiGLEDLRSKLSVIPQE 1233
Cdd:cd03299 2 KVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1234 PVLFigtvrSNLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLH-SEVTD-NGENFSVGERQLLCVARALLRHSKILLLD 1311
Cdd:cd03299 80 YALF-----PHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGiDHLLNrKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1312 EATAAIDTET-DRLIQD--TIRSSFsGCTTLVIAHRLNT--VLGcNRIMVLDQGQILEFDTPSNLLTDENSRFHA 1381
Cdd:cd03299 155 EPFSALDVRTkEKLREElkKIRKEF-GVTVLHVTHDFEEawALA-DKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
584-730 |
2.03e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.00 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 584 FAYVAQQAWILNDSLRENILFGKKyneekyNAVLE---ACCLFPDIIE----LPYGDMTEIGERGANLSGGQRQRVSLAR 656
Cdd:PTZ00265 1298 FSIVSQEPMLFNMSIYENIKFGKE------DATREdvkRACKFAAIDEfiesLPNKYDTNVGPYGKSLSGGQKQRIAIAR 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 657 ALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKG-KTVIFVTHQLQYLPECDDVVLMKDGQ-----IAEHGTHTQLM 730
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELL 1451
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
560-724 |
2.06e-15 |
|
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: 76.05 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLG--GSVSVNGG----------FAYVAQQ-AWILNDSLRENILFGkkyneekynavleACClfpdi 626
Cdd:cd03213 48 KSTLLNALAGRRTGLGvsGEVLINGRpldkrsfrkiIGYVPQDdILHPTLTVRETLMFA-------------AKL----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 627 ielpygdmteigeRGanLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYL 706
Cdd:cd03213 110 -------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSE 174
|
170 180
....*....|....*....|
gi 1207190976 707 --PECDDVVLMKDGQIAEHG 724
Cdd:cd03213 175 ifELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
560-725 |
2.39e-15 |
|
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: 76.30 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGKKYNEEKYNAVLEacclfpdi 626
Cdd:cd03369 47 KSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR-------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 627 ielpygdmteIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSrLFHSAIRPAAKGKTVIFVTHQLQYL 706
Cdd:cd03369 119 ----------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA-LIQKTIREEFTNSTILTIAHRLRTI 187
|
170
....*....|....*....
gi 1207190976 707 PECDDVVLMKDGQIAEHGT 725
Cdd:cd03369 188 IDYDKILVMDAGEVKEYDH 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1166-1375 |
3.41e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.86 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGL-EDLRSKLSVIPQEPVLFigtvrSN 1244
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIF-----RR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1245 LDPWDQYTDA-QIWEALEKTHIKDMVSQLPNSLH-SEVTDN-GENFSVGERQLLCVARALLRHSKILLLDEATAAID--- 1318
Cdd:PRK10895 93 LSVYDNLMAVlQIRDDLSAEQREDRANELMEEFHiEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpis 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1319 -TETDRLIQDtIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDE 1375
Cdd:PRK10895 173 vIDIKRIIEH-LRD--SGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1166-1362 |
3.81e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.05 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSL-----GVALfrlaeLSRGSIIIDGVNIAHIGlEDLRSKL-SVIPQEPVLfiG 1239
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLlnaiaGSLP-----PDSGSILIDGKDVTKLP-EYKRAKYiGRVFQDPMM--G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1240 T-----VRSNLdpwdqytdaqiweAL-----------------EKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCV 1297
Cdd:COG1101 93 TapsmtIEENL-------------ALayrrgkrrglrrgltkkRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1298 ARALLRHSKILLLDEATAAID-------TE-TDRLIQDtirssfSGCTTLVIAHRLNTVLGC-NRIMVLDQGQI 1362
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1150-1375 |
5.32e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.15 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLA---ELSRGSIIIDGVNIAHIGLEDLRSK 1226
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1227 LSVIPQEP-VLFIGTVRSNlDPWDQYTDAQIWEALEKTHIKDMVSQ--LPNSLHSEvtdnGENFSVGERQLLCVARALLR 1303
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGD-DVAFGLENRAVPRPEMIKIVRDVLADvgMLDYIDSE----PANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1304 HSKILLLDEATAAIDTETDRLIQDTIRS--SFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLTDE 1375
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1166-1375 |
6.14e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 75.79 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDL-RSKLSVIPQEPVLFIG-TVRS 1243
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1244 NLD--PWDQYTDAQIWEALEKTH-----IKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDEATA- 1315
Cdd:COG0410 98 NLLlgAYARRDRAEVRADLERVYelfprLKERRRQRAGTL-----------SGGEQQMLAIGRALMSRPKLLLLDEPSLg 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1316 ---AIDTETDRLIQDtIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDE 1375
Cdd:COG0410 167 lapLIVEEIFEIIRR-LNR--EGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADP 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
560-702 |
6.49e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.91 E-value: 6.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG----------FAYVAQQ-AwiLNDSL--RENILFGKKYNEEKYNAVLEACCLF--P 624
Cdd:PRK13539 41 KTTLLRLIAGLLPPAAGTIKLDGGdiddpdvaeaCHYLGHRnA--MKPALtvAENLEFWAAFLGGEELDIAAALEAVglA 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 625 DIIELPYGdmteigergaNLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRP-AAKGKTVIFVTHQ 702
Cdd:PRK13539 119 PLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAELIRAhLAQGGIVIAATHI 186
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
644-739 |
8.01e-15 |
|
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: 79.18 E-value: 8.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRPAAK--GKTVIFVTHQLQYLPE-CDDVVLMKDGQI 720
Cdd:COG1123 143 LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEIL-DLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRI 221
|
90
....*....|....*....
gi 1207190976 721 AEHGTHTQLMEKGRDYAAL 739
Cdd:COG1123 222 VEDGPPEEILAAPQALAAV 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1166-1378 |
9.60e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVL-FIGTVR-- 1242
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRqv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1243 ---------SNLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDEA 1313
Cdd:PRK09536 98 vemgrtphrSRFDTWTETDRAAVERAMERTGVAQFADRPVTSL-----------SGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 1314 TAAIDT-------ETDRLIQDTIRSSFSGCTTLVIAHRLntvlgCNRIMVLDQGQILEFDTPSNLLTDENSR 1378
Cdd:PRK09536 167 TASLDInhqvrtlELVRRLVDDGKTAVAAIHDLDLAARY-----CDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1166-1357 |
9.88e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.52 E-value: 9.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDG--VNIAHIgLEDLRSKLSVIPQEPVL------- 1236
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP-RDAQAAGIAIIHQELNLvpnlsva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1237 ---FIGTVRSN---LDPWDQYTDAQiwEALEKTHI----KDMVSQLpnslhsevtdngenfSVGERQLLCVARALLRHSK 1306
Cdd:COG1129 98 eniFLGREPRRgglIDWRAMRRRAR--ELLARLGLdidpDTPVGDL---------------SVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1307 ILLLDEATAAI-DTETDRLIQ--DTIRSsfSGCTTLVIAHRLNTVLG-CNRIMVL 1357
Cdd:COG1129 161 VLILDEPTASLtEREVERLFRiiRRLKA--QGVAIIYISHRLDEVFEiADRVTVL 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1166-1363 |
1.73e-14 |
|
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: 73.35 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALF-RLAELS-RGSIIIDGVNIahiGLEDLRSKLSVIPQEPVLFigtvrs 1243
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGvSGEVLINGRPL---DKRSFRKIIGYVPQDDILH------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1244 nldpwDQYTdaqIWEALekthikdMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDEATAAIDTETDR 1323
Cdd:cd03213 95 -----PTLT---VRETL-------MFAAKLRGL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207190976 1324 LIQDTIRS-SFSGCTTLVIAHRLNTVL--GCNRIMVLDQGQIL 1363
Cdd:cd03213 149 QVMSLLRRlADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1150-1364 |
1.91e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 76.38 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLV--LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRS-- 1225
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1226 -KLSVIPQEPVLFIG-TVRSN------LDPWDQ-YTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLC 1296
Cdd:PRK11153 82 rQIGMIFQHFNLLSSrTVFDNvalpleLAGTPKaEIKARVTELLELVGLSDKADRYPAQL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1297 VARALLRHSKILLLDEATAAIDTETDRLIQDTIRS--SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILE 1364
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
560-732 |
2.12e-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: 74.29 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-----------GFAYVAQQ-AWILNDSLRENILFG---KKYN-EEKYNAVLEacclf 623
Cdd:cd03299 38 KSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNyALFPHMTVYKNIAYGlkkRKVDkKEIERKVLE----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 624 pdIIElpygdMTEIGE----RGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRPAAK--GKTVI 697
Cdd:cd03299 113 --IAE-----MLGIDHllnrKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR-EELKKIRKefGVTVL 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207190976 698 FVTHQL-QYLPECDDVVLMKDGQIAEHGTHTQLMEK 732
Cdd:cd03299 185 HVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1150-1392 |
2.30e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.25 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPLV---LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNI----AHIGLED 1222
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1223 LRSKLSVIPQ--EPVLFIGTVRS-------NLDPWDQYTDAQIWEALEKTHIK-DMVSQLPNSLhsevtdngenfSVGER 1292
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKdvefgpkNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFEL-----------SGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1293 QLLCVARALLRHSKILLLDEATAAIDTETDR-LIQDTIRSSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSN 1370
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKE 231
|
250 260
....*....|....*....|...
gi 1207190976 1371 LLTDEN-SRFHAMMEAAEETFSR 1392
Cdd:PRK13641 232 IFSDKEwLKKHYLDEPATSRFAS 254
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1159-1369 |
2.42e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.08 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1159 YRDGLPL---VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIA--HIGLEDLRSKLSVIPQE 1233
Cdd:PRK13637 12 YMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1234 P--VLFIGTVR-------SNLDPWDQYTDAQIWEALEKTHIK--DMVSQLPNSLhsevtdngenfSVGERQLLCVARALL 1302
Cdd:PRK13637 92 PeyQLFEETIEkdiafgpINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFEL-----------SGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1303 RHSKILLLDEATAAIDTETDRLIQDTIRSSFS--GCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPS 1369
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1162-1360 |
2.87e-14 |
|
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: 73.52 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1162 GLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSK----LSVIPQEPVLF 1237
Cdd:cd03290 13 GLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1238 IGTVRSNLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAI 1317
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207190976 1318 DTE-TDRLIQDTIRSSFSG--CTTLVIAHRLNTVLGCNRIMVLDQG 1360
Cdd:cd03290 172 DIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1163-1362 |
3.10e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 72.46 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1163 LPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNI----------AHIGL--EDlRSKLSVI 1230
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrrsprdairAGIAYvpED-RKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1231 PQEPvlfigtVRSNLdpwdqytdaqiwealekthikdmvsQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLL 1310
Cdd:cd03215 91 LDLS------VAENI-------------------------ALSSLL-----------SGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1311 DEATAAIDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQI 1362
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
560-724 |
3.12e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 73.30 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG---GFAYVAQQAwiLNDSLRENILF---------------GKKYNEEKYNAVleacc 621
Cdd:cd03298 37 KSTLLNLIAGFETPQSGRVLINGvdvTAAPPADRP--VSMLFQENNLFahltveqnvglglspGLKLTAEDRQAI----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 622 lfpDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDA--RVGSRLFHSAIRpAAKGKTVIFV 699
Cdd:cd03298 110 ---EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPalRAEMLDLVLDLH-AETKMTVLMV 185
|
170 180
....*....|....*....|....*.
gi 1207190976 700 THQLQYLPECDD-VVLMKDGQIAEHG 724
Cdd:cd03298 186 THQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1166-1375 |
3.78e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.89 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIG-TVRSN 1244
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1245 L----DPW-------DQYTDAQIWEALEKTHIKDMVSQLpnslhseVTDngenFSVGERQLLCVARALLRHSKILLLDEA 1313
Cdd:PRK11231 97 VaygrSPWlslwgrlSAEDNARVNQAMEQTRINHLADRR-------LTD----LSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 1314 TAAID----TETDRLIQdtiRSSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDE 1375
Cdd:PRK11231 166 TTYLDinhqVELMRLMR---ELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
600-732 |
4.01e-14 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 73.43 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 600 ENILFG---KKYNEEKYNA-VLEAcclfpdiieLPYGDMTEIGERG-ANLSGGQRQRVSLARALYSERPILLLDDPLSAV 674
Cdd:cd03300 91 ENIAFGlrlKKLPKAEIKErVAEA---------LDLVQLEGYANRKpSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 675 DARVGSRL------FHSAIrpaakGKTVIFVTH-QLQYLPECDDVVLMKDGQIAEHGTHTQLMEK 732
Cdd:cd03300 162 DLKLRKDMqlelkrLQKEL-----GITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
560-733 |
4.08e-14 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 75.53 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-----------------GFAYVAQQAWILND-SLRENILFGKKYNEEKYNAVLEAcc 621
Cdd:TIGR02142 36 KTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLFPHlSVRGNLRYGMKRARPSERRISFE-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 622 lfpDIIELpYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAK-GKTVIFVT 700
Cdd:TIGR02142 114 ---RVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVS 189
|
170 180 190
....*....|....*....|....*....|....
gi 1207190976 701 HQLQYLPE-CDDVVLMKDGQIAEHGTHTQLMEKG 733
Cdd:TIGR02142 190 HSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
534-754 |
5.58e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.51 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 534 HKTLHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMT----------LLGGSVSVNGGFA-----------YVAQQAW 592
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshieLLGRTVQREGRLArdirksrantgYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 593 ILND-SLRENILFGKKYNEEKYNAVLEacCLFPDIIELPYGDMTEIG------ERGANLSGGQRQRVSLARALYSERPIL 665
Cdd:PRK09984 97 LVNRlSVLENVLIGALGSTPFWRTCFS--WFTREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 666 LLDDPLSAVDARvGSRLFHSAIRPAAK--GKTVIFVTHQLQY-LPECDDVVLMKDGQIAEHGTHTQLMEKGRDYaaLFNS 742
Cdd:PRK09984 175 LADEPIASLDPE-SARIVMDTLRDINQndGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFDH--LYRS 251
|
250
....*....|..
gi 1207190976 743 VqqeNLVRKNLK 754
Cdd:PRK09984 252 I---NRVEENAK 260
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
639-720 |
5.68e-14 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 73.17 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 639 ERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVD---ARVGSRLFHSAIRpaAKGKTVIFVTHQLQYLPE-CDDVVL 714
Cdd:COG3638 142 QRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDpktARQVMDLLRRIAR--EDGITVVVNLHQVDLARRyADRIIG 219
|
....*.
gi 1207190976 715 MKDGQI 720
Cdd:COG3638 220 LRDGRV 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
642-725 |
7.10e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.74 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRL------FHSAIRpaakgKTVIFVTH-QLQYLPECDDVVL 714
Cdd:PRK10851 135 AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELrrwlrqLHEELK-----FTSVFVTHdQEEAMEVADRVVV 209
|
90
....*....|.
gi 1207190976 715 MKDGQIAEHGT 725
Cdd:PRK10851 210 MSQGNIEQAGT 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
642-725 |
7.74e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 74.34 E-value: 7.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVD-----------ARVGSRLfhsairpaakGKTVIFVTHQLQYLPE-C 709
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALDpettrsildllKDINREL----------GLTIVLITHEMDVVRRiC 208
|
90
....*....|....*.
gi 1207190976 710 DDVVLMKDGQIAEHGT 725
Cdd:COG1135 209 DRVAVLENGRIVEQGP 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
560-720 |
9.25e-14 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 71.52 E-value: 9.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGGFA----------YVAQ--QAWILNDSLRENILFGKKYNEEKYN---AVLEACCLFP 624
Cdd:cd03226 39 KTTLAKILAGLIKESSGSILLNGKPIkakerrksigYVMQdvDYQLFTDSVREELLLGLKELDAGNEqaeTVLKDLDLYA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 625 DIIELPygdmteigergANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQ 704
Cdd:cd03226 119 LKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYE 187
|
170
....*....|....*..
gi 1207190976 705 YLPE-CDDVVLMKDGQI 720
Cdd:cd03226 188 FLAKvCDRVLLLANGAI 204
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1166-1369 |
1.03e-13 |
|
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: 72.08 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSL-GValfrLAEL---SRGSIIIDGVNIAHIGlEDLRSKL---SV--------- 1229
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLlGL----LAGLdrpTSGTVRLAGQDLFALD-EDARARLrarHVgfvfqsfql 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQ----EPVLFIGTVRSNLDPWDQytdAQiwEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHS 1305
Cdd:COG4181 102 LPTltalENVMLPLELAGRRDARAR---AR--ALLERVGLGHRLDHYPAQL-----------SGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1306 KILLLDEATAAIDTETDRLIQDTIRS--SFSGcTTLVI-------AHRlntvlgCNRIMVLDQGQILEFDTPS 1369
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFElnRERG-TTLVLvthdpalAAR------CDRVLRLRAGRLVEDTAAT 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
644-724 |
1.04e-13 |
|
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: 71.54 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRP-AAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIA 721
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
...
gi 1207190976 722 EHG 724
Cdd:cd03269 208 LYG 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
597-725 |
1.05e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.60 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 597 SLRENILFG----KKYNEEKYNAVLEAcclfpdiieLPYGDMTEIGERG-ANLSGGQRQRVSLARALYSERPILLLDDPL 671
Cdd:PRK09452 102 TVFENVAFGlrmqKTPAAEITPRVMEA---------LRMVQLEEFAQRKpHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 672 SAVDARVgSRLFHSAIRPAAK--GKTVIFVTH-QLQYLPECDDVVLMKDGQIAEHGT 725
Cdd:PRK09452 173 SALDYKL-RKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1150-1375 |
1.53e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.30 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYrdGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNI---AHIGledlRSK 1226
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpsrARHA----RQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1227 LSVIPQ----EPVLfigTVRSNLDPWDQYTdaqiweALEKTHIKDMV------SQLPNSLHSEVTDngenFSVGERQLLC 1296
Cdd:PRK13537 82 VGVVPQfdnlDPDF---TVRENLLVFGRYF------GLSAAAARALVppllefAKLENKADAKVGE----LSGGMKRRLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1297 VARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSF-SGCTTLVIAH------RLntvlgCNRIMVLDQGQILEFDTPS 1369
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPH 223
|
....*.
gi 1207190976 1370 NLLTDE 1375
Cdd:PRK13537 224 ALIESE 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1150-1379 |
1.55e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 73.59 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYrdGLPLVLKNLCFSILPEETIGIVGRTGSGKSSL-----GvalfrLAELSRGSIIIDGVNIAHIGLEDlR 1224
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLlrmiaG-----FETPDSGRILLDGRDVTGLPPEK-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1225 sKLSVIPQEPVLFi-gTVRSN---------LDPwdQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQL 1294
Cdd:COG3842 78 -NVGMVFQDYALFphlTVAENvafglrmrgVPK--AEIRARVAELLELVGLEGLADRYPHQL-----------SGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1295 LCVARALLRHSKILLLDEATAAID--------TETDRLIQDTirssfsGCTTLVIAH------RLntvlgCNRIMVLDQG 1360
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDaklreemrEELRRLQREL------GITFIYVTHdqeealAL-----ADRIAVMNDG 212
|
250
....*....|....*....
gi 1207190976 1361 QILEFDTPSNLLTDENSRF 1379
Cdd:COG3842 213 RIEQVGTPEEIYERPATRF 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
560-721 |
2.01e-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: 71.45 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG----------------FAYVAQQ-AWILNDSLRENILFGKK-------------YN 609
Cdd:cd03256 40 KSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQfNLIERLSVLENVLSGRLgrrstwrslfglfPK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 610 EEKYNAV--LEACclfpDIIELPYgdmteigERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVD---ARVGSRLFH 684
Cdd:cd03256 120 EEKQRALaaLERV----GLLDKAY-------QRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDpasSRQVMDLLK 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207190976 685 SAIRpaAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIA 721
Cdd:cd03256 189 RINR--EEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
642-729 |
3.02e-13 |
|
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: 70.69 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDA-----------RVGSRLfhsairpaakGKTVIFVTHQLQYLPE-C 709
Cdd:cd03258 139 AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPettqsilallrDINREL----------GLTIVLITHEMEVVKRiC 208
|
90 100
....*....|....*....|
gi 1207190976 710 DDVVLMKDGQIAEHGTHTQL 729
Cdd:cd03258 209 DRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
633-724 |
3.08e-13 |
|
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: 70.47 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 633 DMTEIGE-RGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRP-AAKGKTVIFVTHQLQYLPE-C 709
Cdd:cd03266 125 GMEELLDrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV-MATRALREFIRQlRALGKCILFSTHIMQEVERlC 203
|
90
....*....|....*
gi 1207190976 710 DDVVLMKDGQIAEHG 724
Cdd:cd03266 204 DRVVVLHRGRVVYEG 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
560-720 |
3.11e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 69.38 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG--------------GFAYVA----QQAWILNDSLRENILFGkkyneekynavleacc 621
Cdd:cd03215 39 QTELAEALFGLRPPASGEITLDGkpvtrrsprdairaGIAYVPedrkREGLVLDLSVAENIALS---------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 622 lfpdiielpygdmteigergANLSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGSRLF-HSAIRP-AAKGKTVIFV 699
Cdd:cd03215 103 --------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD--VGAKAEiYRLIRElADAGKAVLLI 160
|
170 180
....*....|....*....|....*
gi 1207190976 700 ThqlQYLPE----CDDVVLMKDGQI 720
Cdd:cd03215 161 S---SELDEllglCDRILVMYEGRI 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1167-1364 |
3.23e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.12 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIG---LEDLRSKLSVIPQEPVlfigtvrS 1243
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1244 NLDPwDQYTDAQIWEALeKTH--------------IKDMVSQLPNslHSEVTDNgeNFSVGERQLLCVARALLRHSKILL 1309
Cdd:PRK10261 413 SLDP-RQTVGDSIMEPL-RVHgllpgkaaaarvawLLERVGLLPE--HAWRYPH--EFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1310 LDEATAAIDT----ETDRLIQDTIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILE 1364
Cdd:PRK10261 487 ADEAVSALDVsirgQIINLLLDLQRD--FGIAYLFISHDMAVVERiSHRVAVMYLGQIVE 544
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
560-724 |
3.60e-13 |
|
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: 70.88 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQM--------TLLG---GSVSV-----NGGFAYVAQQAWIL-NDSLRENIL---FG-----KKYNEEKYN 614
Cdd:COG1119 42 KSTLLSLITGDLpptygndvRLFGerrGGEDVwelrkRIGLVSPALQLRFPrDETVLDVVLsgfFDsiglyREPTDEQRE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 615 AVLEACCLFpdiielpygDMTEIGERG-ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGSR-LFHSAIRPAAK 692
Cdd:COG1119 122 RARELLELL---------GLAHLADRPfGTLSQGEQRRVLIARALVKDPELLILDEPTAGLD--LGAReLLLALLDKLAA 190
|
170 180 190
....*....|....*....|....*....|....*
gi 1207190976 693 --GKTVIFVTHQLQYLPEC-DDVVLMKDGQIAEHG 724
Cdd:COG1119 191 egAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
560-725 |
3.83e-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: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG----------------GFAYVAQQAwILNDSL--RENILFGKKYN-----EEKYNAV 616
Cdd:COG1127 44 KSVLLKLIIGLLRPDSGEILVDGqditglsekelyelrrRIGMLFQGG-ALFDSLtvFENVAFPLREHtdlseAEIRELV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 617 LEacCL----FPDIIEL-PygdmteigergANLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRP-- 689
Cdd:COG1127 123 LE--KLelvgLPGAADKmP-----------SELSGGMRKRVALARALALDPEILLYDEPTAGLDP-ITSAVIDELIRElr 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207190976 690 AAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIAEHGT 725
Cdd:COG1127 189 DELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGT 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1152-1366 |
4.12e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1152 FQDVEMRYrdGLPLVLKNLCFSILPEETIGIVGRTGSGKSSlgvaLFRL----AELSRGSIIIDGvniahigleDLRskL 1227
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKIlageLEPDSGEVSIPK---------GLR--I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPVLF-----IGTVRSNLDPWDQyTDAQIWEALEKTHIKDMVSQLPNSLHSEVTDNGE----------------- 1285
Cdd:COG0488 64 GYLPQEPPLDddltvLDTVLDGDAELRA-LEAELEELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1286 ---------NFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRsSFSGcTTLVIAH-R--LNTVlgCNR 1353
Cdd:COG0488 143 eedldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLK-NYPG-TVLVVSHdRyfLDRV--ATR 218
|
250
....*....|...
gi 1207190976 1354 IMVLDQGQILEFD 1366
Cdd:COG0488 219 ILELDRGKLTLYP 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1160-1374 |
4.27e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.76 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1160 RDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRS----KLSVIPQEPV 1235
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1236 LFIG-TVRSNLDPWDQYTDAQIWEALEKThiKDMVSQLpnSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEAT 1314
Cdd:PRK10070 117 LMPHmTVLDNTAFGMELAGINAEERREKA--LDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1315 AAIDTETDRLIQDTI--RSSFSGCTTLVIAHRLNTVLGC-NRIMVLDQGQILEFDTPSNLLTD 1374
Cdd:PRK10070 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
644-740 |
4.33e-13 |
|
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: 71.14 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAK-GKTVIFVTHQL-QYLPECDDVVLMKDGQIA 721
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLdEALRLGDRIAIMKDGRLV 240
|
90 100
....*....|....*....|
gi 1207190976 722 EHGTHTQ-LMEKGRDYAALF 740
Cdd:cd03294 241 QVGTPEEiLTNPANDYVREF 260
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1167-1345 |
4.35e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.96 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELS-----RGSIIIDGVNI--AHIGLEDLRSKLSVIPQEPVLFIG 1239
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1240 TVRSNL----------DpwDQYTDAQIWEALEKTHIKDMVSqlpNSLHsevtDNGENFSVGERQLLCVARALLRHSKILL 1309
Cdd:PRK14239 101 SIYENVvyglrlkgikD--KQVLDEAVEKSLKGASIWDEVK---DRLH----DSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207190976 1310 LDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRL 1345
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1178-1362 |
5.28e-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: 69.44 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1178 ETIGIVGRTGSGKSSLG--VALFRLAElsRGSIIIDGVNIAHigLEDLRSKLSVIPQEPVLF--------IGTVRS---N 1244
Cdd:cd03298 25 EITAIVGPSGSGKSTLLnlIAGFETPQ--SGRVLINGVDVTA--APPADRPVSMLFQENNLFahltveqnVGLGLSpglK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1245 LDPWDQytdAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDEATAAID----TE 1320
Cdd:cd03298 101 LTAEDR---QAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207190976 1321 TDRLIQDTIRSsfSGCTTLVIAHRLNTVLGC-NRIMVLDQGQI 1362
Cdd:cd03298 167 MLDLVLDLHAE--TKMTVLMVTHQPEDAKRLaQRVVFLDNGRI 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1166-1378 |
5.31e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 69.88 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLeDLRSKLSVI--PQEPVLFIG-TVR 1242
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIGylPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1243 SNLDPWDQYTDAQIWEALEKT-------HIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDEATA 1315
Cdd:cd03218 94 ENILAVLEIRGLSKKEREEKLeelleefHITHLRKSKASSL-----------SGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1316 AIDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDENSR 1378
Cdd:cd03218 163 GVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1150-1373 |
6.66e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.49 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPL-------VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHI---G 1219
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1220 LEDLRSKLSVIPQEPvlfIG------TVR----------SNLDPWDQytDAQIWEALEKTHIKDMV-SQLPNSLhsevtd 1282
Cdd:PRK10419 84 RKAFRRDIQMVFQDS---ISavnprkTVReiireplrhlLSLDKAER--LARASEMLRAVDLDDSVlDKRPPQL------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1283 ngenfSVGERQLLCVARALLRHSKILLLDEATAAID----TETDRLIQDTIRSSFSGCttLVIAHRLNTVLG-CNRIMVL 1357
Cdd:PRK10419 153 -----SGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTAC--LFITHDLRLVERfCQRVMVM 225
|
250
....*....|....*.
gi 1207190976 1358 DQGQILEFDTPSNLLT 1373
Cdd:PRK10419 226 DNGQIVETQPVGDKLT 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
644-724 |
7.24e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.18 E-value: 7.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIAE 722
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRA 219
|
..
gi 1207190976 723 HG 724
Cdd:PRK09536 220 AG 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
642-720 |
8.60e-13 |
|
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: 69.10 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDAR-VGSRLfhSAIRPAAK-GKTVIFVTHQLQYLPE-CDDVVLMKDG 718
Cdd:cd03262 134 AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPElVGEVL--DVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
..
gi 1207190976 719 QI 720
Cdd:cd03262 212 RI 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
560-731 |
9.89e-13 |
|
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: 69.00 E-value: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG--------------GFAYVAQQAWILND-SLRENILFG-----KKYNEEKYNAVLEa 619
Cdd:cd03224 39 KTTLLKTIMGLLPPRSGSIRFDGrditglppheraraGIGYVPEGRRIFPElTVEENLLLGayarrRAKRKARLERVYE- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 620 ccLFPDIIELpygdmteIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFV 699
Cdd:cd03224 118 --LFPRLKER-------RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLV 188
|
170 180 190
....*....|....*....|....*....|...
gi 1207190976 700 THQLQY-LPECDDVVLMKDGQIAEHGTHTQLME 731
Cdd:cd03224 189 EQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
560-730 |
1.08e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 69.73 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG------GFAYVAQQAWIL---ND-----SLRENILFGK------KYNEEKYNAVLEA 619
Cdd:COG4604 40 KSTLLSMISRLLPPDSGEVLVDGldvattPSRELAKRLAILrqeNHinsrlTVRELVAFGRfpyskgRLTAEDREIIDEA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 620 cclfpdiieLPYGDMTEIGERGAN-LSGGQRQRVSLARALYSERPILLLDDPLSAVDarvgsrLFHS-----AIRPAA-- 691
Cdd:COG4604 120 ---------IAYLDLEDLADRYLDeLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD------MKHSvqmmkLLRRLAde 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207190976 692 KGKTVIFVTHQL----QYlpeCDDVVLMKDGQIAEHGTHTQLM 730
Cdd:COG4604 185 LGKTVVIVLHDInfasCY---ADHIVAMKDGRVVAQGTPEEII 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1167-1371 |
1.14e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 70.15 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEP-VLFIG-TVRSN 1244
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdNQFVGaTVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1245 LD--------PWDQYTDaQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDEATAA 1316
Cdd:PRK13650 103 VAfglenkgiPHEEMKE-RVNEALELVGMQDFKEREPARL-----------SGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 1317 IDTETDR-LIQ--DTIRSSFsGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNL 1371
Cdd:PRK13650 171 LDPEGRLeLIKtiKGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
640-730 |
1.16e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.66 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 640 RGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQL-QYLPECDDVVLMKDG 718
Cdd:PRK11231 135 RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANG 214
|
90
....*....|..
gi 1207190976 719 QIAEHGTHTQLM 730
Cdd:PRK11231 215 HVMAQGTPEEVM 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1166-1375 |
1.49e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.31 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGV------NIAHIGLEDLRSKLSVIPQEPVLFig 1239
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPF-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1240 tvrSNLDPWDQYTDAQIWEAL-EKTHIKDMVSQ------LPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDE 1312
Cdd:PRK14246 103 ---PHLSIYDNIAYPLKSHGIkEKREIKKIVEEclrkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1313 ATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILE-------FDTPSNLLTDE 1375
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEwgssneiFTSPKNELTEK 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1154-1367 |
1.56e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.52 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1154 DVEMRYRDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALF-RLAELSR--GSIIIDG---VNIAHIGLEDLRS-K 1226
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMgLLAANGRigGSATFNGreiLNLPEKELNKLRAeQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1227 LSVIPQEPVlfigtvrSNLDPW----DQYTD----------AQIWEalEKTHIKDMVsQLPNSlHSEVTDNGENFSVGER 1292
Cdd:PRK09473 99 ISMIFQDPM-------TSLNPYmrvgEQLMEvlmlhkgmskAEAFE--ESVRMLDAV-KMPEA-RKRMKMYPHEFSGGMR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1293 QLLCVARALLRHSKILLLDEATAAIDTETDRLIQ---DTIRSSFsGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDT 1367
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMtllNELKREF-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
642-725 |
2.05e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 68.48 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDAR-VGSRLfhSAIRPAAK-GKTVIFVTHQLQYLPE-CDDVVLMKDG 718
Cdd:COG1126 135 AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPElVGEVL--DVMRDLAKeGMTMVVVTHEMGFAREvADRVVFMDGG 212
|
....*..
gi 1207190976 719 QIAEHGT 725
Cdd:COG1126 213 RIVEEGP 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1148-1379 |
2.55e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 70.10 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1148 GQITFQDVEMRYrDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSL-----GvalfrLAELSRGSIIIDGVNIAHIGLED 1222
Cdd:COG3839 2 ASLELENVSKSY-GGVE-ALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiaG-----LEDPTSGEILIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1223 lRsKLSVIPQEPVLFIG-TVRSNL---------DPwdQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGER 1292
Cdd:COG3839 75 -R-NIAMVFQSYALYPHmTVYENIafplklrkvPK--AEIDRRVREAAELLGLEDLLDRKPKQL-----------SGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1293 QLLCVARALLRHSKILLLDEATAAID--------TETDRLIQDTirssfsGCTTLVIAH------RLntvlgCNRIMVLD 1358
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDaklrvemrAEIKRLHRRL------GTTTIYVTHdqveamTL-----ADRIAVMN 208
|
250 260
....*....|....*....|.
gi 1207190976 1359 QGQILEFDTPSNLLTDENSRF 1379
Cdd:COG3839 209 DGRIQQVGTPEELYDRPANLF 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
636-725 |
2.92e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.98 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 636 EIGERGA----NLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRP-AAKGKTVIFVTHQLQYLPE-C 709
Cdd:COG4152 118 GLGDRANkkveELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP-VNVELLKDVIRElAAKGTTVIFSSHQMELVEElC 196
|
90
....*....|....*.
gi 1207190976 710 DDVVLMKDGQIAEHGT 725
Cdd:COG4152 197 DRIVIINKGRKVLSGS 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
631-730 |
3.14e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.46 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 631 YGDMTEIGERG-----ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQY 705
Cdd:PRK10619 135 YLAKVGIDERAqgkypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGF 214
|
90 100
....*....|....*....|....*.
gi 1207190976 706 LPECDD-VVLMKDGQIAEHGTHTQLM 730
Cdd:PRK10619 215 ARHVSShVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1150-1381 |
3.15e-12 |
|
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: 67.65 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLplVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEdlRSKLSV 1229
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFigtvrSNLDPWD-------------QYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLC 1296
Cdd:cd03300 77 VFQNYALF-----PHLTVFEniafglrlkklpkAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1297 VARALLRHSKILLLDEATAAIDT--------ETDRLiQDTIrssfsGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDT 1367
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLklrkdmqlELKRL-QKEL-----GITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGT 214
|
250
....*....|....
gi 1207190976 1368 PSNLLTDENSRFHA 1381
Cdd:cd03300 215 PEEIYEEPANRFVA 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1167-1372 |
4.02e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.58 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEP-VLFIG-TVRSN 1244
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGaTVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1245 LD--------PWDQYTDaQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDEATAA 1316
Cdd:PRK13642 103 VAfgmenqgiPREEMIK-RVDEALLAVNMLDFKTREPARL-----------SGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1317 ID----TETDRLIQDtIRSSFSgCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLL 1372
Cdd:PRK13642 171 LDptgrQEIMRVIHE-IKEKYQ-LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
874-1119 |
4.49e-12 |
|
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: 68.35 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 874 YVLSMGAALFLKTIRGLVFVKCTVRAA-SVLHD---KLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMqaeML 949
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGqRVVFDlrrDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSS---GL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 950 LQNVTLVLFCLGVVGAVF----PWFLFSIIPLgAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGR 1025
Cdd:cd07346 118 LQLLSDVLTLIGALVILFylnwKLTLVALLLL-PLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1026 GADFIHRYQALLDTNQACQFLfscAMRWLAvrLDLISISLITTVALLIVL-------MHGHISPAYAGLALSYAVQLTGL 1098
Cdd:cd07346 197 EEREIERFREANRDLRDANLR---AARLSA--LFSPLIGLLTALGTALVLlyggylvLQGSLTIGELVAFLAYLGMLFGP 271
|
250 260
....*....|....*....|.
gi 1207190976 1099 FQFTVRLLSETEARFTSVERI 1119
Cdd:cd07346 272 IQRLANLYNQLQQALASLERI 292
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
534-729 |
4.88e-12 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 67.32 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 534 HKTLHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMTLLGGSVSVNGG----------------FAYVAQQ-AWILND 596
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklrgkklrklrrrIGMIFQHyNLIERL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 597 SLRENILFGK------------KYNEEKYNAVLEACCLFpDIIELPYgdmteigERGANLSGGQRQRVSLARALYSERPI 664
Cdd:TIGR02315 95 TVLENVLHGRlgykptwrsllgRFSEEDKERALSALERV-GLADKAY-------QRADQLSGGQQQRVAIARALAQQPDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 665 LLLDDPLSAVDARVGSRLFHSAIRPAAK-GKTVIFVTHQLQYLPE-CDDVVLMKDGQIAEHGTHTQL 729
Cdd:TIGR02315 167 ILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGAPSEL 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
560-715 |
5.75e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.10 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG--FAYVAQQAwILNDSL-------------RENILFGKKYNEEKynAVLEACCLFP 624
Cdd:NF040873 31 KSTLLKVLAGVLRPTSGTVRRAGGarVAYVPQRS-EVPDSLpltvrdlvamgrwARRGLWRRLTRDDR--AAVDDALERV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 625 DIIELPygdmteiGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLfHSAI-RPAAKGKTVIFVTHQL 703
Cdd:NF040873 108 GLADLA-------GRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI-IALLaEEHARGATVVVVTHDL 179
|
170
....*....|..
gi 1207190976 704 QYLPECDDVVLM 715
Cdd:NF040873 180 ELVRRADPCVLL 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1150-1375 |
6.87e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.70 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDglPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNI-AHIGLEdlRSKLS 1228
Cdd:PRK13536 42 IDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1229 VIPQEPVL---FigTVRSNLDPWDQY-------TDAQIWEALEkthikdmVSQLPNSLHSEVTDngenFSVGERQLLCVA 1298
Cdd:PRK13536 118 VVPQFDNLdleF--TVRENLLVFGRYfgmstreIEAVIPSLLE-------FARLESKADARVSD----LSGGMKRRLTLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1299 RALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFS-GCTTLVIAH------RLntvlgCNRIMVLDQGQILEFDTPSNL 1371
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHAL 259
|
....
gi 1207190976 1372 LtDE 1375
Cdd:PRK13536 260 I-DE 262
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1150-1374 |
7.30e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.81 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDG----LPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIG-LEDLR 1224
Cdd:PRK13633 5 IKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1225 SKLSVIPQEP------------VLF----IGT----VRSNLDpwdqytdaqiwEALEKTHIKDMVSQLPNSLhsevtdng 1284
Cdd:PRK13633 85 NKAGMVFQNPdnqivativeedVAFgpenLGIppeeIRERVD-----------ESLKKVGMYEYRRHAPHLL-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1285 enfSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIR--SSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQI 1362
Cdd:PRK13633 146 ---SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
250
....*....|..
gi 1207190976 1363 LEFDTPSNLLTD 1374
Cdd:PRK13633 223 VMEGTPKEIFKE 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1166-1379 |
7.68e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 68.63 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSL-----GvalfrLAELSRGSIIIDGvniahiglEDLRSKLSV-------IPQE 1233
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLlriiaG-----LETPDSGRIVLNG--------RDLFTNLPPrerrvgfVFQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1234 PVLFIG-TVRSN-------LDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHS 1305
Cdd:COG1118 84 YALFPHmTVAENiafglrvRPPSKAEIRARVEELLELVQLEGLADRYPSQL-----------SGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 1306 KILLLDEATAAIDTETDRLIQDTIRSSFS--GCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDENSRF 1379
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVYDRPATPF 229
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
140-408 |
8.61e-12 |
|
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: 67.28 E-value: 8.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 140 MLVAIFSLLITMVAGFVGP---ALLIRALLEFSQCSEVKLLYGLALVAGIFLMELTRSWSLAFMWainYRTAARLRGAAL 216
Cdd:pfam00664 1 LILAILLAILSGAISPAFPlvlGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLL---NHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 217 TFAFQKILRL--RSTKDVSSGELVNICASDGQRLYEAVSVGCLLAGGPLVGMLGLTYTTYFLGPT-ALVGSAIFIIFYPT 293
Cdd:pfam00664 78 RKLFKKILRQpmSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 294 MMLASRMTAYFRKKCVAVTDRRVRLMNEILGCMKFIKMYCWETPFANNIQKVRSEERRN----LEWAGCVQSLTLGVAPV 369
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAgikkAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 1207190976 370 VVVIASVCTFTLHMAlgYDLTAAQAFTVVAVFNSMTFAL 408
Cdd:pfam00664 238 SYALALWFGAYLVIS--GELSVGDLVAFLSLFAQLFGPL 274
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1150-1374 |
1.13e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 66.27 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYrdGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDG--VNIAHIGLEDLR--- 1224
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1225 ----SKLSVIPQ----EPVLFiGTVR----SNLDpwdqyTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGER 1292
Cdd:PRK09493 80 gmvfQQFYLFPHltalENVMF-GPLRvrgaSKEE-----AEKQARELLAKVGLAERAHHYPSEL-----------SGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1293 QLLCVARALLRHSKILLLDEATAAIDTETD----RLIQDTIRssfSGCTTLVIAHRLNTV--LGcNRIMVLDQGQILEFD 1366
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRhevlKVMQDLAE---EGMTMVIVTHEIGFAekVA-SRLIFIDKGRIAEDG 218
|
....*...
gi 1207190976 1367 TPSNLLTD 1374
Cdd:PRK09493 219 DPQVLIKN 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1150-1375 |
1.43e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.80 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDG--VNIAHIGLEDLRSKL 1227
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEP--VLFIGTVRSNLD--------PWDQyTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCV 1297
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSfgavnlklPEDE-VRKRVDNALKRTGIEHLKDKPTHCL-----------SFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1298 ARALLRHSKILLLDEATAAID----TETDRLIQDTIRSsfSGCTTLVIAHRLNTV-LGCNRIMVLDQGQILEFDTPSNLL 1372
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKE--LGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVF 230
|
...
gi 1207190976 1373 TDE 1375
Cdd:PRK13636 231 AEK 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1149-1375 |
1.52e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.09 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1149 QITFQDVEMRYrdGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELS-----RGSIIIDGVNIAHIGLEDL 1223
Cdd:PRK14247 3 KIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1224 RSKLSVIPQEP------VLF----IGTVRSNLDPWDQYTDAQIWEALEKthikdmvSQLPNSLHSEVTDNGENFSVGERQ 1293
Cdd:PRK14247 81 RRRVQMVFQIPnpipnlSIFenvaLGLKLNRLVKSKKELQERVRWALEK-------AQLWDEVKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1294 LLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAH------RLNtvlgcNRIMVLDQGQILE--- 1364
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEwgp 228
|
250
....*....|....*
gi 1207190976 1365 ----FDTPSNLLTDE 1375
Cdd:PRK14247 229 trevFTNPRHELTEK 243
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
560-724 |
1.66e-11 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 65.27 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG-----------FAYVAQQAWILND-SLRENILFG----KKYNEEKYNAVLEACClf 623
Cdd:TIGR01277 37 KSTLLNLIAGFIEPASGSIKVNDQshtglapyqrpVSMLFQENNLFAHlTVRQNIGLGlhpgLKLNAEQQEKVVDAAQ-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 624 pdiiELPYGDMTEigERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGK-TVIFVTHQ 702
Cdd:TIGR01277 115 ----QVGIADYLD--RLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQrTLLMVTHH 188
|
170 180
....*....|....*....|...
gi 1207190976 703 LQYLPE-CDDVVLMKDGQIAEHG 724
Cdd:TIGR01277 189 LSDARAiASQIAVVSQGKIKVVS 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1150-1366 |
1.75e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYrDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSlgvaLFRL----AELSRGSIIIdGVNIahigledlrs 1225
Cdd:COG0488 316 LELEGLSKSY-GDKT-LLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLlageLEPDSGTVKL-GETV---------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1226 KLSVIPQEpvlfigtvRSNLDPwdqytDAQIWEAL-------EKTHIKDMVSQL---PNSLHSEVTDngenFSVGERQLL 1295
Cdd:COG0488 379 KIGYFDQH--------QEELDP-----DKTVLDELrdgapggTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1296 CVARALLRHSKILLLDEATAAIDTETDRLIQDTIRsSFSGcTTLVIAH-R--LNTVlgCNRIMVLDQGQILEFD 1366
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1167-1360 |
1.91e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNI--------AHIGLEDLRSKLSVIPQEPV--- 1235
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldhklaAQLGIGIIYQELSVIDELTVlen 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1236 LFIGTVRS------NLDPWdqytdaqiwealEKTHIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILL 1309
Cdd:PRK09700 101 LYIGRHLTkkvcgvNIIDW------------REMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1310 LDEATAAI-DTETDRL--IQDTIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQG 1360
Cdd:PRK09700 169 MDEPTSSLtNKEVDYLflIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
560-702 |
1.95e-11 |
|
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: 64.69 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG------------FAYVAQQAWILND-SLRENILFGKKYNEEKYNAVLEAcclfpdi 626
Cdd:TIGR01189 39 KTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGLKPElSALENLHFWAAIHGGAQRTIEDA------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 627 ielpygdMTEIGERG------ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRP-AAKGKTVIFV 699
Cdd:TIGR01189 112 -------LAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGLLRAhLARGGIVLLT 183
|
...
gi 1207190976 700 THQ 702
Cdd:TIGR01189 184 THQ 186
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
560-767 |
2.01e-11 |
|
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: 66.42 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLgQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGKKYNEEKYNAVLEACCLFPDI 626
Cdd:cd03289 43 KSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 627 IELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRPAAKGKTVIFVTHQLQYL 706
Cdd:cd03289 122 EQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIEAM 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 707 PECDDVVLMKDGQIAEHGTHTQLM-EKGRDYAALFNSvqqENLVRKNLKNKEKAEKESSPQT 767
Cdd:cd03289 201 LECQRFLVIEENKVRQYDSIQKLLnEKSHFKQAISPS---DRLKLFPRRNSSKSKRKPRPQI 259
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
644-746 |
2.42e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDAR-VGSRLfhSAIRPAAKGK-TVIFVTHQLQYLPE-CDDVVLMKDGQI 720
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPElVGEVL--NTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRI 222
|
90 100
....*....|....*....|....*.
gi 1207190976 721 AEHGthtqlmekgrDYAALFNSVQQE 746
Cdd:PRK11264 223 VEQG----------PAKALFADPQQP 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
597-729 |
3.04e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.67 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 597 SLRENILFGKKY----NEEKYNAVLEACCLFpdiielpygDMTEIGERGAN-LSGGQRQRVSLARALYSERPILLLDDPL 671
Cdd:PRK11432 94 SLGENVGYGLKMlgvpKEERKQRVKEALELV---------DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPL 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 672 SAVDARVgSRLFHSAIRPAAK--GKTVIFVTH-QLQYLPECDDVVLMKDGQIAEHGTHTQL 729
Cdd:PRK11432 165 SNLDANL-RRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
644-724 |
3.09e-11 |
|
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: 64.52 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGSRL-FHSAIRPAAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIA 721
Cdd:cd03264 131 LSGGMRRRVGIAQALVGDPSILIVDEPTAGLD--PEERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLV 208
|
...
gi 1207190976 722 EHG 724
Cdd:cd03264 209 FEG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
643-729 |
3.31e-11 |
|
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: 64.45 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRPAAKGKTVIFVTHQLQ---YLpeCDDVVLMKDGQ 719
Cdd:cd03263 133 TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA-SRRAIWDLILEVRKGRSIILTTHSMDeaeAL--CDRIAIMSDGK 209
|
90
....*....|
gi 1207190976 720 IAEHGTHTQL 729
Cdd:cd03263 210 LRCIGSPQEL 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1166-1362 |
3.57e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.38 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGlEDLRSKLSV--IPQEPVLFIG-TVR 1242
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1243 SNLdpwdQYTDAQIWEALEKthIKDMVSQLPNSLHSEVtdNGENFSVGERQLLCVARALLRHSKILLLDEATAAID-TET 1321
Cdd:PRK15439 105 ENI----LFGLPKRQASMQK--MKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207190976 1322 DRLIQDtIRSSFS-GCTTLVIAHRLNTVLG-CNRIMVLDQGQI 1362
Cdd:PRK15439 177 ERLFSR-IRELLAqGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
644-724 |
3.73e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.59 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDA--RVGSRL----FHSAIrpaakGKTVIFVTH-QLQYLPECDDVVLMK 716
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalRVQMRIeisrLHKRL-----GRTMIYVTHdQVEAMTLADKIVVLD 208
|
....*...
gi 1207190976 717 DGQIAEHG 724
Cdd:PRK11000 209 AGRVAQVG 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
560-725 |
4.05e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 65.14 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG------------------------GFAYVAQQ-------AWILNDSLRENILFgkky 608
Cdd:COG4559 40 KSTLLKLLTGELTPSSGEVRLNGrplaawspwelarrravlpqhsslAFPFTVEEvvalgraPHGSSAAQDRQIVR---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 609 neekynAVLEACclfpdiielpygDMTEIGERG-ANLSGGQRQRVSLARAL-------YSERPILLLDDPLSAVDARVGS 680
Cdd:COG4559 116 ------EALALV------------GLAHLAGRSyQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDLAHQH 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207190976 681 RLFHSAIRPAAKGKTVIFVTHQL----QYlpeCDDVVLMKDGQIAEHGT 725
Cdd:COG4559 178 AVLRLARQLARRGGGVVAVLHDLnlaaQY---ADRILLLHQGRLVAQGT 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1166-1366 |
5.01e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 64.09 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLE-DLRSKLSVIpqEPVLFIGTVrSN 1244
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGgGFNPELTGR--ENIYLNGRL-LG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1245 LDPwdqytdAQIWEALEKthIKDMvSQLPNSLHSEVtdngENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRL 1324
Cdd:cd03220 114 LSR------KEIDEKIDE--IIEF-SELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207190976 1325 IQDTIRSSFSGCTTLVIA-HRLNTVLG-CNRIMVLDQGQILEFD 1366
Cdd:cd03220 181 CQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1161-1381 |
6.06e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.01 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1161 DGLPLVlKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIglEDLRSKLSVIPQEPVLFIG- 1239
Cdd:PRK11607 30 DGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHm 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1240 TVRSNLD--------PWDQYTDaQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLD 1311
Cdd:PRK11607 107 TVEQNIAfglkqdklPKAEIAS-RVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 1312 EATAAIDTE-TDRL---IQDTIRSsfSGCTTLVIAH---RLNTVLGcnRIMVLDQGQILEFDTPSNLLTDENSRFHA 1381
Cdd:PRK11607 175 EPMGALDKKlRDRMqleVVDILER--VGVTCVMVTHdqeEAMTMAG--RIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1150-1378 |
6.74e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.13 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYrdGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLED-LRSKLS 1228
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1229 VIPQEPVLFIG-TVRSNLDPWDQYTDAQIWEalekTHIKDMVSQLPNsLHSEVTDNGENFSVGERQLLCVARALLRHSKI 1307
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERDQFQ----ERIKWVYELFPR-LHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1308 LLLDEATAAIDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDENSR 1378
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQlREQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLANEAVR 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1166-1374 |
7.52e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.29 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELS-----RGSIIIDGVNI--AHIGLEDLRSKLSVIPQEPVLFI 1238
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1239 GTVRSN------LDPWDQYT--DAQIWEALEKTHIKDmvsQLPNSLHSEVTDngenFSVGERQLLCVARALLRHSKILLL 1310
Cdd:PRK14258 102 MSVYDNvaygvkIVGWRPKLeiDDIVESALKDADLWD---EIKHKIHKSALD----LSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 1311 DEATAAIDTETDRLIQDTIRSSF--SGCTTLVIAHRLNTVLGC-----------NRImvldqGQILEFDTPSNLLTD 1374
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLsdftaffkgneNRI-----GQLVEFGLTKKIFNS 246
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1166-1362 |
7.84e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.20 E-value: 7.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDG--VNIAH--------IGL--EDlRSKLSVIPQE 1233
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSprdairagIAYvpED-RKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1234 PvlfigtVRSN--LDPWDQYTDAQ-IWEALEKTHIKDMVSQL---PNSLHSEVTdngeNFSVGERQLLCVARALLRHSKI 1307
Cdd:COG1129 346 S------IRENitLASLDRLSRGGlLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 1308 LLLDEATAAIDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQI 1362
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRElAAEGKAVIVISSELPELLGlSDRILVMREGRI 472
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
638-720 |
7.96e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.31 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 638 GERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDA--RVG-SRLFHSAIRpaAKGKTVIFVTHQL-QYLPECDDVV 713
Cdd:PRK11247 128 NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAltRIEmQDLIESLWQ--QHGFTVLLVTHDVsEAVAMADRVL 205
|
....*..
gi 1207190976 714 LMKDGQI 720
Cdd:PRK11247 206 LIEEGKI 212
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
806-1312 |
8.57e-11 |
|
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: 66.36 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 806 IKAAGGPLAFIVTILLF--LFTTGSIAFSNwwlSYWIRQGSGNSSLLLGnetaesdsmrlnphiqyysrvYVLSMGAALF 883
Cdd:COG4615 8 LRESRWLLLLALLLGLLsgLANAGLIALIN---QALNATGAALARLLLL---------------------FAGLLVLLLL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 884 LKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVdVRLAMQAEMLLQNVTLVLFCLGVV 963
Cdd:COG4615 64 SRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAYL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 964 GAV-FPWFLFSIIPLGAFLFIVNRISRVLIRELKRLENiSQSPFTSHITSSLQG-----LStiyaYGRGADFIHRYqaLL 1037
Cdd:COG4615 143 AWLsPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRARE-AEDRLFKHFRALLEGfkelkLN----RRRRRAFFDED--LQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1038 DTNQACQFLFSCAMRWLAVRLDLISISLITTVALlIVLMHGHISPAYAGLALSYAvqLTGLF------QFTVRLLSETEA 1111
Cdd:COG4615 216 PTAERYRDLRIRADTIFALANNWGNLLFFALIGL-ILFLLPALGWADPAVLSGFV--LVLLFlrgplsQLVGALPTLSRA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1112 RfTSVERINHYIKNLESEGPRQitgCPTSSSSWPAEGQ-ITFQDVEMRYR---DGLPLVLKNLCFSILPEETIGIVGRTG 1187
Cdd:COG4615 293 N-VALRKIEELELALAAAEPAA---ADAAAPPAPADFQtLELRGVTYRYPgedGDEGFTLGPIDLTIRRGELVFIVGGNG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1188 SGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFigtvRSNLDPWDQYTDAQIWEALEKTHIKD 1267
Cdd:COG4615 369 SGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLERLELDH 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1207190976 1268 MVSqlpnslhsevTDNGE----NFSVGERQLLCVARALLRHSKILLLDE 1312
Cdd:COG4615 445 KVS----------VEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
642-725 |
9.23e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 65.21 E-value: 9.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVD-----------ARVGSRLfhsairpaakGKTVIFVTHQLQYLPE-C 709
Cdd:PRK11153 139 AQLSGGQKQRVAIARALASNPKVLLCDEATSALDpattrsilellKDINREL----------GLTIVLITHEMDVVKRiC 208
|
90
....*....|....*.
gi 1207190976 710 DDVVLMKDGQIAEHGT 725
Cdd:PRK11153 209 DRVAVIDAGRLVEQGT 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1175-1363 |
9.51e-11 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 63.08 E-value: 9.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1175 LPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNI----AHIGLEDLRSKLSVIPQEPVLFIG-TVRSNL---- 1245
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlNVRENLafgl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1246 ----DPWDQYTDAQIWEALEKTHIKDM-VSQLpnslhsevtdngenfSVGERQLLCVARALLRHSKILLLDEATAAIDTE 1320
Cdd:cd03297 101 krkrNREDRISVDELLDLLGLDHLLNRyPAQL---------------SGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207190976 1321 TDRLIQDTIRSSFS--GCTTLVIAHRLNTV-LGCNRIMVLDQGQIL 1363
Cdd:cd03297 166 LRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
560-727 |
9.61e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 9.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG----------FAYVAQQA---WILNDSLRENILFGK-------KYNEEKYNAVLEA 619
Cdd:PRK15056 46 KSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDVVMMGRyghmgwlRRAKKRDRQIVTA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 620 CCLFPDIIELPYgdmTEIGErganLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFV 699
Cdd:PRK15056 126 ALARVDMVEFRH---RQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVS 198
|
170 180
....*....|....*....|....*....
gi 1207190976 700 THQLQYLPE-CDDVVLMKDGQIAEHGTHT 727
Cdd:PRK15056 199 THNLGSVTEfCDYTVMVKGTVLASGPTET 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1150-1318 |
1.04e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.45 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYrDGLPLvlkNLCFSILPEETIGIVGRTGSGKSSLG--VALFRLAElsRGSIIIDGVNiaHIGLEDLRSKL 1227
Cdd:PRK10771 2 LKLTDITWLY-HHLPM---RFDLTVERGERVAILGPSGAGKSTLLnlIAGFLTPA--SGSLTLNGQD--HTTTPPSRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SVIPQEPVLFIG-TVRSN----LDPWDQYTDAQ---IWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVAR 1299
Cdd:PRK10771 74 SMLFQENNLFSHlTVAQNiglgLNPGLKLNAAQrekLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALAR 142
|
170
....*....|....*....
gi 1207190976 1300 ALLRHSKILLLDEATAAID 1318
Cdd:PRK10771 143 CLVREQPILLLDEPFSALD 161
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
644-727 |
1.14e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.49 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRP-AAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIA 721
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIV-SIIRElAETGITQVIVTHEVEVARKtASRVVYMENGHIV 220
|
....*.
gi 1207190976 722 EHGTHT 727
Cdd:PRK11124 221 EQGDAS 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
642-739 |
1.15e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.06 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDarvgsrlfhSAIRP----------AAKGKTVIFVTHQLqylpecDD 711
Cdd:PRK10771 128 GQLSGGQRQRVALARCLVREQPILLLDEPFSALD---------PALRQemltlvsqvcQERQLTLLMVSHSL------ED 192
|
90 100 110
....*....|....*....|....*....|....*
gi 1207190976 712 V-------VLMKDGQIAEHGTHTQLMEKGRDYAAL 739
Cdd:PRK10771 193 AariaprsLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1154-1376 |
1.18e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.94 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1154 DVEMRYRDGlPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAH--IGLEDLRSKLSVIP 1231
Cdd:PRK13639 6 DLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1232 QEP--VLFIGTVRS-------NLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALL 1302
Cdd:PRK13639 85 QNPddQLFAPTVEEdvafgplNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1303 RHSKILLLDEATAAID----TETDRLIQDTIRssfSGCTTLVIAHRLNTV-LGCNRIMVLDQGQILEFDTPSNLLTDEN 1376
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDpmgaSQIMKLLYDLNK---EGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
560-721 |
1.20e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG--------------GFAYV----AQQAWILNDSLRENILFG--KKY------NEEKY 613
Cdd:COG1129 291 RTELARALFGADPADSGEIRLDGkpvrirsprdairaGIAYVpedrKGEGLVLDLSIRENITLAslDRLsrggllDRRRE 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 614 NAVLEacclfpDIIEL----PYGDMTEIGergaNLSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGSRL-FHSAIR 688
Cdd:COG1129 371 RALAE------EYIKRlrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGID--VGAKAeIYRLIR 438
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207190976 689 P-AAKGKTVIFVThqlQYLPE----CDDVVLMKDGQIA 721
Cdd:COG1129 439 ElAAEGKAVIVIS---SELPEllglSDRILVMREGRIV 473
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
644-722 |
1.27e-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: 63.22 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSR----LFhsAIRpAAKGKTVIFVTHQLQYLPECDDVVLMKDGQ 719
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidlLF--ELN-RERGTTLVLVTHDPALAARCDRVLRLRAGR 223
|
...
gi 1207190976 720 IAE 722
Cdd:COG4181 224 LVE 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1178-1379 |
1.40e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.49 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1178 ETIGIVGRTGSGKSSLgvalfrLAELSrGSIIIDGVNIAHIGL------------EDLR----------------SKLSV 1229
Cdd:PRK09984 31 EMVALLGPSGSGKSTL------LRHLS-GLITGDKSAGSHIELlgrtvqregrlaRDIRksrantgyifqqfnlvNRLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IpqEPVLfIGTVRSNldP-WDQ----YTDAQIWEALEKTHIKDMVsqlpNSLHSEVTdngeNFSVGERQLLCVARALLRH 1304
Cdd:PRK09984 104 L--ENVL-IGALGST--PfWRTcfswFTREQKQRALQALTRVGMV----HFAHQRVS----TLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 1305 SKILLLDEATAAIDTETDRLIQDTIR--SSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILeFDTPSNLLtdENSRF 1379
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRyCERIVALRQGHVF-YDGSSQQF--DNERF 245
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
560-728 |
2.03e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 62.38 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG---------GFAY-------VAQQAWILND-SLRENILF-----GKKYNEEKY--NA 615
Cdd:COG2884 41 KSTLLKLLYGEERPTSGQVLVNGqdlsrlkrrEIPYlrrrigvVFQDFRLLPDrTVYENVALplrvtGKSRKEIRRrvRE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 616 VLeacclfpdiielpygDMTEIGERG----ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSR---LFHSAIR 688
Cdd:COG2884 121 VL---------------DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEimeLLEEINR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207190976 689 paaKGKTVIFVTHQLQYLPECDD-VVLMKDGQIAEHGTHTQ 728
Cdd:COG2884 186 ---RGTTVLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
644-768 |
2.23e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.72 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRPA-AKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIA 721
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAkANNKTVFVITHTMEHVLEvADEVIVMDKGKIL 255
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 722 EHGTHTQL-MEKgrdyaALFNSVQQE---------NLVRKNLKNKEKAEKEssPQTL 768
Cdd:PRK13631 256 KTGTPYEIfTDQ-----HIINSTSIQvprviqvinDLIKKDPKYKKLYQKQ--PRTI 305
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
644-725 |
2.34e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 62.87 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARAL------YSERPILLLDDPLSAVDarvgsrLFH-----SAIRPAAK--GKTVIFVTHQL----QYl 706
Cdd:PRK13548 135 LSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALD------LAHqhhvlRLARQLAHerGLAVIVVLHDLnlaaRY- 207
|
90
....*....|....*....
gi 1207190976 707 peCDDVVLMKDGQIAEHGT 725
Cdd:PRK13548 208 --ADRIVLLHQGRLVADGT 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
644-727 |
2.64e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 62.34 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRP-AAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIA 721
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVV-EIIRElSQTGITQVIVTHEVEFARKvASQVVYMEKGRII 220
|
....*.
gi 1207190976 722 EHGTHT 727
Cdd:COG4161 221 EQGDAS 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1165-1330 |
3.35e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1165 LVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIahiGLEDLRSKLSVI----PQEPVLfigT 1240
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLghrnAMKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1241 VRSNLDPWDQY---TDAQIWEALEKTHIKDmVSQLPnslhsevtdnGENFSVGERQLLCVARALLRHSKILLLDEATAAI 1317
Cdd:PRK13539 90 VAENLEFWAAFlggEELDIAAALEAVGLAP-LAHLP----------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170
....*....|...
gi 1207190976 1318 DTETDRLIQDTIR 1330
Cdd:PRK13539 159 DAAAVALFAELIR 171
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1167-1371 |
5.22e-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: 60.85 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEdLRSKLSVIPQEPVLFIG-TVRSNL 1245
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1246 D--------PWDQYTD--AQIWEALEKTHIKD-MVSqlpnslhsevtdngeNFSVGERQLLCVARALLRHSKILLLDEAT 1314
Cdd:cd03265 95 YiharlygvPGAERREriDELLDFVGLLEAADrLVK---------------TYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1315 AAIDTETDRLIQDTIRS--SFSGCTTLVIAHRLNTV-LGCNRIMVLDQGQILEFDTPSNL 1371
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
560-724 |
5.23e-10 |
|
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: 61.01 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGgfayvaQQAWIL------NDSL--RENILFG-------KKYNEEKYNAVLEACCLfP 624
Cdd:cd03220 61 KSTLLRLLAGIYPPDSGTVTVRG------RVSSLLglgggfNPELtgRENIYLNgrllglsRKEIDEKIDEIIEFSEL-G 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 625 DIIELPYGdmteigergaNLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVG---SRLFHSAIRpaaKGKTVIFVTH 701
Cdd:cd03220 134 DFIDLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQekcQRRLRELLK---QGKTVILVSH 200
|
170 180
....*....|....*....|....
gi 1207190976 702 QLQYLPE-CDDVVLMKDGQIAEHG 724
Cdd:cd03220 201 DPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
637-720 |
5.49e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.97 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 637 IGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMK 716
Cdd:PRK10535 138 VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIR 217
|
....
gi 1207190976 717 DGQI 720
Cdd:PRK10535 218 DGEI 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
633-725 |
7.82e-10 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 61.29 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 633 DMTEIGERG-ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIR--PAAKGKTVIFVTHQLQYLPEC 709
Cdd:TIGR04520 125 GMEDFRDREpHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPK-GRKEVLETIRklNKEEGITVISITHDMEEAVLA 203
|
90
....*....|....*.
gi 1207190976 710 DDVVLMKDGQIAEHGT 725
Cdd:TIGR04520 204 DRVIVMNKGKIVAEGT 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
644-796 |
7.95e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.57 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSR----LFHSAIRpaAKGKTVIFVTHQL----QYlpeCDDVVLM 715
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK-GRKemmeMFYKLHK--EKGLTTVLVTHSMedaaRY---ADQIVVM 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 716 KDGQIAEHGTHTQLMEKGRDYAALFNSVQqenlvrKNLKNKEKAEKEsspqtLHVSNPPKPDTESKKTDQLMQAEEKGSG 795
Cdd:PRK13634 220 HKGTVFLQGTPREIFADPDELEAIGLDLP------ETVKFKRALEEK-----FGISFPKPCLTLEELAHEVVQLLRKGGH 288
|
.
gi 1207190976 796 A 796
Cdd:PRK13634 289 E 289
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
642-740 |
8.91e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.73 E-value: 8.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRP-AAKGKTVIFVTHqlqYLPE----CDDVVLMK 716
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLF-RIIRRlKAQGVAIIYISH---RLDEvfeiADRVTVLR 214
|
90 100 110
....*....|....*....|....*....|.
gi 1207190976 717 DGQIAEHG-----THTQLMEK--GRDYAALF 740
Cdd:COG1129 215 DGRLVGTGpvaelTEDELVRLmvGRELEDLF 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1167-1361 |
1.03e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLR-SKLSVIPQEpvlfigtvrSNL 1245
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeAGIGIIHQE---------LNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1246 DPwdQYTDAQ-IWEALEKTHI------KDMVSQLPNSL------HSEVTDNGEnFSVGERQLLCVARALLRHSKILLLDE 1312
Cdd:PRK10762 91 IP--QLTIAEnIFLGREFVNRfgridwKKMYAEADKLLarlnlrFSSDKLVGE-LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 1313 ATAAI-DTETDRLIQdTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQ 1361
Cdd:PRK10762 168 PTDALtDTETESLFR-VIRElKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
560-702 |
1.17e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.43 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG------------GFAYVAQQAWILND-SLRENILFGKKYNEEkyNAVLEAcclfpdi 626
Cdd:cd03231 39 KTTLLRILAGLSPPLAGRVLLNGgpldfqrdsiarGLLYLGHAPGIKTTlSVLENLRFWHADHSD--EQVEEA------- 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 627 ieLPYGDMTEIGERGAN-LSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRP-AAKGKTVIFVTHQ 702
Cdd:cd03231 110 --LARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA-GVARFAEAMAGhCARGGMVVLTTHQ 184
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
644-731 |
1.23e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 62.39 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVG-------SRLfhsairPAAKGKTVIFVTHQLQ---YLpeCDDVV 713
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQaqildllRDL------QREHGLAYLFISHDLAvvrAL--AHRVM 497
|
90
....*....|....*...
gi 1207190976 714 LMKDGQIAEHGTHTQLME 731
Cdd:COG4172 498 VMKDGKVVEQGPTEQVFD 515
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
560-701 |
1.24e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 60.65 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG--------GFAYVAQqawilNDSL------RENILFGKKYN----EEKYNAVLEACC 621
Cdd:COG4525 46 KTTLLNLIAGFLAPSSGEITLDGvpvtgpgaDRGVVFQ-----KDALlpwlnvLDNVAFGLRLRgvpkAERRARAEELLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 622 LFpdiielpygDMTEIGERG-ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAK-GKTVIFV 699
Cdd:COG4525 121 LV---------GLADFARRRiWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLI 191
|
..
gi 1207190976 700 TH 701
Cdd:COG4525 192 TH 193
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1150-1379 |
1.28e-09 |
|
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: 60.05 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYrdGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDlrSKLSV 1229
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFIG-TVRSNL-----------DPWDQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCV 1297
Cdd:cd03296 79 VFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1298 ARALLRHSKILLLDEATAAIDTETD-------RLIQDTIrssfsGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPS 1369
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRkelrrwlRRLHDEL-----HVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPD 222
|
250
....*....|
gi 1207190976 1370 NLLTDENSRF 1379
Cdd:cd03296 223 EVYDHPASPF 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
644-768 |
1.43e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.77 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEH 723
Cdd:PRK13644 137 LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207190976 724 GTHTQLMEkgrDYAALFNSVQQENLVR--KNLKNKEKA---EKESSPQTL 768
Cdd:PRK13644 217 GEPENVLS---DVSLQTLGLTPPSLIElaENLKMHGVVipwENTSSPSSF 263
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1162-1368 |
1.45e-09 |
|
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: 63.11 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1162 GLPLVlKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIaHIGLEDLRSKLSVIPQEPVLFIG-T 1240
Cdd:TIGR01257 942 GRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1241 VRSNLDPWDQYTdAQIWEALEKthikDMVSQLPNS-LHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDT 1319
Cdd:TIGR01257 1020 VAEHILFYAQLK-GRSWEEAQL----EMEAMLEDTgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1320 ETDRLIQDTIRSSFSGCTTLVIAHRLNT--VLGcNRIMVLDQGQILEFDTP 1368
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMDEadLLG-DRIAIISQGRLYCSGTP 1144
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
560-725 |
1.61e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.10 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGgfayvaQQAWIL------NDSL--RENILF-----GKKYNEEKYnavleaccLFPDI 626
Cdd:COG1134 65 KSTLLKLIAGILEPTSGRVEVNG------RVSALLelgagfHPELtgRENIYLngrllGLSRKEIDE--------KFDEI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 627 IELpygdmTEIGE------RgaNLSGGQRQRVSLARALYSERPILLLDDPLSAVDA----RVGSRLFhsAIRpaAKGKTV 696
Cdd:COG1134 131 VEF-----AELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARIR--ELR--ESGRTV 199
|
170 180 190
....*....|....*....|....*....|
gi 1207190976 697 IFVTHQLQYLPE-CDDVVLMKDGQIAEHGT 725
Cdd:COG1134 200 IFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
560-702 |
1.95e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.05 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG------GFAYVAQQAWI-----LNDSL--RENILF----GKKYNEEKYNAVLEAccl 622
Cdd:PRK13538 40 KTSLLRILAGLARPDAGEVLWQGepirrqRDEYHQDLLYLghqpgIKTELtaLENLRFyqrlHGPGDDEALWEALAQ--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 623 fpdiielpygdmteIGERG------ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAI-RPAAKGKT 695
Cdd:PRK13538 117 --------------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ-GVARLEALLaQHAEQGGM 181
|
....*..
gi 1207190976 696 VIFVTHQ 702
Cdd:PRK13538 182 VILTTHQ 188
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1166-1378 |
2.10e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 59.66 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLgvalFR----LAELSRGSIIIDGVNIAHIGLeDLRSKLSV--IPQEPVLFIG 1239
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTT----FYmivgLVKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1240 -TVRSNldpwdqytdaqIWEALE-----KTHIKDMVSQLPNSLH-SEVTDN-GENFSVGERQLLCVARALLRHSKILLLD 1311
Cdd:COG1137 93 lTVEDN-----------ILAVLElrklsKKEREERLEELLEEFGiTHLRKSkAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1312 EATAAID--TETDrlIQDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDENSR 1378
Cdd:COG1137 162 EPFAGVDpiAVAD--IQKIIRHlKERGIGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILNNPLVR 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
633-732 |
2.24e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.01 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 633 DMTEIGE----RGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDA--RVGSRLfhsAIRPAAK--GKTVIFVTH-QL 703
Cdd:PRK11650 120 RILELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklRVQMRL---EIQRLHRrlKTTSLYVTHdQV 196
|
90 100
....*....|....*....|....*....
gi 1207190976 704 QYLPECDDVVLMKDGQIAEHGTHTQLMEK 732
Cdd:PRK11650 197 EAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
643-722 |
2.31e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 61.74 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLD------DPlsavDARvgsRLFHSAIRPA--AKGKTVIFVTHQLQYLPECDDVVL 714
Cdd:COG4615 457 DLSQGQRKRLALLVALLEDRPILVFDewaadqDP----EFR---RVFYTELLPElkARGKTVIAISHDDRYFDLADRVLK 529
|
....*...
gi 1207190976 715 MKDGQIAE 722
Cdd:COG4615 530 MDYGKLVE 537
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1150-1376 |
2.32e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.13 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSV 1229
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEP--VLFIGTVrsnldpWDQYT-------------DAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQL 1294
Cdd:PRK13647 84 VFQDPddQVFSSTV------WDDVAfgpvnmgldkdevERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1295 LCVARALLRHSKILLLDEATAAIDTETdrliQDTIRSSFSGC----TTLVIA-HRLNTVLG-CNRIMVLDQGQILEFDTP 1368
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRG----QETLMEILDRLhnqgKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDK 222
|
....*...
gi 1207190976 1369 SnLLTDEN 1376
Cdd:PRK13647 223 S-LLTDED 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1146-1377 |
2.35e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.60 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1146 AEGQITFQDVEMRYrdGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIglEDLRS 1225
Cdd:PRK10619 2 SENKLNVIDLHKRY--GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLV--RDKDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1226 KLSVIPQEPVLFIGT----VRSNLDPWDQYTDAQ-IWEA------LEKTHIKDMVSQLPNSLHSEVTDNGE---NFSVGE 1291
Cdd:PRK10619 78 QLKVADKNQLRLLRTrltmVFQHFNLWSHMTVLEnVMEApiqvlgLSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1292 RQLLCVARALLRHSKILLLDEATAAIDTEtdrLIQDTIRS----SFSGCTTLVIAHRLNTVLGC-NRIMVLDQGQILEFD 1366
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRImqqlAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEG 234
|
250
....*....|.
gi 1207190976 1367 TPSNLLTDENS 1377
Cdd:PRK10619 235 APEQLFGNPQS 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1150-1362 |
2.36e-09 |
|
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: 58.83 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDglPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIA-----HIGL--ED 1222
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiaarnRIGYlpEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1223 --LRSKLSVIPQepVLFIGTVRsNLDPwdQYTDAQIWEALEKTHIKDMVSQlpnslhsevtdNGENFSVGERQLLCVARA 1300
Cdd:cd03269 79 rgLYPKMKVIDQ--LVYLAQLK-GLKK--EEARRRIDEWLERLELSEYANK-----------RVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1301 LLRHSKILLLDEATAAIDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQI 1362
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
634-735 |
2.63e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.03 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 634 MTEIGERG-ANLSGGQRQRVSLARALySERP-ILLLDDPLSAVDARvGSRLFHSAIR--PAAKGKTVIFVTHQLQYLPEC 709
Cdd:PRK13635 130 MEDFLNREpHRLSGGQKQRVAIAGVL-ALQPdIIILDEATSMLDPR-GRREVLETVRqlKEQKGITVLSITHDLDEAAQA 207
|
90 100
....*....|....*....|....*.
gi 1207190976 710 DDVVLMKDGQIAEHGTHTQLMEKGRD 735
Cdd:PRK13635 208 DRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
595-746 |
2.66e-09 |
|
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: 61.36 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 595 NDSLRENILfgKKYNEEKYNAVlEACCLFPDIIElpygdMTEIGER----GANLSGGQRQRVSLARALYSERPILLLDDP 670
Cdd:TIGR03269 124 DDTVLDNVL--EALEEIGYEGK-EAVGRAVDLIE-----MVQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEP 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 671 LSAVDARVgSRLFHSAIRPAAK--GKTVIFVTHQLQYLPE-CDDVVLMKDGQIAEHGTHTQLMEKgrdYAALFNSVQQE 746
Cdd:TIGR03269 196 TGTLDPQT-AKLVHNALEEAVKasGISMVLTSHWPEVIEDlSDKAIWLENGEIKEEGTPDEVVAV---FMEGVSEVEKE 270
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1166-1345 |
2.83e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.72 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAE-----LSRGSIIIDGVNI-AHIGLEDLRSKLSVIPQEPVLFIG 1239
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1240 TVRSN---------LDPWDQY--------TDAQIWEAlekthIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALL 1302
Cdd:PRK14271 116 SIMDNvlagvrahkLVPRKEFrgvaqarlTEVGLWDA-----VKDRLSDSPFRL-----------SGGQQQLLCLARTLA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207190976 1303 RHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRL 1345
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1166-1368 |
3.47e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.94 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGvNIAHIgLE---DLRSKLSVIpqEPVLFIGTVR 1242
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSAL-LElgaGFHPELTGR--ENIYLNGRLL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1243 SnldpwdqYTDAQIWEALEktHIKDmVSQLPNSLHSEVtdngENFSVGERQLLCVARALLRHSKILLLDEATAAIDTE-- 1320
Cdd:COG1134 117 G-------LSRKEIDEKFD--EIVE-FAELGDFIDQPV----KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfq 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 1321 ---TDRLIQdtIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTP 1368
Cdd:COG1134 183 kkcLARIRE--LRE--SGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1166-1343 |
3.77e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSIlPEETI-GIVGRTGSGKSSLGVALFRLAELS-----RGSIIIDGVNIAHIGLE--DLRSKLSVIPQEPVLF 1237
Cdd:PRK14267 19 VIKGVDLKI-PQNGVfALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1238 ----------IGTVRSNLDPWDQYTDAQIWEALEKTHIKDMVSqlpnslhSEVTDNGENFSVGERQLLCVARALLRHSKI 1307
Cdd:PRK14267 98 phltiydnvaIGVKLNGLVKSKKELDERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207190976 1308 LLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAH 1343
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
642-722 |
4.46e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 58.25 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARAlYSERP-ILLLDDPLSAVDARVGSR---LFHSAIRPAAkgKTVIFVTHQLQYLPECDDVVLMKD 717
Cdd:PRK10584 145 AQLSGGEQQRVALARA-FNGRPdVLFADEPTGNLDRQTGDKiadLLFSLNREHG--TTLILVTHDLQLAARCDRRLRLVN 221
|
....*
gi 1207190976 718 GQIAE 722
Cdd:PRK10584 222 GQLQE 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
642-731 |
5.13e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.57 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDarvgSRLFHSAIRP----AAKGKTVIFVTHQLQYLPECDD-VVLMK 716
Cdd:PRK09493 135 SELSGGQQQRVAIARALAVKPKLMLFDEPTSALD----PELRHEVLKVmqdlAEEGMTMVIVTHEIGFAEKVASrLIFID 210
|
90
....*....|....*
gi 1207190976 717 DGQIAEHGTHTQLME 731
Cdd:PRK09493 211 KGRIAEDGDPQVLIK 225
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
644-725 |
5.37e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 58.70 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAK-GKTVIFVTHQLQYLPEC-DDVVLMKDGQIA 721
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHIsDKVLVMHQGEVV 229
|
....
gi 1207190976 722 EHGT 725
Cdd:COG4167 230 EYGK 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
560-702 |
6.12e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.21 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGqmtlL----GGSVSV--NGGFAYVAQQAWILNDSLRENILF---GKKYNEEKYNAVLEACCLfPDIIElp 630
Cdd:COG4178 402 KSTLLRAIAG----LwpygSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGL-GHLAE-- 474
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 631 ygDMTEIGERGANLSGGQRQRVSLARALYSeRP-ILLLDDPLSAVDARVGSRLfHSAIRPAAKGKTVIFVTHQ 702
Cdd:COG4178 475 --RLDEEADWDQVLSLGEQQRLAFARLLLH-KPdWLFLDEATSALDEENEAAL-YQLLREELPGTTVISVGHR 543
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
644-740 |
6.19e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.66 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAK-GKTVIFVTHQL-QYLPECDDVVLMKDGQIA 721
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLdEAMRIGDRIAIMQNGEVV 244
|
90 100
....*....|....*....|
gi 1207190976 722 EHGTHTQLMEK-GRDYAALF 740
Cdd:PRK10070 245 QVGTPDEILNNpANDYVRTF 264
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
901-1119 |
7.50e-09 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 58.55 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 901 SVLHD---KLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVdvrlamqAEM-------LLQNVTLVlfcLGVVGAVF--- 967
Cdd:cd18544 71 RIIYDlrrDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEAL-------NELftsglvtLIGDLLLL---IGILIAMFlln 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 968 ---PWFLFSIIPlgaFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALldtNQAcq 1044
Cdd:cd18544 141 wrlALISLLVLP---LLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEI---NQE-- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1045 fLFSCAMRwlAVRLDLI---SISLITTVALLIVLMHGhispayAGLALSYAVQLTGLFQFT---------VRLLSEteaR 1112
Cdd:cd18544 213 -YRKANLK--SIKLFALfrpLVELLSSLALALVLWYG------GGQVLSGAVTLGVLYAFIqyiqrffrpIRDLAE---K 280
|
250
....*....|....
gi 1207190976 1113 FT-------SVERI 1119
Cdd:cd18544 281 FNilqsamaSAERI 294
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
560-731 |
8.34e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 57.68 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG--------------GFAYVAQQAWILND-SLRENILFG--KKYNEEKYNAVLEACC- 621
Cdd:COG0410 42 KTTLLKAISGLLPPRSGSIRFDGeditglpphriarlGIGYVPEGRRIFPSlTVEENLLLGayARRDRAEVRADLERVYe 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 622 LFPDIIELpygdmteIGERGANLSGGQRQRVSLARALYSERPILLLDDP---LS-AVDARVGSRLfhSAIRpaAKGKTVI 697
Cdd:COG0410 122 LFPRLKER-------RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPslgLApLIVEEIFEII--RRLN--REGVTIL 190
|
170 180 190
....*....|....*....|....*....|....*
gi 1207190976 698 FVTHQLQYLPE-CDDVVLMKDGQIAEHGTHTQLME 731
Cdd:COG0410 191 LVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
633-761 |
8.47e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 58.27 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 633 DMTE-IGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvGSRLFHSAIRPAAKGK--TVIFVTHQLQYLPEC 709
Cdd:PRK13640 132 GMLDyIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA-GKEQILKLIRKLKKKNnlTVISITHDIDEANMA 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 710 DDVVLMKDGQIAEHGTHTQLMEK-------GRDYaALFNSVQQENL-----VRKNLKNKEKAEK 761
Cdd:PRK13640 211 DQVLVLDDGKLLAQGSPVEIFSKvemlkeiGLDI-PFVYKLKNKLKekgisVPQEINTEEKLVQ 273
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
597-746 |
8.65e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.25 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 597 SLRENILFGKKYNEEKynavleacclfpdiielpyGDMTEIGER------------------GANLSGGQRQRVSLARAL 658
Cdd:PRK14243 106 SIYDNIAYGARINGYK-------------------GDMDELVERslrqaalwdevkdklkqsGLSLSGGQQQRLCIARAI 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 659 YSERPILLLDDPLSAVDArVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIAEHGTHTQLMEKGRDYAA 738
Cdd:PRK14243 167 AVQPEVILMDEPCSALDP-ISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVEFDRTEK 245
|
....*...
gi 1207190976 739 LFNSVQQE 746
Cdd:PRK14243 246 IFNSPQQQ 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1150-1386 |
9.34e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 9.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDglplVLKNLCFSILPEETIGIVGRTGSGKSSLGVALF-----RlaelSRGSIIIDG--VNI------- 1215
Cdd:PRK13549 265 LTAWDPVNPHIK----RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFgaypgR----WEGEIFIDGkpVKIrnpqqai 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1216 -AHIGL--EDlRSKLSVIPQEPVLFIGTVrSNLDpwdQYTDA-QIWEALEKTHIKDMVSQL---PNSLHSEVTdngeNFS 1288
Cdd:PRK13549 337 aQGIAMvpED-RKRDGIVPVMGVGKNITL-AALD---RFTGGsRIDDAAELKTILESIQRLkvkTASPELAIA----RLS 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1289 VGERQLLCVARALLRHSKILLLDEATAAIDT----ETDRLIQDTIRssfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQIl 1363
Cdd:PRK13549 408 GGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQLVQ---QGVAIIVISSELPEVLGlSDRVLVMHEGKL- 483
|
250 260
....*....|....*....|...
gi 1207190976 1364 EFDTPSNLLTDENsrfhaMMEAA 1386
Cdd:PRK13549 484 KGDLINHNLTQEQ-----VMEAA 501
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1167-1383 |
9.84e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 9.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSL-----GVALFRLAElsrGSIIIDGVNIAHIGLEDL-RSKLSVIPQEPVL---- 1236
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLmkvlsGVYPHGTYE---GEIIFEGEELQASNIRDTeRAGIAIIHQELALvkel 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1237 ------FIGT--VRSNLDPWDQ-YTDAQIWeaLEKTHIkDMVSQLPNSlhsevtdngeNFSVGERQLLCVARALLRHSKI 1307
Cdd:PRK13549 98 svleniFLGNeiTPGGIMDYDAmYLRAQKL--LAQLKL-DINPATPVG----------NLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1308 LLLDEATAAI-DTETDRLIqDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDensRFHAMM 1383
Cdd:PRK13549 165 LILDEPTASLtESETAVLL-DIIRDlKAHGIACIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMTED---DIITMM 239
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1158-1318 |
1.05e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.88 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1158 RYRDGL-----PLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIaHIGLEDLRS-KLSVIP 1231
Cdd:PRK15112 15 RYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSqRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1232 QEPVLF------IGTV-----RSNLDPWDQYTDAQIWEALEKTHI-KDMVSQLPNSLHSevtdngenfsvGERQLLCVAR 1299
Cdd:PRK15112 94 QDPSTSlnprqrISQIldfplRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAP-----------GQKQRLGLAR 162
|
170
....*....|....*....
gi 1207190976 1300 ALLRHSKILLLDEATAAID 1318
Cdd:PRK15112 163 ALILRPKVIIADEALASLD 181
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1153-1376 |
1.15e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.64 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1153 QDVEMRYRdglplvLKNLCFSILPEETIGIVGRTGSGKSSLgvaLFRLAEL--SRGSIIIDGVNIAHIGLEDL---RSKL 1227
Cdd:PRK03695 4 NDVAVSTR------LGPLSAEVRAGEILHLVGPNGAGKSTL---LARMAGLlpGSGSIQFAGQPLEAWSAAELarhRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1228 SviPQEPVLFigtvrsNLDPWdQYTD----AQIWEALEKTHIKDMVS--QLPNSLHSEVTdngeNFSVGERQ-------L 1294
Cdd:PRK03695 75 S--QQQTPPF------AMPVF-QYLTlhqpDKTRTEAVASALNEVAEalGLDDKLGRSVN----QLSGGEWQrvrlaavV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1295 LCVARALLRHSKILLLDEATAAID----TETDRLIQDTIRssfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPS 1369
Cdd:PRK03695 142 LQVWPDINPAGQLLLLDEPMNSLDvaqqAALDRLLSELCQ---QGIAVVMSSHDLNHTLRhADRVWLLKQGKLLASGRRD 218
|
....*..
gi 1207190976 1370 NLLTDEN 1376
Cdd:PRK03695 219 EVLTPEN 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
634-731 |
1.21e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 634 MTEIGERGAN-LSGGQRQRVSLARALySERP-ILLLDDPLSAVDARVGSRLFHSAIRPAAK-GKTVIFVTH-QLQYLPEC 709
Cdd:PRK11607 139 MQEFAKRKPHqLSGGQRQRVALARSL-AKRPkLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMA 217
|
90 100
....*....|....*....|..
gi 1207190976 710 DDVVLMKDGQIAEHGTHTQLME 731
Cdd:PRK11607 218 GRIAIMNRGKFVQIGEPEEIYE 239
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
560-766 |
1.31e-08 |
|
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: 59.92 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLgQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGKKYNEEKYNAVLEACCLFPDI 626
Cdd:TIGR01271 1258 KSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVI 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 627 IELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRPAAKGKTVIFVTHQLQYL 706
Cdd:TIGR01271 1337 EQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEAL 1415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 707 PECDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFNSVQQENLVRKNLKNKEKaeKESSPQ 766
Cdd:TIGR01271 1416 LECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADRLKLFPLHRRNSSK--RKPQPK 1473
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
644-725 |
1.33e-08 |
|
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: 58.14 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGS---RLFHSAIRpaAKGKTVIFVTHQL---QYLpeCDDVVLMKD 717
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAqilNLLKDLQR--ELGLAILFITHDLgvvAEI--ADRVAVMYA 226
|
....*...
gi 1207190976 718 GQIAEHGT 725
Cdd:COG0444 227 GRIVEEGP 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1166-1362 |
1.43e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.38 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIgLEDLRsklsVIPQEpvlfigtvrSNL 1245
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-REDTR----LMFQD---------ARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1246 DPWDQYTD-----------AQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDEAT 1314
Cdd:PRK11247 93 LPWKKVIDnvglglkgqwrDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1315 AAIDTETDRLIQDTIRSSFS--GCTTLVIAHRLN-TVLGCNRIMVLDQGQI 1362
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1150-1376 |
1.59e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.48 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPL---VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIG----LED 1222
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1223 LRSKLSVIPQ--EPVLFIGTVRSNLD--------PWDQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGER 1292
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIfgpknfkmNLDEVKNYAHRLLMDLGFSRDVMSQSPFQM-----------SGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1293 QLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRS--SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPS 1369
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPK 231
|
....*..
gi 1207190976 1370 NLLTDEN 1376
Cdd:PRK13646 232 ELFKDKK 238
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
633-756 |
1.77e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.43 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 633 DMTEIGERG-ANLSGGQRQRVSLARALySERP-ILLLDDPLSAVDARvGSRLFHSAIRPAAK--GKTVIFVTHQLQYLPE 708
Cdd:PRK13650 129 GMQDFKEREpARLSGGQKQRVAIAGAV-AMRPkIIILDEATSMLDPE-GRLELIKTIKGIRDdyQMTVISITHDLDEVAL 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1207190976 709 CDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFNSVQQENLVRKNLKNK 756
Cdd:PRK13650 207 SDRVLVMKNGQVESTSTPRELFSRGNDLLQLGLDIPFTTSLVQSLRQN 254
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
560-701 |
1.78e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 56.34 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTL---LGGSVSVNG-----------GFAYVAQQAWiLND--SLRENILFG--KKYN-EEKYNAVLEAc 620
Cdd:COG4136 40 KSTLLAAIAGTLSPafsASGEVLLNGrrltalpaeqrRIGILFQDDL-LFPhlSVGENLAFAlpPTIGrAQRRARVEQA- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 621 clfpdiieLPYGDMTEIGERG-ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDA--RVGSRLF-HSAIRpaAKGKTV 696
Cdd:COG4136 118 --------LEEAGLAGFADRDpATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAalRAQFREFvFEQIR--QRGIPA 187
|
....*
gi 1207190976 697 IFVTH 701
Cdd:COG4136 188 LLVTH 192
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1285-1361 |
1.86e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.50 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1285 ENFSVGERQLLCVARALLRHSKILLLDEATAAI-DTETDRLIqDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQ 1361
Cdd:COG3845 140 EDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVMAiADRVTVLRRGK 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
560-721 |
1.86e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG--------------GFAYVAQQAWIL-NDSLRENILFG---KKYNEEKYNAVLEA-- 619
Cdd:PRK15439 50 KSTLMKIIAGIVPPDSGTLEIGGnpcarltpakahqlGIYLVPQEPLLFpNLSVKENILFGlpkRQASMQKMKQLLAAlg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 620 CCLFPDIielpygdmteigeRGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRP-AAKGKTVIF 698
Cdd:PRK15439 130 CQLDLDS-------------SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLF-SRIRElLAQGVGIVF 195
|
170 180
....*....|....*....|....*..
gi 1207190976 699 VTHQlqyLPE----CDDVVLMKDGQIA 721
Cdd:PRK15439 196 ISHK---LPEirqlADRISVMRDGTIA 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1166-1371 |
1.97e-08 |
|
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: 57.17 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSiiidgvnIAHIGledlrsKLSVIPQEPVLFIGTVRSNL 1245
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK-------IKHSG------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1246 ---DPWDQYTDAQIWEALEkthIKDMVSQLPNSLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETD 1322
Cdd:cd03291 119 ifgVSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 1323 RLIqdtirssFSGC--------TTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNL 1371
Cdd:cd03291 196 KEI-------FESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1167-1389 |
1.98e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.68 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELS--RGSIIIDGVNIAHIGLEDLRSK-LSVIPQEPVLFIG-TVR 1242
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1243 SNLdpwdqYTDAQIWEALEKTHIKDMVSQLPNSLH------SEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAA 1316
Cdd:TIGR02633 97 ENI-----FLGNEITLPGGRMAYNAMYLRAKNLLRelqldaDNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1317 IDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDensRFHAMMEAAEET 1389
Cdd:TIGR02633 172 LTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSED---DIITMMVGREIT 243
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
560-729 |
1.99e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.91 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQM---TLLGGSVSVNGG----------FAYVaQQAWILNDSL--RENILF----------GKKYNEEKYN 614
Cdd:TIGR00955 64 KTTLMNALAFRSpkgVKGSGSVLLNGMpidakemraiSAYV-QQDDLFIPTLtvREHLMFqahlrmprrvTKKEKRERVD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 615 AVLEACCLfpdiieLPYGDmTEIGERGA--NLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAK 692
Cdd:TIGR00955 143 EVLQALGL------RKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK 215
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207190976 693 GKTVIFVTHQLQYLPEC--DDVVLMKDGQIAEHGTHTQL 729
Cdd:TIGR00955 216 GKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
583-731 |
2.06e-08 |
|
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: 56.40 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 583 GFAYVAQQAWILND-SLRENIL-------FGKKYNEEKYNAVLEacclfpdiiELpygDMTEIGER-GANLSGGQRQRVS 653
Cdd:cd03218 76 GIGYLPQEASIFRKlTVEENILavleirgLSKKEREEKLEELLE---------EF---HITHLRKSkASSLSGGERRRVE 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 654 LARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQL-QYLPECDDVVLMKDGQIAEHGTHTQLME 731
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1150-1373 |
2.26e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDG--LPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRL-----AELSRGSIIIDGVNIAHIGLED 1222
Cdd:PRK15134 6 LAIENLSVAFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1223 LR----SKLSVIPQEPVLfigtvrsNLDPWD------------------QYTDAQIWEALEKTHIKDMVSQLPNSLHsev 1280
Cdd:PRK15134 86 LRgvrgNKIAMIFQEPMV-------SLNPLHtlekqlyevlslhrgmrrEAARGEILNCLDRVGIRQAAKRLTDYPH--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1281 tdngeNFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFS--GCTTLVIAHRLNTVLG-CNRIMVL 1357
Cdd:PRK15134 156 -----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVM 230
|
250
....*....|....*.
gi 1207190976 1358 DQGQILEFDTPSNLLT 1373
Cdd:PRK15134 231 QNGRCVEQNRAATLFS 246
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
639-731 |
2.35e-08 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 56.32 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 639 ERGANLSGGQRQRVSLARALySERP-ILLLDDPLSAVDARVGSRLFHSAIRPAAK-GKTVIFVTHQL-QYLPECDDVVLM 715
Cdd:TIGR01184 110 KRPGQLSGGMKQRVAIARAL-SIRPkVLLLDEPFGALDALTRGNLQEELMQIWEEhRVTVLMVTHDVdEALLLSDRVVML 188
|
90
....*....|....*.
gi 1207190976 716 KDGQIAEHGthtQLME 731
Cdd:TIGR01184 189 TNGPAANIG---QILE 201
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1181-1375 |
2.50e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.72 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1181 GIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQE-PVLFIGTVRSNLD----PWD------ 1249
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVRELVAigryPWHgalgrf 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1250 -QYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDEATAAID----TETDRL 1324
Cdd:PRK10575 121 gAADREKVEEAISLVGLKPLAHRLVDSL-----------SGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLAL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 1325 IQDTirSSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDE 1375
Cdd:PRK10575 190 VHRL--SQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1169-1386 |
2.59e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.30 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1169 NLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELS-RGSIIIDG--VNIAHIgLEDLRSKLSVIPQE-------PVLFI 1238
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNP-AQAIRAGIAMVPEDrkrhgivPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1239 GTvRSNLDPWDQYTD-AQIWEALEKTHIKDMVSQLPNSLHSEVTDNGeNFSVGERQLLCVARALLRHSKILLLDEATAAI 1317
Cdd:TIGR02633 357 GK-NITLSVLKSFCFkMRIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1318 DT----ETDRLIQDTIRssfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQiLEFDTPSNLLTDENsrfhaMMEAA 1386
Cdd:TIGR02633 435 DVgakyEIYKLINQLAQ---EGVAIIVVSSELAEVLGlSDRVLVIGEGK-LKGDFVNHALTQEQ-----VLAAA 499
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
592-722 |
2.76e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.62 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 592 WILNDSLRENILFGKKYNEEKYNAVLEAcclfpdiIELPYGDMTEigeRGANLSGGQRQRVSLARALYSERPILLLDDPL 671
Cdd:PRK10419 110 EIIREPLRHLLSLDKAERLARASEMLRA-------VDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 672 SAVDaRVgsrLFHSAIRPAAK-----GKTVIFVTHQLQyLPE--CDDVVLMKDGQIAE 722
Cdd:PRK10419 180 SNLD-LV---LQAGVIRLLKKlqqqfGTACLFITHDLR-LVErfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
644-725 |
2.98e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 56.76 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIAE 722
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIK 225
|
...
gi 1207190976 723 HGT 725
Cdd:PRK13641 226 HAS 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1166-1364 |
3.05e-08 |
|
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: 55.23 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVAL--FRLAELSRGSIIIDGVNIAHIGLEDlRSKLSVI--PQEPVLFIGtV 1241
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGIFlaFQYPPEIPG-V 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1242 RsnldpwdqytdaqiwealekthIKDMVSQLpnslhsevtdnGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTET 1321
Cdd:cd03217 93 K----------------------NADFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207190976 1322 DRLIQDTIRS-SFSGCTTLVIAHR---LNTVLGcNRIMVLDQGQILE 1364
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHYqrlLDYIKP-DRVHVLYDGRIVK 185
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
560-732 |
3.21e-08 |
|
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: 56.46 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG-------------GFAYVAQQAWILNDSLRENILFGKKYNEEKYNAVLEACCLFPDI 626
Cdd:cd03288 60 KSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 627 IELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVgSRLFHSAIRPAAKGKTVIFVTHQLQYL 706
Cdd:cd03288 140 KSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTI 218
|
170 180
....*....|....*....|....*.
gi 1207190976 707 PECDDVVLMKDGQIAEHGTHTQLMEK 732
Cdd:cd03288 219 LDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
640-725 |
3.37e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.98 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 640 RGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIR-PAAKGKTVIFVTHQLQYLPECDDVVLMKDG 718
Cdd:PRK11629 142 RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
....*..
gi 1207190976 719 QIAEHGT 725
Cdd:PRK11629 222 RLTAELS 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
560-736 |
3.90e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.94 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSAL-----LGQMTLLGGSVSVNGGFAY---------------VAQQAWILNDSLRENILFGKKYNEEKYNAVLEA 619
Cdd:PRK14239 44 KSTLLRSInrmndLNPEVTITGSIVYNGHNIYsprtdtvdlrkeigmVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 620 CclfpdiielpygdmTEIGERGAN---------------LSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFH 684
Cdd:PRK14239 124 A--------------VEKSLKGASiwdevkdrlhdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDP-ISAGKIE 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 685 SAIRPAAKGKTVIFVTHQLQYLPECDD-VVLMKDGQIAEHG-THTQLMEKGR----DY 736
Cdd:PRK14239 189 ETLLGLKDDYTMLLVTRSMQQASRISDrTGFFLDGDLIEYNdTKQMFMNPKHketeDY 246
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
597-735 |
4.14e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 55.81 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 597 SLRENILFGKKYNEEKYNAVLEacclfpDIIE---------------LpygdmteiGERGANLSGGQRQRVSLARALYSE 661
Cdd:COG1117 107 SIYDNVAYGLRLHGIKSKSELD------EIVEeslrkaalwdevkdrL--------KKSALGLSGGQQQRLCIARALAVE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 662 RPILLLDDPLSAVDarvgsrlfhsairPAAKGK------------TVIFVTHQLQYLPEC-DDVVLMKDGQIAEHGTHTQ 728
Cdd:COG1117 173 PEVLLMDEPTSALD-------------PISTAKieelilelkkdyTIVIVTHNMQQAARVsDYTAFFYLGELVEFGPTEQ 239
|
....*..
gi 1207190976 729 LMEKGRD 735
Cdd:COG1117 240 IFTNPKD 246
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
644-735 |
5.77e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIAE 722
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
90
....*....|...
gi 1207190976 723 hgTHTQLMEKGRD 735
Cdd:PRK11288 221 --TFDDMAQVDRD 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1154-1368 |
6.09e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.78 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1154 DVEMRYRDglPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDG--VNIAHIGLEDLRSKLSVIP 1231
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1232 QEP--VLFIGTVRS-------NLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALL 1302
Cdd:PRK13638 84 QDPeqQIFYTDIDSdiafslrNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCL-----------SHGQKKRVAIAGALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 1303 RHSKILLLDEATAAIDTE-TDRLIQDTIRSSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTP 1368
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAgRTQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAP 220
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
899-1119 |
6.11e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 55.95 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 899 AASVLHD---KLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMqAEMLLQNVTLVLFCLGVVGAVFPWF-LFSI 974
Cdd:cd18543 67 SLGVEHDlrtDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLaLVAL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 975 IPLGAFLFIVNRISRVLIRELKRLENiSQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTnqacqfLFSCAMRwl 1054
Cdd:cd18543 146 ASLPPLVLVARRFRRRYFPASRRAQD-QAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARR------LRATRLR-- 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 1055 AVRLD------LISISLITTVALLIV----LMHGHISpayAG--LA-LSYAVQLTGLFQFTVRLLSETEARFTSVERI 1119
Cdd:cd18543 217 AARLRarfwplLEALPELGLAAVLALggwlVANGSLT---LGtlVAfSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1162-1375 |
6.51e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.38 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1162 GLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVL----- 1236
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpgdit 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1237 ---FIGTVRSNLDP----WDQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILL 1309
Cdd:PRK10253 98 vqeLVARGRYPHQPlftrWRKEDEEAVTKAMQATGITHLADQSVDTL-----------SGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1310 LDEATAAIDTETD----RLIQDTIRSsfSGCTTLVIAHRLNTvlGC---NRIMVLDQGQILEFDTPSNLLTDE 1375
Cdd:PRK10253 167 LDEPTTWLDISHQidllELLSELNRE--KGYTLAAVLHDLNQ--ACryaSHLIALREGKIVAQGAPKEIVTAE 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1172-1318 |
6.55e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.13 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1172 FSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIA---HIGLEDLRSKLSVIPQEPVLFIG---TVRSNL 1245
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPYGSLNprkKVGQIL 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1246 -DPWDQYTDAQIWEALEKTHikDMVSQLpnSLHSEVTDNGEN-FSVGERQLLCVARALLRHSKILLLDEATAAID 1318
Cdd:PRK11308 116 eEPLLINTSLSAAERREKAL--AMMAKV--GLRPEHYDRYPHmFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
560-670 |
6.75e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.00 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG--FAYVAQQAWILND-SLRENILFGKKYN---EEKYNAVLEACCLFPDIIELpYGD 633
Cdd:COG0488 37 KSTLLKILAGELEPDSGEVSIPKGlrIGYLPQEPPLDDDlTVLDTVLDGDAELralEAELEELEAKLAEPDEDLER-LAE 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 634 -MTEIGERGA--------------------------NLSGGQRQRVSLARALYSERPILLLDDP 670
Cdd:COG0488 116 lQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
560-702 |
6.93e-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: 53.70 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVS--VNGGFAYVAQQAWILNDSLRENILFgkkyneekynavleacclfpdiielPYGDMtei 637
Cdd:cd03223 40 KSSLFRALAGLWPWGSGRIGmpEGEDLLFLPQRPYLPLGTLREQLIY-------------------------PWDDV--- 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 638 gerganLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLfHSAIRpaAKGKTVIFVTHQ 702
Cdd:cd03223 92 ------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL-YQLLK--ELGITVISVGHR 147
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
642-723 |
7.12e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLS-----AVDarvgsRLFHSAIRPAAKGKTVIFVTHQLQylpE----CDDV 712
Cdd:COG3845 140 EDLSVGEQQRVEILKALYRGARILILDEPTAvltpqEAD-----ELFEILRRLAAEGKSIIFITHKLR---EvmaiADRV 211
|
90
....*....|.
gi 1207190976 713 VLMKDGQIAEH 723
Cdd:COG3845 212 TVLRRGKVVGT 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1166-1364 |
7.23e-08 |
|
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: 57.00 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRL----AELSRGSIIIDGVNIAHIGLEDLR----SKLSVIPQEPVlf 1237
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPM-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1238 igtvrSNLDPW----DQ----------YTDAQIW----EALEKTHIKD---MVSQLPNSLhsevtdngenfSVGERQLLC 1296
Cdd:COG4172 103 -----TSLNPLhtigKQiaevlrlhrgLSGAAARaralELLERVGIPDperRLDAYPHQL-----------SGGQRQRVM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1297 VARALLRHSKILLLDEATAAIDTETDR----LIQDTIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILE 1364
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALDVTVQAqildLLKDLQRE--LGMALLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
644-729 |
7.52e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.49 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLfHSAIRPAAKGKTVIFVTHQL-QYLPECDDVVLMKDGQIAE 722
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVE 242
|
....*..
gi 1207190976 723 HGTHTQL 729
Cdd:PRK14271 243 EGPTEQL 249
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1150-1361 |
7.67e-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: 52.84 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLplVLKNLCFSILPEETIGIVGRTGSGKSSLgvalfrlaelsrgsiiidgvniahigledlrskLSV 1229
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEPVLFIGTVrsnldpwdqytdaqiwealeKTHIKDMVSQLPNslhsevtdngenFSVGERQLLCVARALLRHSKILL 1309
Cdd:cd03221 46 IAGELEPDEGIV--------------------TWGSTVKIGYFEQ------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1310 LDEATAAIDTETDRLIQDTIRsSFSGcTTLVIAH-R--LNTVlgCNRIMVLDQGQ 1361
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALK-EYPG-TVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1166-1375 |
8.57e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.63 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIII-DGVNIAHIGLED---------------LRSKLSV 1229
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgDIYIGDKKNNHElitnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IPQEP--VLFIGTVRSNLDPWDQYTDAQIWEALEKT--HIKDMvsqlpnSLHSEVTD-NGENFSVGERQLLCVARALLRH 1304
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAkfYLNKM------GLDDSYLErSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1305 SKILLLDEATAAIDTETDRLIQDTIRSS-FSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDE 1375
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1150-1374 |
8.82e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 56.35 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRY---RDGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIII----DGVNIAHIGLeD 1222
Cdd:TIGR03269 280 IKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-D 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1223 LRSK----LSVIPQEPVLFI-GTVRSNLdpwdqyTDAQIWE-----------------ALEKTHIKDMVSQLPNSLhsev 1280
Cdd:TIGR03269 359 GRGRakryIGILHQEYDLYPhRTVLDNL------TEAIGLElpdelarmkavitlkmvGFDEEKAEEILDKYPDEL---- 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1281 tdngenfSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFS--GCTTLVIAHRLNTVLG-CNRIMVL 1357
Cdd:TIGR03269 429 -------SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALM 501
|
250
....*....|....*..
gi 1207190976 1358 DQGQILEFDTPSNLLTD 1374
Cdd:TIGR03269 502 RDGKIVKIGDPEEIVEE 518
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
585-713 |
8.97e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 585 AYVAQQAWILNDSLRENILF-----GKKYNEEKYNAVLEAcclfpdiIELPygdmTEIGERGAN-LSGGQRQRVSLARAL 658
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFpwqirNQQPDPAIFLDDLER-------FALP----DTILTKNIAeLSGGEKQRISLIRNL 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 659 YSERPILLLDDPLSAVD---ARVGSRLFHSAIRpaAKGKTVIFVTHQLQYLPECDDVV 713
Cdd:PRK10247 153 QFMPKVLLLDEITSALDesnKHNVNEIIHRYVR--EQNIAVLWVTHDKDEINHADKVI 208
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
903-1082 |
9.22e-08 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 55.51 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 903 LHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAV-FPWFLFSIIPLGAFL 981
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdWKLTLIALVVLPLAA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 982 FIVNRISRvLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYqalldtNQACQFLFSCAMRWLAVRlDLI 1061
Cdd:cd18552 154 LPIRRIGK-RLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRF------RKANERLRRLSMKIARAR-ALS 225
|
170 180 190
....*....|....*....|....*....|
gi 1207190976 1062 S--ISLITTVALLIVL-------MHGHISP 1082
Cdd:cd18552 226 SplMELLGAIAIALVLwyggyqvISGELTP 255
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1172-1374 |
9.83e-08 |
|
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: 55.88 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1172 FSILPEETIGIVGRTGSGKSSL--GVA-LFRLAelsRGSIIIDG---------VNI-AHigledlRSKLSVIPQEPVLFI 1238
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLlrAIAgLERPD---SGRIRLGGevlqdsargIFLpPH------RRRIGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1239 G-TVRSNLdpwdQYTDAQIWEALEKTHIKDMVSQL---------PNSLhsevtdngenfSVGERQLLCVARALLRHSKIL 1308
Cdd:COG4148 91 HlSVRGNL----LYGRKRAPRAERRISFDEVVELLgighlldrrPATL-----------SGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1309 LLDEATAAIDTETDRLIQD---TIRSSFsGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTD 1374
Cdd:COG4148 156 LMDEPLAALDLARKAEILPyleRLRDEL-DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
583-725 |
9.85e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.40 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 583 GFAYVAQQAWILNDSLRENILFGKKY----NEEKYNAVLEacclFPDIIELPygdmTEIGERGA-NLSGGQRQRVSLARA 657
Cdd:PRK13645 93 GLVFQFPEYQLFQETIEKDIAFGPVNlgenKQEAYKKVPE----LLKLVQLP----EDYVKRSPfELSGGQKRRVALAGI 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 658 LYSERPILLLDDPLSAVDARvGSRLFHSAIRPAAK--GKTVIFVTHQL-QYLPECDDVVLMKDGQIAEHGT 725
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKeyKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1150-1366 |
1.19e-07 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 53.80 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYrdGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAhigleDLRSK--- 1226
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-----DLPPKdrd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1227 LSVIPQEPVLFIG-TVRSNLD--------PWDQyTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCV 1297
Cdd:cd03301 74 IAMVFQNYALYPHmTVYDNIAfglklrkvPKDE-IDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 1298 ARALLRHSKILLLDEATAAID--------TETDRLIQDTirssfsGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFD 1366
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDaklrvqmrAELKRLQQRL------GTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1178-1367 |
1.35e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.10 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1178 ETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDL---RSKLSVIPQEPVlfigtvrSNLDPwdQYTDA 1254
Cdd:PRK15079 48 ETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDPL-------ASLNP--RMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1255 Q-IWEALE-----------KTHIKDM---VSQLPNSL----HSevtdngenFSVGERQLLCVARALLRHSKILLLDEATA 1315
Cdd:PRK15079 119 EiIAEPLRtyhpklsrqevKDRVKAMmlkVGLLPNLInrypHE--------FSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 1316 AIDTETD----RLIQDTIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDT 1367
Cdd:PRK15079 191 ALDVSIQaqvvNLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGT 245
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
644-724 |
1.48e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.32 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSR---LFHSAIRPAAKGktVIFVTHQLQYLPEC-DDVVLMKDGQ 719
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARildLLESIVQKRALG--MLLVTHDMGVVARLaDDVAVMSHGR 218
|
....*
gi 1207190976 720 IAEHG 724
Cdd:PRK10418 219 IVEQG 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1166-1364 |
1.66e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.86 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLgVALFRLAELSR-GSIIIDG--------VNIAHIGLedLRSKLSVIPQE--- 1233
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSL-LRVLNLLEMPRsGTLNIAGnhfdfsktPSDKAIRE--LRRNVGMVFQQynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1234 -PVLfigTVRSNLdpwdqytdaqiWEA------LEKTHIKDMVSQLPNSLHseVTDNGENF----SVGERQLLCVARALL 1302
Cdd:PRK11124 94 wPHL---TVQQNL-----------IEApcrvlgLSKDQALARAEKLLERLR--LKPYADRFplhlSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1303 RHSKILLLDEATAAIDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILE 1364
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
643-731 |
1.69e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGSR--LFHSAIRPAAKGKTVIFVTHQlqyLPE----CDDVVLMK 716
Cdd:PRK11288 396 NLSGGNQQKAILGRWLSEDMKVILLDEPTRGID--VGAKheIYNVIYELAAQGVAVLFVSSD---LPEvlgvADRIVVMR 470
|
90
....*....|....*
gi 1207190976 717 DGQIAEHGTHTQLME 731
Cdd:PRK11288 471 EGRIAGELAREQATE 485
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1150-1376 |
1.74e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.12 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGlPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAhiglEDLRSKL-S 1228
Cdd:PRK15056 7 IVVNDVTVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1229 VIPQE-------PVLFIGTV---RSNLDPWDQYTDAQ----IWEALEKThikDMVsqlpNSLHSEVtdnGEnFSVGERQL 1294
Cdd:PRK15056 82 YVPQSeevdwsfPVLVEDVVmmgRYGHMGWLRRAKKRdrqiVTAALARV---DMV----EFRHRQI---GE-LSGGQKKR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1295 LCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNLLT 1373
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFT 230
|
...
gi 1207190976 1374 DEN 1376
Cdd:PRK15056 231 AEN 233
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
850-1038 |
1.85e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 54.40 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 850 LLGNETAESDSMRLNPHIQYYSRVYVLSMGAALFLKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILN 929
Cdd:cd18577 29 FTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 930 RFSKDMDEvdVRLAMqAE---MLLQNVTLVLFCLgVVGAVFPW----FLFSIIPLGAFLFIVnrISRVLIR-ELKRLENI 1001
Cdd:cd18577 109 RLTSDTNL--IQDGI-GEklgLLIQSLSTFIAGF-IIAFIYSWkltlVLLATLPLIAIVGGI--MGKLLSKyTKKEQEAY 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207190976 1002 SQSpfTSHITSSLQGLSTIYAYGRGADFIHRYQALLD 1038
Cdd:cd18577 183 AKA--GSIAEEALSSIRTVKAFGGEEKEIKRYSKALE 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1172-1362 |
2.03e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1172 FSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNI----------AHIGL--EDlRSKLSVIPqepvlfIG 1239
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirsprdairAGIMLcpED-RKAEGIIP------VH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1240 TVRSNLD--------PWDQYTDAQiWEA-LEKTHIKDMVSQLPnslhsevtdNGE----NFSVGERQLLCVARALLRHSK 1306
Cdd:PRK11288 347 SVADNINisarrhhlRAGCLINNR-WEAeNADRFIRSLNIKTP---------SREqlimNLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 1307 ILLLDEATAAIDTETDRLIQDTI-RSSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQI 1362
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
560-721 |
2.22e-07 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 53.43 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQM---TLLGGSVSVNG----------GFAYVAQQ-AWILNDSLRENILF-----GKKYNEEKYNAVLEAC 620
Cdd:cd03234 46 KTTLLDAISGRVeggGTTSGQILFNGqprkpdqfqkCVAYVRQDdILLPGLTVRETLTYtailrLPRKSSDAIRKKRVED 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 621 CLFPDIIELPYGdmteiGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVT 700
Cdd:cd03234 126 VLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTI 200
|
170 180
....*....|....*....|....*..
gi 1207190976 701 HQlqylPEC------DDVVLMKDGQIA 721
Cdd:cd03234 201 HQ----PRSdlfrlfDRILLLSSGEIV 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
641-729 |
2.25e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.90 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 641 GANLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDD-VVLMKDGQ 719
Cdd:PRK14246 151 ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARVADyVAFLYNGE 229
|
90
....*....|
gi 1207190976 720 IAEHGTHTQL 729
Cdd:PRK14246 230 LVEWGSSNEI 239
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1158-1362 |
2.29e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.28 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1158 RYRDG--LPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHI---GLEDLRS-KLSVIP 1231
Cdd:PRK11629 14 RYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1232 Q-----------EPV---LFIGTVRSNldpwdqytdaqiwEALEKTHikDMVSQLpnSLHSEVTDNGENFSVGERQLLCV 1297
Cdd:PRK11629 94 QfhhllpdftalENVampLLIGKKKPA-------------EINSRAL--EMLAAV--GLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1298 ARALLRHSKILLLDEATAAIDTETD----RLIQDTIRSsfSGCTTLVIAHRLNTVLGCNRIMVLDQGQI 1362
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNAdsifQLLGELNRL--QGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
593-724 |
2.32e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.76 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 593 ILNDSLRENILFGKKYN---------EEKYNAVLEACCLFPDIielpygdMTEIGERGANLSGGQRQRVSLARALYSERP 663
Cdd:PRK14247 94 IPNLSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPE 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 664 ILLLDDPLSAVDARVGSRLfHSAIRPAAKGKTVIFVTHQLQYLPECDD-VVLMKDGQIAEHG 724
Cdd:PRK14247 167 VLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHFPQQAARISDyVAFLYKGQIVEWG 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
642-746 |
2.36e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.10 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhsAIRPAAKGK---TVIFVTHQLQYLPE-CDDVVLMKD 717
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL--ALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQ 501
|
90 100
....*....|....*....|....*....
gi 1207190976 718 GQIAEHGthtqlmekgrDYAALFNSVQQE 746
Cdd:PRK15134 502 GEVVEQG----------DCERVFAAPQQE 520
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
643-724 |
3.07e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.94 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSR----LFHSAIRpaaKGKTVIFVTHQLQY-LPECDDVVLMKD 717
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP-QGVKeileIFDNLNK---QGKTIILVTHDLDNvLEWTKRTIFFKD 240
|
....*..
gi 1207190976 718 GQIAEHG 724
Cdd:PRK13651 241 GKIIKDG 247
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
644-733 |
3.26e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.60 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIR--PAAKGKTVIFVTHQLQYLPECDDVVLMKDGQIA 721
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL-DLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVY 221
|
90
....*....|..
gi 1207190976 722 EHGTHTQLMEKG 733
Cdd:PRK13648 222 KEGTPTEIFDHA 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1166-1364 |
3.74e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.83 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNI-AHIGLEDLRSKLSVIPQEpvlfIGTVRSN 1244
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIRQLRQH----VGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1245 LDPWDQYTdaqiweALE---------KTHIKDMVSQLPNSLHSEVTDNGEN------FSVGERQLLCVARALLRHSKILL 1309
Cdd:PRK11264 94 FNLFPHRT------VLEniiegpvivKGEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 1310 LDEATAAIDTETDRLIQDTIRSSFSGCTTLVI-AHRLNTVLG-CNRIMVLDQGQILE 1364
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIvTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
642-731 |
3.89e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.92 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRPAAKGKTVIFVTHQ-LQYLPECDDVVLMKDGQI 720
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKL 226
|
90
....*....|.
gi 1207190976 721 AEHGTHTQLME 731
Cdd:PRK14267 227 IEVGPTRKVFE 237
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
597-732 |
4.30e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.68 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 597 SLRENIL-FGKKY--NEEKYNAVLeacclfPDIIELPYGDmTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSA 673
Cdd:PRK13536 130 TVRENLLvFGRYFgmSTREIEAVI------PSLLEFARLE-SKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 674 VDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPE-CDDVVLMKDG-QIAEHGTHTQLMEK 732
Cdd:PRK13536 203 LDPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHALIDEH 263
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
644-738 |
4.34e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.78 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGS-------RLFHSAirpaakGKTVIFVTHQLQ---YLpeCDDVV 713
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREqmqtlllKLWQET------GKQVLLITHDIEeavFM--ATELV 200
|
90 100
....*....|....*....|....*..
gi 1207190976 714 LMK--DGQIAEHGThtqlMEKGRDYAA 738
Cdd:PRK11248 201 LLSpgPGRVVERLP----LNFARRFVA 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
644-725 |
4.65e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 53.16 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIAE 722
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIK 217
|
...
gi 1207190976 723 HGT 725
Cdd:PRK13639 218 EGT 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
643-725 |
4.66e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.88 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIR-PAAKGKTVIFVTHQLQYLPECDD-VVLMKDGQI 720
Cdd:PRK13652 137 HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlPETYGMTVIFSTHQLDLVPEMADyIYVMDKGRI 216
|
....*
gi 1207190976 721 AEHGT 725
Cdd:PRK13652 217 VAYGT 221
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
879-1037 |
5.12e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 52.98 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 879 GAALF---LKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSkDMDEVDVRLAMQAEMLLQNVTL 955
Cdd:cd18782 50 VAALLeavLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLLDVLF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 956 VLFCLGVVgAVFPWFL----FSIIPL-GAFLFIVNRISRVLIRELKRleniSQSPFTSHITSSLQGLSTIYAYGRGADFI 1030
Cdd:cd18782 129 SVIYIAVL-FSYSPLLtlvvLATVPLqLLLTFLFGPILRRQIRRRAE----ASAKTQSYLVESLTGIQTVKAQNAELKAR 203
|
....*..
gi 1207190976 1031 HRYQALL 1037
Cdd:cd18782 204 WRWQNRY 210
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
644-704 |
5.49e-07 |
|
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: 50.82 E-value: 5.49e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 644 LSGGQRQRVSLARAL----YSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQ 704
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPE 142
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
643-722 |
5.91e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLD------DPlsavdarVGSRLFHSAIRPA--AKGKTVIFVTHQLQYLPECDDVVL 714
Cdd:PRK10522 449 KLSKGQKKRLALLLALAEERDILLLDewaadqDP-------HFRREFYQVLLPLlqEMGKTIFAISHDDHYFIHADRLLE 521
|
....*...
gi 1207190976 715 MKDGQIAE 722
Cdd:PRK10522 522 MRNGQLSE 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
644-724 |
6.04e-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: 53.65 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSaIRPAAK--GKTVIFVTHQLQYLPE-CDDVVLMKDGQI 720
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHS-ILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKI 506
|
....
gi 1207190976 721 AEHG 724
Cdd:TIGR03269 507 VKIG 510
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1160-1318 |
6.85e-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: 51.34 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1160 RDGLpLVLKNLCFSILPEETIGIVGRTGSGKSSLgvaLFRLAELSR---GSIIIDGVNIAHIGLEDLRSKLSVIPQEPVL 1236
Cdd:cd03231 10 RDGR-ALFSGLSFTLAAGEALQVTGPNGSGKTTL---LRILAGLSPplaGRVLLNGGPLDFQRDSIARGLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1237 FIGTVRSNLDPW-DQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDEATA 1315
Cdd:cd03231 86 TTLSVLENLRFWhADHSDEQVEEALARVGLNGFEDRPVAQL-----------SAGQQRRVALARLLLSGRPLWILDEPTT 154
|
...
gi 1207190976 1316 AID 1318
Cdd:cd03231 155 ALD 157
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
586-729 |
7.57e-07 |
|
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: 51.60 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 586 YVAQQAwILNDSL--RENI-LFGKKY---NEEKYNAVLEAcclfpdiieLPYGDMTEIGER-GANLSGGQRQRVSLARAL 658
Cdd:cd03265 77 IVFQDL-SVDDELtgWENLyIHARLYgvpGAERRERIDEL---------LDFVGLLEAADRlVKTYSGGMRRRLEIARSL 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 659 YSERPILLLDDPLSAVDARVGSRLFhSAIRP--AAKGKTVIFVTHqlqYLPE----CDDVVLMKDGQIAEHGTHTQL 729
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVW-EYIEKlkEEFGMTILLTTH---YMEEaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1150-1343 |
8.66e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.40 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDglPLVLKNLCFSILPEETIGIVGRTGSGKSSLgvalFRL----AELSRGSIII-DGVNIAhigledlr 1224
Cdd:TIGR03719 323 IEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTL----FRMitgqEQPDSGTIEIgETVKLA-------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1225 sklsvipqepvlFIGTVRSNLDPwdqytDAQIWEALEKTHikDMVsQLPN-SLHSEVTDNGENF------------SVGE 1291
Cdd:TIGR03719 389 ------------YVDQSRDALDP-----NKTVWEEISGGL--DII-KLGKrEIPSRAYVGRFNFkgsdqqkkvgqlSGGE 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 1292 RQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIrSSFSGCtTLVIAH 1343
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL-LNFAGC-AVVISH 498
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1153-1345 |
8.99e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1153 QDVEMRYrdGLPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAEL-----SRGSIIIDGVNI--AHIGLEDLRS 1225
Cdd:PRK14243 14 ENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1226 KLSVIPQEPVLFIGTVRSNL------DPWDQYTDAQIWEALEKTHIKDMVSqlpnslhSEVTDNGENFSVGERQLLCVAR 1299
Cdd:PRK14243 92 RIGMVFQKPNPFPKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEVK-------DKLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207190976 1300 ALLRHSKILLLDEATAAIDTETDRLIQDTIRSSFSGCTTLVIAHRL 1345
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
908-1082 |
9.29e-07 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 52.06 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 908 FKTLLLSPMRFFDTTPLGRILNRFSkdmDEVDVRLAMqAEMLLQ---NVTLVLFCLGVVgAVFPWFLFSI--IPLGAFLF 982
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFN---DANKIREAI-SSTTISlflDLLMVIISGIIL-FFYNWKLFLItlLIIPLYIL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 983 IVNRISRVlIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNQACQFLFScamrWLAVRLDLIS 1062
Cdd:cd18570 157 IILLFNKP-FKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLG----KLSNLQSSIK 231
|
170 180
....*....|....*....|....*.
gi 1207190976 1063 --ISLITTVALLIV----LMHGHISP 1082
Cdd:cd18570 232 glISLIGSLLILWIgsylVIKGQLSL 257
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
644-720 |
9.49e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.57 E-value: 9.49e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKT-VIFVTHQLQ-YLPECDDVVLMKDGQI 720
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDeILRLADRVVVLEQGKV 207
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
644-743 |
9.91e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.34 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQ--LQYLPECDDVVLMKDGQIA 721
Cdd:PLN03211 207 ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpsSRVYQMFDSVLVLSEGRCL 286
|
90 100
....*....|....*....|..
gi 1207190976 722 EHGthtqlmeKGRDYAALFNSV 743
Cdd:PLN03211 287 FFG-------KGSDAMAYFESV 301
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1162-1364 |
9.98e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.32 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1162 GLPLVLKnlcfsilPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGlEDLRSKLS------------V 1229
Cdd:PRK10584 28 GVELVVK-------RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD-EEARAKLRakhvgfvfqsfmL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1230 IP--------QEPVLFIGTVrsnldpwDQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARAL 1301
Cdd:PRK10584 100 IPtlnalenvELPALLRGES-------SRQSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 1302 LRHSKILLLDEATAAIDTETDRLIQDTIrssFS-----GCTTLVIAHRLNTVLGCNRIMVLDQGQILE 1364
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLL---FSlnrehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
644-732 |
1.08e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.93 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVV-LMKDGQIAE 722
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVyVLRQGQILT 216
|
90
....*....|....*.
gi 1207190976 723 HG------THTQLMEK 732
Cdd:PRK13638 217 HGapgevfACTEAMEQ 232
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
901-1078 |
1.30e-06 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 51.70 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 901 SVLHD---KLFKTLLLSPMRFFDTTPLGRILNRFSKDMDevdvrlAMQaeMLLQN--VTLVLFCLGVVGAVFPWFL---- 971
Cdd:cd18545 70 RILYDlrqDLFSHLQKLSFSFFDSRPVGKILSRVINDVN------SLS--DLLSNglINLIPDLLTLVGIVIIMFSlnvr 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 972 -----FSIIPlgaFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNqacqfl 1046
Cdd:cd18545 142 lalvtLAVLP---LLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNREN------ 212
|
170 180 190
....*....|....*....|....*....|....*
gi 1207190976 1047 FSCAMRwlAVRL-DLI--SISLITTVALLIVLMHG 1078
Cdd:cd18545 213 RKANMR--AVRLnALFwpLVELISALGTALVYWYG 245
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
644-732 |
1.31e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 52.04 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVD-----------ARVGSRLfhsairpaakGKTVIFVTHQL---QYLpeC 709
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqaqvlnllEDLQDEL----------GLTYLFISHDLsvvRHI--S 225
|
90 100
....*....|....*....|...
gi 1207190976 710 DDVVLMKDGQIAEHGTHTQLMEK 732
Cdd:COG4608 226 DRVAVMYLGKIVEIAPRDELYAR 248
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
645-734 |
2.09e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 645 SGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSR---LFHSAIRPAakGKTVIFVTHQLQYLPE-CDDVVLMKDGQI 720
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQvlnLMMDLQQEL--GLSYVFISHDLSVVEHiADEVMVMYLGRC 233
|
90
....*....|....
gi 1207190976 721 AEHGTHTQLMEKGR 734
Cdd:PRK11308 234 VEKGTKEQIFNNPR 247
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1160-1320 |
2.18e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.80 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1160 RDGLPLvLKNLCFSILPEETIGIVGRTGSGKSSLgvaLFRLAELSR---GSIIIDGVNIAHIGlEDLRSKLsvipqepvL 1236
Cdd:PRK13538 11 RDERIL-FSGLSFTLNAGELVQIEGPNGAGKTSL---LRILAGLARpdaGEVLWQGEPIRRQR-DEYHQDL--------L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1237 FIG---TVRSNLDPW----------DQYTDAQIWEALEKTHIKDM----VSQLpnslhsevtdngenfSVGERQLLCVAR 1299
Cdd:PRK13538 78 YLGhqpGIKTELTALenlrfyqrlhGPGDDEALWEALAQVGLAGFedvpVRQL---------------SAGQQRRVALAR 142
|
170 180
....*....|....*....|.
gi 1207190976 1300 ALLRHSKILLLDEATAAIDTE 1320
Cdd:PRK13538 143 LWLTRAPLWILDEPFTAIDKQ 163
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
560-769 |
2.21e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG--------------GFAYVAQQAWILND-SLRENILFGK------------KYNEEK 612
Cdd:PRK09700 44 KSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlGIGIIYQELSVIDElTVLENLYIGRhltkkvcgvniiDWREMR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 613 YNAvleacclfpDIIELPYGDMTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAK 692
Cdd:PRK09700 124 VRA---------AMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 693 GKTVIFVTHQLQYLPE-CDDVVLMKDGQIAehgthtqlmekgrdYAALFNSVQQENLVR----KNLKNKEKAEKESSPQT 767
Cdd:PRK09700 195 GTAIVYISHKLAEIRRiCDRYTVMKDGSSV--------------CSGMVSDVSNDDIVRlmvgRELQNRFNAMKENVSNL 260
|
..
gi 1207190976 768 LH 769
Cdd:PRK09700 261 AH 262
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1167-1371 |
2.29e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLED-LRSKLSVIPQE----PVLfigTV 1241
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1242 RSNLdpwdqytdaqiwealekthikdMVSQLPNS--------LHSEVTDN----GENF---------SVGERQLLCVARA 1300
Cdd:PRK11288 97 AENL----------------------YLGQLPHKggivnrrlLNYEAREQlehlGVDIdpdtplkylSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 1301 LLRHSKILLLDEATAAIDT-ETDRL--IQDTIRSsfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQ-ILEFDTPSNL 1371
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSArEIEQLfrVIRELRA--EGRVILYVSHRMEEIFAlCDAITVFKDGRyVATFDDMAQV 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1166-1376 |
2.36e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.96 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEP--VLFIGTVRS 1243
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1244 -------NLDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDEATAA 1316
Cdd:PRK13652 99 diafgpiNLGLDEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1317 IDTETDRLIQDTIR--SSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDEN 1376
Cdd:PRK13652 168 LDPQGVKELIDFLNdlPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
560-723 |
2.67e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.60 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG--FAYVAQQAWIL--NDSLRENIlfgKKYNEEKYNAVLEACC---LFPdiielpyG 632
Cdd:COG0488 354 KSTLLKLLAGELEPDSGTVKLGETvkIGYFDQHQEELdpDKTVLDEL---RDGAPGGTEQEVRGYLgrfLFS-------G 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 633 DM--TEIGergaNLSGGQRQRVSLARALYSERPILLLDDP-----LSAVDArvgsrL------FhsairpaaKGkTVIFV 699
Cdd:COG0488 424 DDafKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldIETLEA-----LeealddF--------PG-TVLLV 485
|
170 180
....*....|....*....|....*.
gi 1207190976 700 THQlQYLPE--CDDVVLMKDGQIAEH 723
Cdd:COG0488 486 SHD-RYFLDrvATRILEFEDGGVREY 510
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1150-1388 |
2.69e-06 |
|
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: 51.73 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYrDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSL--------------GVALFRLA-------------- 1201
Cdd:TIGR03269 1 IEVKNLTKKF-DGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLmhvlrgmdqyeptsGRIIYHVAlcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1202 -------ELSRGSIIIDGVNIAHIGLEDLRSKLSVIPQEPVLFIG--TVRSN----LDPWDQYTDAQIWEALEkthIKDM 1268
Cdd:TIGR03269 79 gepcpvcGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvleaLEEIGYEGKEAVGRAVD---LIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1269 VSqlpnsLHSEVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSSF--SGCTTLVIAHrLN 1346
Cdd:TIGR03269 156 VQ-----LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSH-WP 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1207190976 1347 TVLG--CNRIMVLDQGQILEFDTPSNLLtdenSRFhamMEAAEE 1388
Cdd:TIGR03269 230 EVIEdlSDKAIWLENGEIKEEGTPDEVV----AVF---MEGVSE 266
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
583-675 |
2.76e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 50.03 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 583 GFAYVAQQAWILND-SLRENILfgkkyneekynAVLEacclfpdIIELPYGDMTEIGE--------------RGANLSGG 647
Cdd:COG1137 79 GIGYLPQEASIFRKlTVEDNIL-----------AVLE-------LRKLSKKEREERLEelleefgithlrksKAYSLSGG 140
|
90 100
....*....|....*....|....*...
gi 1207190976 648 QRQRVSLARALYSERPILLLDDPLSAVD 675
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
642-677 |
3.22e-06 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 49.74 E-value: 3.22e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDAR 677
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAA 186
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
906-1075 |
3.64e-06 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 50.56 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 906 KLFKTLL-LSPmRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCL-----------GVVGAVFPwflFS 973
Cdd:cd18575 74 AVFAHLLrLSP-SFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLvmlfitspkltLLVLLVIP---LV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 974 IIPLGAFLFIVNRISRvliRELKRLENISqspftSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNqacqflFSCAMRW 1053
Cdd:cd18575 150 VLPIILFGRRVRRLSR---ASQDRLADLS-----AFAEETLSAIKTVQAFTREDAERQRFATAVEAA------FAAALRR 215
|
170 180
....*....|....*....|..
gi 1207190976 1054 LAVRldlisiSLITTVALLIVL 1075
Cdd:cd18575 216 IRAR------ALLTALVIFLVF 231
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
873-1036 |
3.66e-06 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 50.48 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 873 VYVLSMGAALflktIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVdvrlamqAEMLLQN 952
Cdd:cd18547 54 LYLLSALFSY----LQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNI-------SQALSQS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 953 VTLVLF-CLGVVGAVFpwFLFSI-----------IPLGAFL-FIVNRISRVLIRelKRLENISQspFTSHITSSLQGLST 1019
Cdd:cd18547 123 LTQLISsILTIVGTLI--MMLYIsplltlivlvtVPLSLLVtKFIAKRSQKYFR--KQQKALGE--LNGYIEEMISGQKV 196
|
170
....*....|....*..
gi 1207190976 1020 IYAYGRGADFIHRYQAL 1036
Cdd:cd18547 197 VKAFNREEEAIEEFDEI 213
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1150-1374 |
3.80e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.40 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLP---LVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIA----HIGLED 1222
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1223 LRSKLSVIPQ--EPVLFIGTVRSNLDPWDQYTDAQIWEALEKThiKDMVSQLpnSLHSEVTDNGE-NFSVGERQLLCVAR 1299
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKA--REMIELV--GLPEELLARSPfELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1300 ALLRHSKILLLDEATAAIDTETDRLIQDTirssFS------GCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLL 1372
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEM----FYklhkekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIF 234
|
..
gi 1207190976 1373 TD 1374
Cdd:PRK13634 235 AD 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
527-732 |
3.98e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.12 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 527 QSIRPPLHKTLHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMTLLGGSVSVNG-------------------GFAYV 587
Cdd:PRK13643 12 QPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeikpvrkkvGVVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 588 AQQAWILNDSLRENILFG-KKYNEEKYnavlEACCLFPDIIELpYGDMTEIGERGA-NLSGGQRQRVSLARALYSERPIL 665
Cdd:PRK13643 92 FPESQLFEETVLKDVAFGpQNFGIPKE----KAEKIAAEKLEM-VGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 666 LLDDPLSAVD--ARVG-SRLFHSAIRpaaKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIAEHGTHTQLMEK 732
Cdd:PRK13643 167 VLDEPTAGLDpkARIEmMQLFESIHQ---SGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1167-1364 |
4.25e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSI-------------IIDGVNIAHIGLEDLR-SKLSVIPQ 1232
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1233 E------PVLFIG-----TVRSNLDPWDQYTDAQIWEALEKTHIKD---MVSQLPNSLhsevtdngenfSVGERQLLCVA 1298
Cdd:PRK10261 112 EpmtslnPVFTVGeqiaeSIRLHQGASREEAMVEAKRMLDQVRIPEaqtILSRYPHQL-----------SGGMRQRVMIA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1299 RALLRHSKILLLDEATAAIDTETDRLIQDTIR--SSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILE 1364
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
644-725 |
4.40e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.09 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRPAAK--GKTVIFVTHQLQYLPECDDVVLMKDGQIA 721
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP-SGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
....
gi 1207190976 722 EHGT 725
Cdd:PRK13633 224 MEGT 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1150-1362 |
5.17e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.10 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1150 ITFQDVEMRYRDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLED---LRSK 1226
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1227 LSVIPQEPVLFIG-TVRSNL-------DPWDQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVA 1298
Cdd:PRK10908 81 IGMIFQDHHLLMDrTVYDNVaipliiaGASGDDIRRRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1299 RALLRHSKILLLDEATAAIDtetDRLIQDTIR--SSFS--GCTTLVIAHRLNTVLGCN-RIMVLDQGQI 1362
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLD---DALSEGILRlfEEFNrvGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
644-729 |
5.44e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.86 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRPAAK--GKTVIFVTHQLQYLPE-CDDVVLMKDGQI 720
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIL-QLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRC 235
|
....*....
gi 1207190976 721 AEHGTHTQL 729
Cdd:PRK15134 236 VEQNRAATL 244
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1172-1364 |
5.71e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.54 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1172 FSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDG-----VNIAHIGLED----LRSKLSVIPQEPvlfigtvR 1242
Cdd:PRK11701 27 FDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAErrrlLRTEWGFVHQHP-------R 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1243 SNLDP----------------WDQYTD----AQIWeaLEKTHI-KDMVSQLPNSlhsevtdngenFSVGERQLLCVARAL 1301
Cdd:PRK11701 100 DGLRMqvsaggnigerlmavgARHYGDiratAGDW--LERVEIdAARIDDLPTT-----------FSGGMQQRLQIARNL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 1302 LRHSKILLLDEATAAIDTETDRLIQDTIRSSFS--GCTTLVIAHRLNTV-LGCNRIMVLDQGQILE 1364
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
644-729 |
5.84e-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: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVD-----------ARVGSRLfhsairpaakGKTVIFVTHQL----QYlpe 708
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqaqildllKDLQREL----------GMALLLITHDLgvvrRF--- 223
|
90 100
....*....|....*....|.
gi 1207190976 709 CDDVVLMKDGQIAEHGTHTQL 729
Cdd:COG4172 224 ADRVAVMRQGEIVEQGPTAEL 244
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
642-725 |
5.84e-06 |
|
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: 48.97 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDP---LSAVDARVGSRLFHSAirpAAKGKTVIFVTHQLQYLPE-CDDVVLMKD 717
Cdd:cd03219 142 GELSYGQQRRLEIARALATDPKLLLLDEPaagLNPEETEELAELIREL---RERGITVLLVEHDMDVVMSlADRVTVLDQ 218
|
....*...
gi 1207190976 718 GQIAEHGT 725
Cdd:cd03219 219 GRVIAEGT 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
560-722 |
6.13e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.39 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLG-------QMTLLGGSVSVNGGFAyvAQQAWI------LND----SLRENILFGKKY-------NEEKYNA 615
Cdd:PRK10762 43 KSTMMKVLTGiytrdagSILYLGKEVTFNGPKS--SQEAGIgiihqeLNLipqlTIAENIFLGREFvnrfgriDWKKMYA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 616 vlEACCLFPDIiELPYGDMTEIGErganLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRP-AAKGK 694
Cdd:PRK10762 121 --EADKLLARL-NLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLF-RVIRElKSQGR 192
|
170 180 190
....*....|....*....|....*....|
gi 1207190976 695 TVIFVTHQLQYLPE-CDDVVLMKDGQ-IAE 722
Cdd:PRK10762 193 GIVYISHRLKEIFEiCDDVTVFRDGQfIAE 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1288-1385 |
6.23e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 50.10 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1288 SVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIR---SSFsGCTTLVIAHRLNTVLGC-NRIMVLDQGQIL 1363
Cdd:PRK11432 138 SGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQF-NITSLYVTHDQSEAFAVsDTVIVMNKGKIM 216
|
90 100
....*....|....*....|....
gi 1207190976 1364 EFDTPSNLLTDENSRFHA--MMEA 1385
Cdd:PRK11432 217 QIGSPQELYRQPASRFMAsfMGDA 240
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
560-728 |
6.50e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.80 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSvsvngGFAYVAQQAWILNDSLRENILFGKKYNEEKYnaVLEACCLfpdiielpyGDMTEIGE 639
Cdd:COG2401 69 KSTLLRLLAGALKGTPVA-----GCVDVPDNQFGREASLIDAIGRKGDFKDAVE--LLNAVGL---------SDAVLWLR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 640 RGANLSGGQRQRVSLARALySERP-ILLLDDPLSAVD---ARVGSRLFHSAIRpaAKGKTVIFVTHQ------LQylpec 709
Cdd:COG2401 133 RFKELSTGQKFRFRLALLL-AERPkLLVIDEFCSHLDrqtAKRVARNLQKLAR--RAGITLVVATHHydviddLQ----- 204
|
170
....*....|....*....
gi 1207190976 710 DDVVLMKDgqiaeHGTHTQ 728
Cdd:COG2401 205 PDLLIFVG-----YGGVPE 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
645-725 |
6.88e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.72 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 645 SGGQRQRVSLARALYSeRPILLL-DDPLSAVDARVGS----------RLFHSAIrpaakgktvIFVTHQLQYLPE-CDDV 712
Cdd:PRK09473 163 SGGMRQRVMIAMALLC-RPKLLIaDEPTTALDVTVQAqimtllnelkREFNTAI---------IMITHDLGVVAGiCDKV 232
|
90
....*....|...
gi 1207190976 713 VLMKDGQIAEHGT 725
Cdd:PRK09473 233 LVMYAGRTMEYGN 245
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1178-1392 |
7.44e-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: 48.94 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1178 ETIGIVGRTGSGKSSLgvalfrlAELSRGSIIIDGVNIahiglEDLRSKLSVIPQE-PVLFIGTVRSNLDPWDQ--YTDA 1254
Cdd:cd03237 26 EVIGILGPNGIGKTTF-------IKMLAGVLKPDEGDI-----EIELDTVSYKPQYiKADYEGTVRDLLSSITKdfYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1255 QIwealeKTHIKDMVsQLPNSLHSEVTDngenFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIR--SS 1332
Cdd:cd03237 94 YF-----KTEIAKPL-QIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRrfAE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1333 FSGCTTLVIAHR--LNTVLGcNRIMVLDqGQILEF---DTPSNLLTDENsRFHAMMEAaeeTFSR 1392
Cdd:cd03237 164 NNEKTAFVVEHDiiMIDYLA-DRLIVFE-GEPSVNgvaNPPQSLRSGMN-RFLKNLDI---TFRR 222
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
865-1082 |
7.53e-06 |
|
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: 49.46 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 865 PHIQYYSRVYVLSMGAALFLKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAM 944
Cdd:cd18572 33 EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 945 QAEMLLQNVTLVL----FCLGVvgavfPWFL----FSIIPLgafLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQG 1016
Cdd:cd18572 113 NLNVFLRNLVQLVgglaFMFSL-----SWRLtllaFITVPV---IALITKVYGRYYRKLSKEIQDALAEANQVAEEALSN 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1017 LSTIYAYGRGADFIHRYQALLDTNQAC---QFLFSCAMRWLAVRLDlisisLITTVALLIV----LMHGHISP 1082
Cdd:cd18572 185 IRTVRSFATEEREARRYERALDKALKLsvrQALAYAGYVAVNTLLQ-----NGTQVLVLFYgghlVLSGRMSA 252
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
643-720 |
7.60e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGSRL-FHSAI-RPAAKGKTVIFVTHQlqyLPE----CDDVVLMK 716
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID--VGAKYeIYTIInELAAEGKGVIVISSE---LPEllgmCDRIYVMN 478
|
....
gi 1207190976 717 DGQI 720
Cdd:NF040905 479 EGRI 482
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
898-1119 |
7.72e-06 |
|
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: 49.48 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 898 RAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVgAVFPW----FLFS 973
Cdd:cd18557 66 RIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIIL-FILSWkltlVLLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 974 IIPLgafLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRY----QALLDTNQACQFLFSC 1049
Cdd:cd18557 145 VIPL---LLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYsealDRSYRLARKKALANAL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1050 AMrwlavrldlISISLITTVALLIVL-------MHGHISPayaGLALSYAVqLTGLFQFTVRLLSETEARFT----SVER 1118
Cdd:cd18557 222 FQ---------GITSLLIYLSLLLVLwyggylvLSGQLTV---GELTSFIL-YTIMVASSVGGLSSLLADIMkalgASER 288
|
.
gi 1207190976 1119 I 1119
Cdd:cd18557 289 V 289
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
593-725 |
8.26e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.02 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 593 ILNDSLRENILFGKKYNEEKYNAVLEACCLFPDIIELpYGDMteigerganLSGGQRQRVSLARALYSERPILLLDDPLS 672
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASY-YPHM---------LAPGQKQRLGLARALILRPKVIIADEALA 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 673 AVDARVGSRLFHSAIRPAAK-GKTVIFVTHQLQYLPECDDVVL-MKDGQIAEHGT 725
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLvMHQGEVVERGS 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1167-1366 |
8.37e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSI---LPEETI-GIVGRTGSGKSSLGVALFRLAELSRGSIIIDGvniaHIgLEDLRSKLSVIP---------QE 1233
Cdd:PRK11144 10 LGDLCLTVnltLPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG----RV-LFDAEKGICLPPekrrigyvfQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1234 PVLFIG-TVRSNLdpwdQY-----TDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKI 1307
Cdd:PRK11144 85 ARLFPHyKVRGNL----RYgmaksMVAQFDKIVALLGIEPLLDRYPGSL-----------SGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190976 1308 LLLDEATAAID--------TETDRLIQDT---IrssfsgcttLVIAHRLNTVLG-CNRIMVLDQGQILEFD 1366
Cdd:PRK11144 150 LLMDEPLASLDlprkrellPYLERLAREInipI---------LYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
560-722 |
8.63e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNG--------------GFAYVAQQ----AWILNDSLRENILFGKKYNEEKYNAvleACC 621
Cdd:PRK09700 302 RTELMNCLFGVDKRAGGEIRLNGkdisprspldavkkGMAYITESrrdnGFFPNFSIAQNMAISRSLKDGGYKG---AMG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 622 LFPDIIELPYGD---------MTEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAK 692
Cdd:PRK09700 379 LFHEVDEQRTAEnqrellalkCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD 458
|
170 180 190
....*....|....*....|....*....|.
gi 1207190976 693 GKTVIFVTHQL-QYLPECDDVVLMKDGQIAE 722
Cdd:PRK09700 459 GKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1153-1362 |
8.69e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.03 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1153 QDVEMRYRDGLPlVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIGLEDLR-SKLSVIP 1231
Cdd:COG3845 261 ENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIP 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1232 QEPvLFIGTVrSNLDPWD-----QYTDAQI-------WEALEKtHIKDMVSQL---PNSLHSEVtdngENFSVGERQLLC 1296
Cdd:COG3845 340 EDR-LGRGLV-PDMSVAEnlilgRYRRPPFsrggfldRKAIRA-FAEELIEEFdvrTPGPDTPA----RSLSGGNQQKVI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 1297 VARALLRHSKILL-------LDE-ATAAIdteTDRLIQ--DtirssfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQI 1362
Cdd:COG3845 413 LARELSRDPKLLIaaqptrgLDVgAIEFI---HQRLLElrD------AGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1140-1344 |
9.13e-06 |
|
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: 50.13 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1140 SSSSWPAEGQITFQDVEMRYrDGLPLVLKN-------LCFSILPEETIGIVGRTGSGKSSLgvalFR-LAEL--SRGSII 1209
Cdd:TIGR00954 435 NSNLVPGRGIVEYQDNGIKF-ENIPLVTPNgdvliesLSFEVPSGNNLLICGPNGCGKSSL----FRiLGELwpVYGGRL 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1210 IdgvniahiglEDLRSKLSVIPQEPVLFIGTVR-------SNLDPWDQ-YTDAQIWEALEKTHIKDMVSQlpNSLHSEVT 1281
Cdd:TIGR00954 510 T----------KPAKGKLFYVPQRPYMTLGTLRdqiiypdSSEDMKRRgLSDKDLEQILDNVQLTHILER--EGGWSAVQ 577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1282 DNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRSsfSGCTTLVIAHR 1344
Cdd:TIGR00954 578 DWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
898-1119 |
9.67e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 49.05 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 898 RAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDvRLAMQAemLLQNVTLVLFCLGVVGAVFpWF-----LF 972
Cdd:cd18564 84 RVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQ-DLLVSG--VLPLLTNLLTLVGMLGVMF-WLdwqlaLI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 973 SIIPLGAFLFIVNRISRvLIRELKRLENISQSPFTSHITSSLQGLSTIYAYGRGADFIHRYQALldtnqacqflfscAMR 1052
Cdd:cd18564 160 ALAVAPLLLLAARRFSR-RIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARE-------------NRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1053 WLAVRLDLI--------SISLITTVALLIVL-------MHGHISPayaGLALSYAVQLTGLFQfTVRLLSETEARFT--- 1114
Cdd:cd18564 226 SLRAGLRAArlqallspVVDVLVAVGTALVLwfgawlvLAGRLTP---GDLLVFLAYLKNLYK-PVRDLAKLTGRIAkas 301
|
....*.
gi 1207190976 1115 -SVERI 1119
Cdd:cd18564 302 aSAERV 307
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
531-701 |
1.17e-05 |
|
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: 47.79 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 531 PPLHKTLHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMTLLGGSVSVNG------------------GFAYvaQQAW 592
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrkiGVVF--QDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 593 ILND-SLRENILF-----GKKYNE--EKYNAVLEACCLFPDIIELPygdmteigergANLSGGQRQRVSLARALYSERPI 664
Cdd:cd03292 89 LLPDrNVYENVAFalevtGVPPREirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207190976 665 LLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTH 701
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-736 |
1.21e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.49 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGK-TVIFVTHQLQYLPECDDVVLM------ 715
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFfkgnen 229
|
90 100
....*....|....*....|....*.
gi 1207190976 716 KDGQIAEHGTHTQLM-----EKGRDY 736
Cdd:PRK14258 230 RIGQLVEFGLTKKIFnsphdSRTREY 255
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
642-731 |
1.51e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGS-----RLFHSAirpAAKGKTVIFVTHQlqyLPE----CDDV 712
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID--VGAkyeiyKLINQL---VQQGVAIIVISSE---LPEvlglSDRV 475
|
90 100
....*....|....*....|....
gi 1207190976 713 VLMKDGQIA-----EHGTHTQLME 731
Cdd:PRK13549 476 LVMHEGKLKgdlinHNLTQEQVME 499
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
531-733 |
1.60e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.24 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 531 PPLHKTLHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMTLLGGSVSVNG-------------------GFAYVAQQA 591
Cdd:PRK13646 17 PYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkriGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 592 WILNDSLRENILFGKK--------YNEEKYNAVLEACclFP-DIIEL-PYgdmteigergaNLSGGQRQRVSLARALYSE 661
Cdd:PRK13646 97 QLFEDTVEREIIFGPKnfkmnldeVKNYAHRLLMDLG--FSrDVMSQsPF-----------QMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 662 RPILLLDDPLSAVDARvgSRlfHSAIRPAAK-----GKTVIFVTHQL----QYlpeCDDVVLMKDGQIAEHGTHTQLMEK 732
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQ--SK--RQVMRLLKSlqtdeNKTIILVSHDMnevaRY---ADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 1207190976 733 G 733
Cdd:PRK13646 237 K 237
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
643-731 |
1.75e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 48.25 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVD--------ARVgSRLFHSairpaaKGKTVIFVTHQLQYLPE-CDDVV 713
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqvdvlALV-HRLSQE------RGLTVIAVLHDINMAARyCDYLV 219
|
90
....*....|....*...
gi 1207190976 714 LMKDGQIAEHGTHTQLME 731
Cdd:PRK10575 220 ALRGGEMIAQGTPAELMR 237
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
643-725 |
1.78e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.06 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRL--FHSAIRPAAKgKTVIFVTHQLQYLPECDDVVLMKDGQI 720
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIkkIMVDLRKTRK-KTLISITHDMDEAILADKVIVFSEGKL 220
|
....*
gi 1207190976 721 AEHGT 725
Cdd:PRK13632 221 IAQGK 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
560-724 |
1.95e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.19 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGGFAYVAQQAWILN---------------DSLRENILFG-------KKYNEEKYNAVL 617
Cdd:PRK13647 44 KSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvglvfqdpddqvfsSTVWDDVAFGpvnmgldKDEVERRVEEAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 618 EACclfpdiielpygDMTEIGERGA-NLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTV 696
Cdd:PRK13647 124 KAV------------RMWDFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTV 191
|
170 180
....*....|....*....|....*....
gi 1207190976 697 IFVTHQLQYLPE-CDDVVLMKDGQIAEHG 724
Cdd:PRK13647 192 IVATHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
644-726 |
1.96e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 48.26 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHqlqYLPE----CDDVVLMKDG- 718
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH---FMEEaerlCDRLCVIEEGr 215
|
....*...
gi 1207190976 719 QIAEHGTH 726
Cdd:PRK13537 216 KIAEGAPH 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1167-1361 |
1.98e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIA-HIGLEDLRSKLSVIPQEPVLFIG-TVRSN 1244
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQrSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1245 L------------DPWDQYTDAQ-IWEALE-KTHIKDMVSQLpnslhsevtdngenfSVGERQLLCVARALLRHSKILLL 1310
Cdd:PRK10982 94 MwlgryptkgmfvDQDKMYRDTKaIFDELDiDIDPRAKVATL---------------SVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1311 DEATAAI-DTETDRLIQDTIRSSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQ 1361
Cdd:PRK10982 159 DEPTSSLtEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1138-1364 |
2.05e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.81 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1138 PTSSSSWPaegQITFQDVEMRYRDGlPLVLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAH 1217
Cdd:PRK10522 314 PQAFPDWQ---TLELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1218 IGLEDLRSKLSVIPQEPVLFIGTvrsnLDPWDQYTDAQIWEA-LEKTHIKDMVSQLPNslhsEVTDNgeNFSVGERQLLC 1296
Cdd:PRK10522 390 EQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHKLELEDG----RISNL--KLSKGQKKRLA 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 1297 VARALLRHSKILLLDEATAAIDTETDR--------LIQDTirssfsGCTTLVIAHRLNTVLGCNRIMVLDQGQILE 1364
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRRefyqvllpLLQEM------GKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
642-776 |
3.00e-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: 48.39 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRpaAKGkTVIFVTHQLQYLpecDDVVlmkdGQIA 721
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE--YPG-TVVAVTHDRYFL---DNVA----GWIL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 722 E---------HGTHTQLMEK--------GRDYAALFNSVQQE-NLVRKNLK---NKEKA-----------EKESSPQTLH 769
Cdd:TIGR03719 230 EldrgrgipwEGNYSSWLEQkqkrleqeEKEESARQKTLKRElEWVRQSPKgrqAKSKArlaryeellsqEFQKRNETAE 309
|
....*..
gi 1207190976 770 VSNPPKP 776
Cdd:TIGR03719 310 IYIPPGP 316
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1166-1363 |
3.08e-05 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 46.94 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGvNIAHIGLEDLRSKLSVI------------PQE 1233
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVfgqktqlwwdlpVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1234 PVLFIGTVRsNLDPwDQYTD--AQIWEALEKTHIkdmvsqlpnsLHSEVtdngENFSVGERQLLCVARALLRHSKILLLD 1311
Cdd:cd03267 115 SFYLLAAIY-DLPP-ARFKKrlDELSELLDLEEL----------LDTPV----RQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1312 EATAAIDTETDRLIQDTIR--SSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQIL 1363
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKeyNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
584-725 |
3.42e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.35 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 584 FAYVAQQawILNDSLRENILFGKK----YNEEKYNAVLEACclfpDIIELPYGDMTEigERGANLSGGQRQRVSLARALY 659
Cdd:PRK13637 89 FQYPEYQ--LFEETIEKDIAFGPInlglSEEEIENRVKRAM----NIVGLDYEDYKD--KSPFELSGGQKRRVAIAGVVA 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 660 SERPILLLDDPLSAVDARVGSRLFhSAIRPAAKGK--TVIFVTHQLQYLPE-CDDVVLMKDGQIAEHGT 725
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEIL-NKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
638-725 |
4.22e-05 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 46.96 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 638 GERGANLSGGQRQRVSLARALYSERPILLLDDP---LSAVDARVGSRLFHSaIRpAAKGKTVIFVTH------QLqylpe 708
Cdd:COG0411 147 DEPAGNLSYGQQRRLEIARALATEPKLLLLDEPaagLNPEETEELAELIRR-LR-DERGITILLIEHdmdlvmGL----- 219
|
90
....*....|....*...
gi 1207190976 709 CDDVVLMKDGQ-IAEhGT 725
Cdd:COG0411 220 ADRIVVLDFGRvIAE-GT 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1168-1375 |
4.22e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1168 KNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIA-HIGLEDLRSKLSVIPQ---EPVLFIG-TVR 1242
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1243 SNLDPWDQYTDAQ-------IWEALEKTHIKDMVSQLPNSLHSeVTDNGENFSVGERQLLCVARALLRHSKILLLDEATA 1315
Cdd:PRK09700 360 QNMAISRSLKDGGykgamglFHEVDEQRTAENQRELLALKCHS-VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 1316 AIDTETDRLIQDTIRS-SFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLTDE 1375
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITvCDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
903-1082 |
4.68e-05 |
|
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: 47.02 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 903 LHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGVVGAVFPWF-LFSIIPLGAFL 981
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLtLIALLPLPLLA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 982 FIVNRISRVLIRELKRleniSQSPF---TSHITSSLQGLSTIYAYGRGADFIHRYQALLDTNqacqflFSCAMRwlAVRL 1058
Cdd:cd18541 155 LLVYRLGKKIHKRFRK----VQEAFsdlSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEY------VEKNLR--LARV 222
|
170 180 190
....*....|....*....|....*....|....
gi 1207190976 1059 D---LISISLITTVALLIVL-------MHGHISP 1082
Cdd:cd18541 223 DalfFPLIGLLIGLSFLIVLwyggrlvIRGTITL 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
644-729 |
5.22e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHsAIRPAAKGKT--VIFVTHQLQYLPE-CDDVVLMKDGQI 720
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEA 247
|
....*....
gi 1207190976 721 AEHGTHTQL 729
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1173-1358 |
6.43e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1173 SILPEETIGIVGRTGSGKSSLgvalfrlAELSRGSIIIDGVNIahigleDLRSKLSVIPQEPVLFI-GTVRSNLDPW--D 1249
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTF-------AKILAGVLKPDEGEV------DEDLKISYKPQYISPDYdGTVEEFLRSAntD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1250 QYTDAQIWEALekthIKDMvsQLPNSLHSEVTDngenFSVGERQLLCVARALLRHSKILLLDEATAAIDTE----TDRLI 1325
Cdd:COG1245 429 DFGSSYYKTEI----IKPL--GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAI 498
|
170 180 190
....*....|....*....|....*....|....
gi 1207190976 1326 QDTIRSsfSGCTTLVIAHRLNTV-LGCNRIMVLD 1358
Cdd:COG1245 499 RRFAEN--RGKTAMVVDHDIYLIdYISDRLMVFE 530
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1166-1349 |
7.77e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 45.88 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIID-GVNIAHIgledlRSKLSVIPQEPVlfigTVRSN 1244
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgKLRIGYV-----PQKLYLDTTLPL----TVNRF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1245 LDPWDQYTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRL 1324
Cdd:PRK09544 90 LRLRPGTKKEDILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|....*...
gi 1207190976 1325 IQDTI---RSSFsGCTTLVIAHRLNTVL 1349
Cdd:PRK09544 159 LYDLIdqlRREL-DCAVLMVSHDLHLVM 185
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1286-1375 |
8.12e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 45.75 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1286 NFSVGERQLLCVARALLRHSKILLLDEATAAID-TETDRLIQ--DTIRSSFsGCTTLVIAHRLNTVLG-CNRIMVLDQGQ 1361
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGT 231
|
90
....*....|....
gi 1207190976 1362 ILEFDTPSNLLTDE 1375
Cdd:PRK11300 232 PLANGTPEEIRNNP 245
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
560-702 |
8.58e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 47.05 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSV--NGGFAYVAQQAWILNDSLRENILFGKKYNEEKYNAVLEAcclfpDIIE-LPYGDMTE 636
Cdd:TIGR00954 491 KSSLFRILGELWPVYGGRLTKpaKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDK-----DLEQiLDNVQLTH 565
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 637 IGERGAN----------LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRpaaKGKTVIFVTHQ 702
Cdd:TIGR00954 566 ILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE---FGITLFSVSHR 638
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
873-1119 |
8.64e-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: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 873 VYVLSMGAA----LFLKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEM 948
Cdd:cd18563 44 LLVLGLAGAyvlsALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 949 LLQNVTLVLFCLGVVGAVFPWF-LFSIIP----LGAFLFIVNRISRVLIRELKRLENIsqspfTSHITSSLQGLSTIYAY 1023
Cdd:cd18563 124 FLTNILMIIGIGVVLFSLNWKLaLLVLIPvplvVWGSYFFWKKIRRLFHRQWRRWSRL-----NSVLNDTLPGIRVVKAF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1024 GRGADFIHRY----QALLDTNqacqflfscamrwlaVRLDLIS------ISLITTVALLIV-------LMHGHISP---- 1082
Cdd:cd18563 199 GQEKREIKRFdeanQELLDAN---------------IRAEKLWatffplLTFLTSLGTLIVwyfggrqVLSGTMTLgtlv 263
|
250 260 270
....*....|....*....|....*....|....*..
gi 1207190976 1083 AYaglaLSYAVQLTGLFQFTVRLLSETEARFTSVERI 1119
Cdd:cd18563 264 AF----LSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
644-734 |
9.72e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.89 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHqlqylpecddvvLMKDgqIAEH 723
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH------------LMDD--VANY 211
|
90
....*....|.
gi 1207190976 724 GTHTQLMEKGR 734
Cdd:PRK13649 212 ADFVYVLEKGK 222
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
645-790 |
1.09e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 46.24 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 645 SGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSR---LFHSAIRPAakGKTVIFVTHQLQYLPECDDVVL-MKDGQI 720
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQvvnLLQQLQREM--GLSLIFIAHDLAVVKHISDRVLvMYLGHA 240
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 721 AEHGThtqlmekgrdYAALFNSVQQenlvrknlknkekaekessPQT--LHVSNP-PKPDTESKKTDQLMQAE 790
Cdd:PRK15079 241 VELGT----------YDEVYHNPLH-------------------PYTkaLMSAVPiPDPDLERNKTIQLLEGE 284
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1174-1358 |
1.19e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.34 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1174 ILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIiidgvniahigleDLRSKLSVIPQepvlFI-----GTVRSNL-DP 1247
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELKISYKPQ----YIkpdydGTVEDLLrSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1248 WDQYTDAQIWEALekthIKDMvsQLPNSLHSEVTDngenFSVGERQLLCVARALLRHSKILLLDEATAAIDTE----TDR 1323
Cdd:PRK13409 425 TDDLGSSYYKSEI----IKPL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAK 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207190976 1324 LIQDTIRSsfSGCTTLVIAHRLNTV-LGCNRIMVLD 1358
Cdd:PRK13409 495 AIRRIAEE--REATALVVDHDIYMIdYISDRLMVFE 528
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
560-719 |
1.21e-04 |
|
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: 43.59 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG--FAYVAQqawilndslrenilfgkkyneekynavleacclfpdiielpygdmtei 637
Cdd:cd03221 39 KSTLLKLIAGELEPDEGIVTWGSTvkIGYFEQ------------------------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 638 gerganLSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGSRLF-HSAIRpaAKGKTVIFVTHQLQYLPE-CDDVVLM 715
Cdd:cd03221 71 ------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD--LESIEAlEEALK--EYPGTVILVSHDRYFLDQvATKIIEL 140
|
....
gi 1207190976 716 KDGQ 719
Cdd:cd03221 141 EDGK 144
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
873-1082 |
1.27e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 45.56 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 873 VYVLSMGAALFLKTirglVFVKCTVRAA-SVLHD---KLFKTLLLSPMRFFDTTPLGRILNRFSKDMDevdvrlAMQAem 948
Cdd:cd18546 44 AYLAVVLAGWVAQR----AQTRLTGRTGeRLLYDlrlRVFAHLQRLSLDFHERETSGRIMTRMTSDID------ALSE-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 949 LLQN-----VTLVLFCLGVVGAVFpWF--------LFSIIPLGAFLFIVNRISRVLIRELKrlENISQSpfTSHITSSLQ 1015
Cdd:cd18546 112 LLQTglvqlVVSLLTLVGIAVVLL-VLdprlalvaLAALPPLALATRWFRRRSSRAYRRAR--ERIAAV--NADLQETLA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1016 GLSTIYAYGRGADFIHRYQAL----LDTNQACQFLFscAMRWLAVRLdlisISLITTVALLIV----LMHGHISP 1082
Cdd:cd18546 187 GIRVVQAFRRERRNAERFAELsddyRDARLRAQRLV--AIYFPGVEL----LGNLATAAVLLVgawrVAAGTLTV 255
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
882-1020 |
1.33e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 45.58 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 882 LFLKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSkdmDEVDVR--LAMQAEMLLQNVTLVLFC 959
Cdd:cd18555 56 GLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRAN---SNVYIRqiLSNQVISLIIDLLLLVIY 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 960 LGVVgAVFPWFLFSI-IPLGAFLFIVNRISRVLIRELKRLENISQSPFTSHITSSLQGLSTI 1020
Cdd:cd18555 133 LIYM-LYYSPLLTLIvLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETI 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
643-732 |
1.35e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.32 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPlSA---VDARVgsrLFHSAIRPAA--KGKTVIFVTHQLQYLPECDDVVLMKD 717
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEP-SAhldVEQRL---AVAKAIRRFAenRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
90
....*....|....*
gi 1207190976 718 GQIAEHGTHTQLMEK 732
Cdd:COG1245 531 GEPGVHGHASGPMDM 545
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
642-754 |
1.67e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.08 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGS---RLFHSairpaAKGK---TVIFVTHQLQYLPECDDVVLM 715
Cdd:PRK13642 139 ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQeimRVIHE-----IKEKyqlTVLSITHDLDEAASSDRILVM 213
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207190976 716 KDGQIAEHGTHTQLMEKGRDYAALFNSVQQENLVRKNLK 754
Cdd:PRK13642 214 KAGEIIKEAAPSELFATSEDMVEIGLDVPFSSNLMKDLR 252
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
560-717 |
1.70e-04 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 44.63 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGGFAYVAQQAWILNDSLreniLFGKKyNEEKYN-AVLEACCLFPDIIELPYG------ 632
Cdd:cd03267 60 KTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV----VFGQK-TQLWWDlPVIDSFYLLAAIYDLPPArfkkrl 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 633 ----DMTEIGE------RgaNLSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRPAAK--GKTVIFVT 700
Cdd:cd03267 135 delsELLDLEElldtpvR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV-VAQENIRNFLKEYNRerGTTVLLTS 211
|
170
....*....|....*..
gi 1207190976 701 HQLQYLPECDDVVLMKD 717
Cdd:cd03267 212 HYMKDIEALARRVLVID 228
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
856-1076 |
1.71e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 45.52 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 856 AESDSMRLNPHIQYYSRVYVLSMGAALFLKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFD----TTplGRILNRF 931
Cdd:cd18578 40 SLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpenST--GALTSRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 932 SKDMDEV----DVRLAmqaeMLLQNVTLVLFCLgVVGAVFPWFL----FSIIPLGAFLFIVNriSRVLIR-ELKRLENIS 1002
Cdd:cd18578 118 STDASDVrglvGDRLG----LILQAIVTLVAGL-IIAFVYGWKLalvgLATVPLLLLAGYLR--MRLLSGfEEKNKKAYE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1003 QSpfTSHITSSLQGLSTIYAYGRGADFIHRYQALLDT------------------NQACQFLFSCAMRWLAVRldLISIS 1064
Cdd:cd18578 191 ES--SKIASEAVSNIRTVASLTLEDYFLEKYEEALEEplkkglrralisglgfglSQSLTFFAYALAFWYGGR--LVANG 266
|
250
....*....|..
gi 1207190976 1065 LITTVALLIVLM 1076
Cdd:cd18578 267 EYTFEQFFIVFM 278
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
595-702 |
1.74e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.17 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 595 NDSLRENILFGKKYNEEKYnAVLEACCLFP--DIIELPYGdmteigergaNLSGGQRQRVSLARALYSERPILLLDDPLS 672
Cdd:PRK13540 88 YLTLRENCLYDIHFSPGAV-GITELCRLFSleHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
90 100 110
....*....|....*....|....*....|
gi 1207190976 673 AVDARVGSRLFHSAIRPAAKGKTVIFVTHQ 702
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
639-719 |
1.92e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 639 ERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPE-CDDVVLMKD 717
Cdd:PRK10982 130 AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRD 209
|
..
gi 1207190976 718 GQ 719
Cdd:PRK10982 210 GQ 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
643-730 |
1.98e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGSR--LFHSAIRPAAKGKTVIFVTHQlqyLPEC----DDVVLMK 716
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD--VGAKkeIYQLINQFKAEGLSIILVSSE---MPEVlgmsDRILVMH 469
|
90
....*....|....*....
gi 1207190976 717 DGQI-----AEHGTHTQLM 730
Cdd:PRK10762 470 EGRIsgeftREQATQEKLM 488
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
635-721 |
2.10e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 635 TEIGergaNLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQL-QYLPECDDVV 713
Cdd:PRK10982 387 TQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRIL 462
|
....*...
gi 1207190976 714 LMKDGQIA 721
Cdd:PRK10982 463 VMSNGLVA 470
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
645-724 |
2.35e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.53 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 645 SGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFhSAIRP--AAKGKTVIFVTHQL---QYLPecDDVVLMKDGQ 719
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLL-DLLRGlvRELGLAVVIVTHDLavaRLLA--HRLLVMKQGR 229
|
....*
gi 1207190976 720 IAEHG 724
Cdd:PRK11701 230 VVESG 234
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
644-730 |
2.53e-04 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 44.45 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERP-------ILLLDDPLSAVDA-------RVGSRLfhsairpAAKGKTVIFVTHQLQY-LPE 708
Cdd:COG4138 127 LSGGEWQRVRLAAVLLQVWPtinpegqLLLLDEPMNSLDVaqqaaldRLLREL-------CQQGITVVMSSHDLNHtLRH 199
|
90 100
....*....|....*....|..
gi 1207190976 709 CDDVVLMKDGQIAEHGTHTQLM 730
Cdd:COG4138 200 ADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
643-725 |
2.70e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 44.32 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGSRLFHS-AIRPAA--KGKTVIFVTHQLQYLPECDDVVLMKDGQ 719
Cdd:cd03237 115 ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLMASkVIRRFAenNEKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
....*.
gi 1207190976 720 IAEHGT 725
Cdd:cd03237 193 PSVNGV 198
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1178-1373 |
3.00e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.79 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1178 ETIGIVGRTGSGKSSLGVALFRLAE----LSRGSIIIDGVNIAHIGLEDLRS----KLSVIPQEPvlfigtvRSNLDP-- 1247
Cdd:PRK15093 34 EIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERRKlvghNVSMIFQEP-------QSCLDPse 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1248 ------------------WDQYTDAQIWEALEKTH---IKDMvSQLPNSLHSEVTDngenfsvGERQLLCVARALLRHSK 1306
Cdd:PRK15093 107 rvgrqlmqnipgwtykgrWWQRFGWRKRRAIELLHrvgIKDH-KDAMRSFPYELTE-------GECQKVMIAIALANQPR 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190976 1307 ILLLDEATAAIDTETD--------RLIQDtirssfSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEFDTPSNLLT 1373
Cdd:PRK15093 179 LLIADEPTNAMEPTTQaqifrlltRLNQN------NNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
643-703 |
3.42e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 3.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGSRLFHS-AIRPAAKGKTVIFVTHQL 703
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQRLNVArLIRELAEGKYVLVVEHDL 271
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
535-730 |
3.54e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 43.71 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 535 KTLHRIDLCIQKGSLVGVCGGVGSGKSSLLSALLGQMTLLGGSVSVNGGFAYVAQQAWILNDSL---------------R 599
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVaivpegrrvfsrmtvE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 600 ENILFGKKYNE-EKYNAVLEACC-LFPDIIElpygdmtEIGERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDAR 677
Cdd:PRK11614 99 ENLAMGGFFAErDQFQERIKWVYeLFPRLHE-------RRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 678 VGSRLFHSAIRPAAKGKTVIFVTHQL-QYLPECDDVVLMKDGQIAEHGTHTQLM 730
Cdd:PRK11614 172 IIQQIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
644-721 |
3.71e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGSRL-FHSAIRP-AAKGKTVIFVTHQLQYLPECDDVVL-MKDGQI 720
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD--VSARNdIYQLIRSiAAQNVAVLFISSDLEEIEQMADRVLvMHQGEI 481
|
.
gi 1207190976 721 A 721
Cdd:PRK15439 482 S 482
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
643-720 |
4.09e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 43.92 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGK-TVIFVTHQLQYLPECDD-VVLMKDGQI 720
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNrLIMMHEGRI 227
|
|
| DUF87 |
pfam01935 |
Helicase HerA, central domain; This entry represents the central domain found in archaeal ... |
1180-1327 |
4.33e-04 |
|
Helicase HerA, central domain; This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.
Pssm-ID: 376671 [Multi-domain] Cd Length: 220 Bit Score: 43.51 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1180 IGIVGRTGSGKSSL-GVALFRLAELSRGSIII-----DGVNIAHIGLEDlrsKLSVIPQEPVLFIGTvrSNLDPWD---- 1249
Cdd:pfam01935 26 FAILGSTGSGKSNTvAVLLEELLEKKGATVLIfdphgEYGTLFRDLGAE---NVNVITPDPELKINP--WLLSPEDladl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1250 -------QYTD-----AQIWEALEKTHIKDMVSQ--LPNSLHSEVTDNGENFSVGERqllcVARALLRHSKILLLDEATA 1315
Cdd:pfam01935 101 leelnlpNAEVqrsilEEALDQLKSEELGKLSIDelIEKILEELLTEAAELNKLSND----AIRRVLDKLERLLRSGGLI 176
|
170
....*....|..
gi 1207190976 1316 AIDTETDRLIQD 1327
Cdd:pfam01935 177 LTSTDIIKLILD 188
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
563-720 |
4.45e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.63 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 563 LLSALLGQMTLLGGSVSVNG--------------GFAYVAQ----QAWILNDSLRENILFGKKYNEE-------KYNAVL 617
Cdd:COG3845 300 LAEALAGLRPPASGSIRLDGeditglsprerrrlGVAYIPEdrlgRGLVPDMSVAENLILGRYRRPPfsrggflDRKAIR 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 618 EACClfpDIIE----LPYGDMTEIGergaNLSGGQRQRVSLARALYSERPILLLDDPLSAVDarVGSRLF-HSAIRPAA- 691
Cdd:COG3845 380 AFAE---ELIEefdvRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD--VGAIEFiHQRLLELRd 450
|
170 180 190
....*....|....*....|....*....|
gi 1207190976 692 KGKTVIFVTHQLQYLPE-CDDVVLMKDGQI 720
Cdd:COG3845 451 AGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1167-1364 |
5.13e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSL-----GVALFRLAElsrGSIIIDGvNIAHIGleDLRSK----LSVIPQE---- 1233
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLmkvlsGVYPHGSYE---GEILFDG-EVCRFK--DIRDSealgIVIIHQElali 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1234 PVL------FIG--TVRSNLDPWDQyTDAQIWEALEKTHIKDmvsqLPNSLhseVTDNGenfsVGERQLLCVARALLRHS 1305
Cdd:NF040905 91 PYLsiaeniFLGneRAKRGVIDWNE-TNRRARELLAKVGLDE----SPDTL---VTDIG----VGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 1306 KILLLDEATAAI-DTETDRLIqDTIRsSF--SGCTTLVIAHRLNTVLG-CNRIMVLDQGQILE 1364
Cdd:NF040905 159 KLLILDEPTAALnEEDSAALL-DLLL-ELkaQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1166-1329 |
5.83e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.55 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1166 VLKNLCFSILPEETIGIVGRTGSGKSSLGVALFRLAELSRGSIIIDGVNIAHIgledlrsklsvipQEPVL-FIG----- 1239
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------------AKPYCtYIGhnlgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1240 ----TVRSNLDPWDQYTD--AQIWEALEKTHIKDMVSQLPNSLHSevtdngenfsvGERQLLCVARALLRHSKILLLDEA 1313
Cdd:PRK13541 82 klemTVFENLKFWSEIYNsaETLYAAIHYFKLHDLLDEKCYSLSS-----------GMQKIVAIARLIACQSDLWLLDEV 150
|
170
....*....|....*.
gi 1207190976 1314 TAAIDTETDRLIQDTI 1329
Cdd:PRK13541 151 ETNLSKENRDLLNNLI 166
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
643-728 |
5.93e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.17 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDARvgSRLFHS-AIRPAAK--GKTVIFVTHQLQYLPECDDVVLMKDGQ 719
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE--QRLNAArAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
....*....
gi 1207190976 720 IAEHGTHTQ 728
Cdd:cd03222 149 PGVYGIASQ 157
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
560-732 |
6.44e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 43.30 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 560 KSSLLSALLGQMTLLGGSVSVNGG-FAYVAQQawILNdsLRENI--LFGKKYNEEKYNAVLEACCLFPDIIELPygdMTE 636
Cdd:PRK13636 45 KSTLFQNLNGILKPSSGRILFDGKpIDYSRKG--LMK--LRESVgmVFQDPDNQLFSASVYQDVSFGAVNLKLP---EDE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 637 IGERGAN-----------------LSGGQRQRVSLARALYSERPILLLDDPLSAVDArVGSRLFHSAIRPAAK--GKTVI 697
Cdd:PRK13636 118 VRKRVDNalkrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP-MGVSEIMKLLVEMQKelGLTII 196
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207190976 698 FVTHQLQYLP-ECDDVVLMKDGQIAEHGTHTQLMEK 732
Cdd:PRK13636 197 IATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
887-1082 |
6.83e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 43.24 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 887 IRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEV-DVRLAMQAEMLLQNVTLV-----LFCL 960
Cdd:cd18576 55 FRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIqDTLTTTLAEFLRQILTLIggvvlLFFI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 961 -----GVVGAVFPWFLFSIIPLGAFLfivNRISRvlirelKRLENISQSpfTSHITSSLQGLSTIYAYGRGADFIHRYQA 1035
Cdd:cd18576 135 swkltLLMLATVPVVVLVAVLFGRRI---RKLSK------KVQDELAEA--NTIVEETLQGIRVVKAFTREDYEIERYRK 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207190976 1036 LLDTnqacqfLFSCAMRWLAVRLDLIS-ISLITTVALLIVL-------MHGHISP 1082
Cdd:cd18576 204 ALER------VVKLALKRARIRALFSSfIIFLLFGAIVAVLwyggrlvLAGELTA 252
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
643-719 |
9.06e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 9.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQ 719
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
626-719 |
9.38e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.54 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 626 IIELPYGDMTeIGERGANLSGGQRQRVSLARALYSERP--ILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQL 703
Cdd:cd03238 71 LIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL 149
|
90
....*....|....*.
gi 1207190976 704 QYLPECDDVVLMKDGQ 719
Cdd:cd03238 150 DVLSSADWIIDFGPGS 165
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1240-1371 |
9.76e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1240 TVRSNLD--------PWDQyTDAQIWEALEKTHIKDMVSQLPNSLhsevtdngenfSVGERQLLCVARALLRHSKILLLD 1311
Cdd:NF033858 355 TVRQNLElharlfhlPAAE-IAARVAEMLERFDLADVADALPDSL-----------PLGIRQRLSLAVAVIHKPELLILD 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207190976 1312 EATAAIDTET-DRLIQDTIR-SSFSGCTTLVIAHRLNTVLGCNRIMVLDQGQILEFDTPSNL 1371
Cdd:NF033858 423 EPTSGVDPVArDMFWRLLIElSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAAL 484
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
638-732 |
1.02e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 638 GERGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVThqlQYLPECD----DVV 713
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT---QYMEEAEqlahELT 215
|
90
....*....|....*....
gi 1207190976 714 LMKDGQIAEHGTHTQLMEK 732
Cdd:NF000106 216 VIDRGRVIADGKVDELKTK 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
640-724 |
1.06e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 41.86 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 640 RGanLSGGQRQRVSLARALYSERPILLLDDPLSAVDArvgSRLFH--SAIRPAAKG-KTVIFVThQLQYLPEC----DDV 712
Cdd:cd03233 117 RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDS---STALEilKCIRTMADVlKTTTFVS-LYQASDEIydlfDKV 190
|
90
....*....|..
gi 1207190976 713 VLMKDGQIAEHG 724
Cdd:cd03233 191 LVLYEGRQIYYG 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
642-731 |
1.11e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 43.27 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQL-QYLPECDDVVLMKDGQI 720
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKL 481
|
90
....*....|....*.
gi 1207190976 721 A----EHG-THTQLME 731
Cdd:TIGR02633 482 KgdfvNHAlTQEQVLA 497
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
641-733 |
1.16e-03 |
|
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: 41.74 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 641 GANLSGGQRQRVSLARALYSERPILLLDDPLSAVD-------ARVGSRLfhsairpAAKGKTVIFVTHQ---LQYLPEcD 710
Cdd:cd03217 102 NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidalrlvAEVINKL-------REEGKSVLIITHYqrlLDYIKP-D 173
|
90 100
....*....|....*....|....*.
gi 1207190976 711 DVVLMKDGQIAEHGTHT---QLMEKG 733
Cdd:cd03217 174 RVHVLYDGRIVKSGDKElalEIEKKG 199
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
644-718 |
1.37e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 1.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQ--LQYLPECDDVVLMKDG 718
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRG 1096
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
642-676 |
1.61e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.61e-03
10 20 30
....*....|....*....|....*....|....*
gi 1207190976 642 ANLSGGQRQRVSLARALYSERPILLLDDPLSAVDA 676
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
644-703 |
1.63e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.78 E-value: 1.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGS---RLFHSAIRpaaKGKTVIFVTHQL 703
Cdd:PRK10908 138 LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEgilRLFEEFNR---VGVTVLMATHDI 197
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
645-735 |
1.66e-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: 43.08 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 645 SGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQIAEH 723
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCL 2151
|
90
....*....|..
gi 1207190976 724 GTHTQLMEKGRD 735
Cdd:TIGR01257 2152 GTIQHLKSKFGD 2163
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1178-1364 |
1.91e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1178 ETIGIVGRTGSGKSSLGVALFRL----AELSRGSIIIDGVNIAHIGLEDLR----SKLSVIPQEPVlfigtvrSNLDPwd 1249
Cdd:PRK11022 34 EVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPM-------TSLNP-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1250 QYTDA-QIWEALeKTH--------------------IKDMVSQLPNSLHsevtdngeNFSVGERQLLCVARALLRHSKIL 1308
Cdd:PRK11022 105 CYTVGfQIMEAI-KVHqggnkktrrqraidllnqvgIPDPASRLDVYPH--------QLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 1309 LLDEATAAID-TETDRLIQDTIRSSFSGCTTLV-IAHRLNTVL-GCNRIMVLDQGQILE 1364
Cdd:PRK11022 176 IADEPTTALDvTIQAQIIELLLELQQKENMALVlITHDLALVAeAAHKIIVMYAGQVVE 234
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
887-1002 |
1.91e-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: 42.03 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 887 IRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFSKDMDEVDVRLAMQAEMLLQNVTLVLFCLGV---V 963
Cdd:cd18542 58 LQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIImfsI 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1207190976 964 GAVFPWFLFSIIPLGAFLFIV--NRISRV--LIRE-LKRL-----ENIS 1002
Cdd:cd18542 138 NWKLTLISLAIIPFIALFSYVffKKVRPAfeEIREqEGELntvlqENLT 186
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
644-724 |
2.43e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 41.51 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFH--SAIRpAAKGKTVIFVTHQL-QYLPECDDVVLMKDGQI 720
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEllSELN-REKGYTLAAVLHDLnQACRYASHLIALREGKI 222
|
....
gi 1207190976 721 AEHG 724
Cdd:PRK10253 223 VAQG 226
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
596-725 |
2.71e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.06 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 596 DSLREniLF-----GKKYNEE----KYNA-----VL-----EACCLFPDI----------IELPYGDMTeIGERGANLSG 646
Cdd:cd03271 96 DEIRE--LFcevckGKRYNREtlevRYKGksiadVLdmtveEALEFFENIpkiarklqtlCDVGLGYIK-LGQPATTLSG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 647 GQRQRVSLARALY---SERPILLLDDP---LSAVDARvgsRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLM----- 715
Cdd:cd03271 173 GEAQRIKLAKELSkrsTGKTLYILDEPttgLHFHDVK---KLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLgpegg 249
|
170
....*....|.
gi 1207190976 716 -KDGQIAEHGT 725
Cdd:cd03271 250 dGGGQVVASGT 260
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1178-1350 |
3.58e-03 |
|
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: 39.66 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1178 ETIGIVGRTGSGKSSLGVALFR-LAELSRGSIIIDGVNIAHIGLEDLRSKLsvipqepvlfigtvrsnldpwdqytdaqi 1256
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLII----------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1257 wealekthikdmvsqlpnslhseVTDNGENFSVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIRS----- 1331
Cdd:smart00382 54 -----------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllll 110
|
170 180
....*....|....*....|.
gi 1207190976 1332 --SFSGCTTLVIAHRLNTVLG 1350
Cdd:smart00382 111 lkSEKNLTVILTTNDEKDLGP 131
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
644-675 |
3.68e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 40.87 E-value: 3.68e-03
10 20 30
....*....|....*....|....*....|..
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVD 675
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1288-1351 |
3.87e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.47 E-value: 3.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190976 1288 SVGERQLLCVARALLRHSKILLLDEATAAIDTETDRLIQDTIrSSFSGcTTLVIAH-RL---NTVLGC 1351
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DSYQG-TVLLVSHdRQfvdNTVTEC 507
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
645-770 |
4.23e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 645 SGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIR-PaakgKTVIFVTHQLQYLPE-CDDVVLMKDGQIAE 722
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKwP----KTFIVVSHAREFLNTvVTDILHLHGQKLVT 421
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1207190976 723 HGTHTQLMEKGRDyaalfnsvqqenlvrKNLKNKEKAEKESSPQTLHV 770
Cdd:PLN03073 422 YKGDYDTFERTRE---------------EQLKNQQKAFESNERSRSHM 454
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1167-1365 |
5.70e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1167 LKNLCFSILPEETIGIVGRTGSGKSSLgvalfrlaelsrgSIIIDGVNIAHIGLEDLRSKLSVIpqepvlfigTVRSNLD 1246
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTL-------------SNLIAGVTMPNKGTVDIKGSAALI---------AISSGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 1247 pwDQYTDAQIWE------ALEKTHIKDMVSQLpnslhSEVTDNG-------ENFSVGERQLLCVARALLRHSKILLLDEA 1313
Cdd:PRK13545 98 --GQLTGIENIElkglmmGLTKEKIKEIIPEI-----IEFADIGkfiyqpvKTYSSGMKSRLGFAISVHINPDILVIDEA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 1314 TAAID-TETDRLIQDTIRSSFSGCTTLVIAHRLNTVLG-CNRIMVLDQGQILEF 1365
Cdd:PRK13545 171 LSVGDqTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEY 224
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1163-1199 |
5.97e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 40.52 E-value: 5.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1207190976 1163 LPLVLKNLCFSILPEE-------TIGIVGRTGSGKSSLGVALFR 1199
Cdd:COG3596 18 LPQVLRELLAEALERLlvelpppVIALVGKTGAGKSSLINALFG 61
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
535-719 |
7.17e-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: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 535 KTLHRIDLCIQKGSLVGVCGGVGSGKSSLLSALL---------GQMTLLGGSVSVNG-------GFAYVAQQAWILND-S 597
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvyphgtwdGEIYWSGSPLKASNirdteraGIVIIHQELTLVPElS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 598 LRENILFGKKYNEE----KYNAVLEACCLFPDIIELPYGDMT-EIGERGanlsGGQRQRVSLARALYSERPILLLDDPLS 672
Cdd:TIGR02633 95 VAENIFLGNEITLPggrmAYNAMYLRAKNLLRELQLDADNVTrPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207190976 673 AVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPE-CDDVVLMKDGQ 719
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
873-1037 |
7.69e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 39.87 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 873 VYVLSMgaalFLKTIRGLVFVKCTVRAASVLHDKLFKTLLLSPMRFFDTTPLGRILNRFsKDMDEVDVRLAMQAEMLLQN 952
Cdd:cd18566 51 AILLES----LLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 953 VTLVLFCLGVVGAVFPWFLFsiIPLGAFLFIV------NRISRVLIRELKRLENISQspftSHITSSLQGLSTIYAYGRG 1026
Cdd:cd18566 126 LPFVLIFLGLIWYLGGKLVL--VPLVLLGLFVlvaillGPILRRALKERSRADERRQ----NFLIETLTGIHTIKAMAME 199
|
170
....*....|.
gi 1207190976 1027 ADFIHRYQALL 1037
Cdd:cd18566 200 PQMLRRYERLQ 210
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
639-724 |
8.05e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 639 ERGAN-LSGGQRQRVSLARALYSERP--ILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQYLPECDDVVLM 715
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDI 562
|
....*....
gi 1207190976 716 KDGQiAEHG 724
Cdd:TIGR00630 563 GPGA-GEHG 570
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
644-734 |
9.02e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.11 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 644 LSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAK-GKTVIFVTHQLQYLPE-CDDVVLMKDGQIA 721
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEaAHKIIVMYAGQVV 233
|
90
....*....|...
gi 1207190976 722 EHGTHTQLMEKGR 734
Cdd:PRK11022 234 ETGKAHDIFRAPR 246
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
557-761 |
9.59e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 557 GSGKSSLLSALLGQMTLLGGSVSVNGGFAYVAQQAWiLNDSLR--ENILF-----GKKYNEEKYnavleaccLFPDIIEL 629
Cdd:PRK13546 60 GSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAG-LSGQLTgiENIEFkmlcmGFKRKEIKA--------MTPKIIEF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190976 630 pygdmTEIGE----RGANLSGGQRQRVSLARALYSERPILLLDDPLSAVDARVGSRLFHSAIRPAAKGKTVIFVTHQLQY 705
Cdd:PRK13546 131 -----SELGEfiyqPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQ 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190976 706 LPE-CDDVVLMKDGQIAEHGTHTQLMEKGRDYAALFN--SVQQENLVRKNLKNKEKAEK 761
Cdd:PRK13546 206 VRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKkkSKAEQKEFRNKLDESRFVIK 264
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
643-713 |
9.78e-03 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 39.66 E-value: 9.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190976 643 NLSGGQRQRVSLARALYSERPILLLDDPLSAVDAR---VGSRLFHSAIRPaakGKTVIFVTHQLQYLPECDDVV 713
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAED---DNYVLVVEHDLAVLDYLSDYI 209
|
|
| |
