|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
212-1575 |
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: 839.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 212 IPIRS-VYIGNIDDVPSQIFYIFEFVITSTLQPIKLT-SPIKDNSSIIYVRDDHTSPSREHISSILSCITWSWITNFIWE 289
Cdd:TIGR00957 145 AILRSkILLALKEDAIVDPFRDTTFYIYFALVLSQLVlSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVY 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 290 AQKNTIKLKDIWGLSMEDYSIFILKGF----------TRRNK-----------------HIN------------------ 324
Cdd:TIGR00957 225 GYRQPLEESDLWSLNKEDTSEMVVPVLvenwkkeckkTRKQPvsavygkkdpskpkgssQLDaneevealivksphkprk 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 325 -NLTLALFESFKTYLLIGMLWVLVNSIVNLLPTILMKRFLEIVDNPNRSSScmnLAWLYIIGMFICRL--TLA------I 395
Cdd:TIGR00957 305 pSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDW---QGYFYTGLLFVCAClqTLIlhqyfhI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 396 CnsqgqFVSDkicLRIRAILIGEIYAKGLrrrlftspkTSSDSDSISANLGTIINLISIDSFKVSELANYLYVTVQAVIM 475
Cdd:TIGR00957 382 C-----FVSG---MRIKTAVMGAVYRKAL---------VITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQ 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 476 IIVVVGLLFNFLGVSAFAGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKS 555
Cdd:TIGR00957 445 VILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEG 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 556 IRQKELRSLLKKSLVWSVTSFLWFVTPTLVTGVTFAICTFVQHED-LNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSK 634
Cdd:TIGR00957 525 IRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNiLDAEKAFVSLALFNILRFPLNILPMVISSIVQAS 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 635 VSLKRISDFLRMD--DTEKYNQLTISP-DKNKIEFKNATLTWNENDSDMnafkLCGLNIKFQIGKLNLILGSTGSGKSAL 711
Cdd:TIGR00957 605 VSLKRLRIFLSHEelEPDSIERRTIKPgEGNSITVHNATFTWARDLPPT----LNGITFSIPEGALVAVVGQVGCGKSSL 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 712 LLGLLGELNLISGSIivpslepkhdlipdceGLTNSFAYCSQSAWLLNDTVKNNIIFDNFYNEDRYNKVIDACGLKRDLE 791
Cdd:TIGR00957 681 LSALLAEMDKVEGHV----------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLE 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 792 ILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCItGP--LMKNRTCILVTHNVS 869
Cdd:TIGR00957 745 ILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVI-GPegVLKNKTRILVTHGIS 823
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 870 LtLRNAHFAIVLENGKVKNQGTITEL-QSKGLFKE---KYVQLSSRDSINEKNANRLKAPRK------------------ 927
Cdd:TIGR00957 824 Y-LPQVDVIIVMSGGKISEMGSYQELlQRDGAFAEflrTYAPDEQQGHLEDSWTALVSGEGKeakliengmlvtdvvgkq 902
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 928 -------------NDSQKIEPVTENINFDANfVNDGQLIEEEEKSNGAISPDVYKWYLKFFGGFKALTALFaLYITAQIL 994
Cdd:TIGR00957 903 lqrqlsasssdsgDQSRHHGSSAELQKAEAK-EETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIF-LFVCNHVS 980
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 995 FISQSWWIRHWVNDTnvrinapgfamdtlplkgMTDSSKNkhNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKI 1074
Cdd:TIGR00957 981 ALASNYWLSLWTDDP------------------MVNGTQN--NTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVL 1040
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1075 FNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPRFLTVAVIVFVLYFF 1154
Cdd:TIGR00957 1041 HQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFF 1120
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1155 VGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRFILENMNKIDQNNRAFFYLSVTVKWFSFRVDMIGA 1234
Cdd:TIGR00957 1121 VQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGN 1200
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1235 FIVLASGSFILLNIANIDSGLAGISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYSSIEQENYLGHDEGRilllnE 1314
Cdd:TIGR00957 1201 CIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETA-----P 1275
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1315 PS-WPKDGEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDL 1393
Cdd:TIGR00957 1276 PSgWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGL 1355
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1394 VTLRRSITIIPQDPILFAGTIKSNVDPYDEYDEKKIFKALSQVNLissHEFEEVLNSEerfnsthnkflnLHTEIAEGGL 1473
Cdd:TIGR00957 1356 HDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHL---KTFVSALPDK------------LDHECAEGGE 1420
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1474 NLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEY 1553
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
|
1450 1460
....*....|....*....|..
gi 6321752 1554 DRPSELLKdERGIFYSMCRDSG 1575
Cdd:TIGR00957 1501 GAPSNLLQ-QRGIFYSMAKDAG 1521
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
217-1575 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 751.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 217 VYIGNIddVPSQIFYIFEFVITSTLQPIKLTSPIKDNSSIIYVRDDhtSPSREHI-----SSILSCITWSWITNFIWEAQ 291
Cdd:PLN03130 176 LYISEV--AAQVLFGILLLVYFPNLDPYPGYTPIGSESVDDYEYEE--LPGGEQIcperhANIFSRIFFGWMTPLMQLGY 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 292 KNTIKLKDIWGLSMEDYSIFILKGFTR-----RNKHINNLTLALFESFKTYLLIGMLWVLVNSIVNLLPTILMKRFLEIV 366
Cdd:PLN03130 252 KRPLTEKDVWKLDTWDQTETLYRSFQKcwdeeLKKPKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESM 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 367 DNPNRssscmnlAW---LYIIGMFICRLTLAICnsQGQFVSD--KICLRIRAILIGEIYAKGLR-----RRLFTSpktss 436
Cdd:PLN03130 332 QNGEP-------AWigyIYAFSIFVGVVLGVLC--EAQYFQNvmRVGFRLRSTLVAAVFRKSLRlthegRKKFTS----- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 437 dsdsisanlGTIINLISIDSFKVSELANYLYVTVQAVIMIIVVVGLLFNFLGVSAFAGISIILVMFPLNFLLANLLGKFQ 516
Cdd:PLN03130 398 ---------GKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLT 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 517 KQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSLLKKSLVWSVTSFLWFVTPTLVTGVTFAICTFV 596
Cdd:PLN03130 469 KEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 597 QHeDLNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVSLKRISDFLRMDDTEKYNQLTISPDKNKIEFKNATLTWnen 676
Cdd:PLN03130 549 GG-DLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGLPAISIKNGYFSW--- 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 677 DSDMNAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVpslepkhdlipdcegLTNSFAYCSQSAW 756
Cdd:PLN03130 625 DSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV---------------IRGTVAYVPQVSW 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 757 LLNDTVKNNIIFDNFYNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLS 836
Cdd:PLN03130 690 IFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 837 AVDSHTAVWIYENCITGPLmKNRTCILVTHNVSLtLRNAHFAIVLENGKVKNQGTITELQSKG-LFKEKYVQLSSRDSIN 915
Cdd:PLN03130 770 ALDAHVGRQVFDKCIKDEL-RGKTRVLVTNQLHF-LSQVDRIILVHEGMIKEEGTYEELSNNGpLFQKLMENAGKMEEYV 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 916 EKNaNRLKAPRKNDSQKIEPVTENINFDANFVNDGQ-----LIEEEEKSNGAISPDVYKWYLKFFGGFKALTALFALYIT 990
Cdd:PLN03130 848 EEN-GEEEDDQTSSKPVANGNANNLKKDSSSKKKSKegksvLIKQEERETGVVSWKVLERYKNALGGAWVVMILFLCYVL 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 991 AQILFISQSWWIRHWVNDTNVRINAPGfamdtlplkgmtdssknkhnafYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRA 1070
Cdd:PLN03130 927 TEVFRVSSSTWLSEWTDQGTPKTHGPL----------------------FYNLIYALLSFGQVLVTLLNSYWLIMSSLYA 984
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1071 SRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPRFLTVAVIVFV 1150
Cdd:PLN03130 985 AKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLV 1064
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1151 LYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRFILENMNKIDQNNRaffYLSVTV---KWFSF 1227
Cdd:PLN03130 1065 LFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIR---FTLVNMssnRWLAI 1141
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1228 RVDMIGAFIVLASGSFILLNIANIDSGLA-----GISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYSSIEQENYL 1302
Cdd:PLN03130 1142 RLETLGGLMIWLTASFAVMQNGRAENQAAfastmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPL 1221
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1303 GHDEGRilllNEPSWPKDGEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIK 1382
Cdd:PLN03130 1222 VIENNR----PPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL 1297
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1383 IDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNVDPYDEYDEKKIFKALSQVNLisshefEEVLnseeRFNSthnkfL 1462
Cdd:PLN03130 1298 IDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHL------KDVI----RRNS-----L 1362
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1463 NLHTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRI 1542
Cdd:PLN03130 1363 GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRI 1442
|
1370 1380 1390
....*....|....*....|....*....|...
gi 6321752 1543 IVMDAGEVKEYDRPSELLKDERGIFYSMCRDSG 1575
Cdd:PLN03130 1443 LVLDAGRVVEFDTPENLLSNEGSAFSKMVQSTG 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
266-1575 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 709.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 266 PSREHI-----SSILSCITWSWITNFIWEAQKNTIKLKDIWGLSMEDYSIFILKGF-------TRRNKHInnLTLALFES 333
Cdd:PLN03232 221 RGGENIcperyASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFqrcwteeSRRPKPW--LLRALNNS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 334 FKTYLLIGMLWVLVNSIVNLLPTILMKRFLeivdnpnRSSSCMNLAWL---YIIGMFICRLTLAICNSQGQFVSDKICLR 410
Cdd:PLN03232 299 LGGRFWLGGIFKIGHDLSQFVGPVILSHLL-------QSMQEGDPAWVgyvYAFLIFFGVTFGVLCESQYFQNVGRVGFR 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 411 IRAILIGEIYAKGLR-----RRLFTSpktssdsdsisanlGTIINLISIDSFKVSELANYLYVTVQAVIMIIVVVGLLFN 485
Cdd:PLN03232 372 LRSTLVAAIFHKSLRltheaRKNFAS--------------GKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQ 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 486 FLGVSAFAGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSLL 565
Cdd:PLN03232 438 QLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFR 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 566 KKSLVWSVTSFLWFVTPTLVTGVTFAICTFVQHeDLNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVSLKRISDFLR 645
Cdd:PLN03232 518 KAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGG-DLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLL 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 646 MDDTEKYNQLTISPDKNKIEFKNATLTWnenDSDMNAFKLCGLNIKFQIGKLNLILGSTGSGKSALLlgllgelnlisgS 725
Cdd:PLN03232 597 SEERILAQNPPLQPGAPAISIKNGYFSW---DSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLI------------S 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 726 IIVPSLEPKHDLIPDCEGltnSFAYCSQSAWLLNDTVKNNIIFDNFYNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKG 805
Cdd:PLN03232 662 AMLGELSHAETSSVVIRG---SVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERG 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 806 ITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLmKNRTCILVTHNVSLtLRNAHFAIVLENGK 885
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDEL-KGKTRVLVTNQLHF-LPLMDRIILVSEGM 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 886 VKNQGTITELQSKG-LFKEKYVQLSSRDSINEKNANRlkaprKNDSQKIEPVTENI-NFDANFVNDGQ-----LIEEEEK 958
Cdd:PLN03232 817 IKEEGTFAELSKSGsLFKKLMENAGKMDATQEVNTND-----ENILKLGPTVTIDVsERNLGSTKQGKrgrsvLVKQEER 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 959 SNGAISPDVYKWYLKFFGGFKALTALFALYITAQILFISQSWWIRHWVNDTNVRINAPGFamdtlplkgmtdssknkhna 1038
Cdd:PLN03232 892 ETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSPGF-------------------- 951
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1039 fyYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLE 1118
Cdd:PLN03232 952 --YIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMN 1029
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1119 VTIFCLIQCASIIFLITVITPRFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDER 1198
Cdd:PLN03232 1030 MFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYD 1109
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1199 RFILENMNKIDQNNRAFFYLSVTVKWFSFRVDMIGAFIVLASGSFILLNIANIDS--GLA---GISLTYAILFTDGALWL 1273
Cdd:PLN03232 1110 RMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENqaGFAstmGLLLSYTLNITTLLSGV 1189
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1274 VRLYSTFEMNMNSVERLKEYSSIEQEnylghdEGRILLLNEP--SWPKDGEIEIENLSLRYAPNLPPVIRNVSFKVDPQS 1351
Cdd:PLN03232 1190 LRQASKAENSLNSVERVGNYIDLPSE------ATAIIENNRPvsGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSE 1263
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1352 KIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNVDPYDEYDEKKIFK 1431
Cdd:PLN03232 1264 KVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWE 1343
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1432 ALSQVNLisshefEEVLNseerfnstHNKFlNLHTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDH 1511
Cdd:PLN03232 1344 ALERAHI------KDVID--------RNPF-GLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 1512 LIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELLKDERGIFYSMCRDSG 1575
Cdd:PLN03232 1409 LIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTG 1472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
326-1570 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 600.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 326 LTLALFESFKTYLLIGMLWVLVNSIVNLLPTILMKRFLEIVDNPNRSsscmnlaWLY----IIGMFICRLTLAICNSQGQ 401
Cdd:PTZ00243 234 LLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNAT-------WGRglglVLTLFLTQLIQSVCLHRFY 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 402 FVSDKICLRIRAILIGEIYAKglrrrLFT-SPKTSSDSDsisANLGTIINLISIDSFKVSELANYLYVTVQAVIMIIVVV 480
Cdd:PTZ00243 307 YISIRCGLQYRSALNALIFEK-----CFTiSSKSLAQPD---MNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSI 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 481 GLLFNFLGVSAFAGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKE 560
Cdd:PTZ00243 379 LLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 561 LRSLLKKSLVWSVTSFLWFVTPTLVTGVTFAICTFVQHEdLNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVSLKRI 640
Cdd:PTZ00243 459 LRYLRDVQLARVATSFVNNATPTLMIAVVFTVYYLLGHE-LTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRI 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 641 SDFLRMDD---------TEKYNQLTISPDKNKIE--FKNATLT-----------------------W------------- 673
Cdd:PTZ00243 538 STFLECDNatcstvqdmEEYWREQREHSTACQLAavLENVDVTafvpvklprapkvktsllsralrMlcceqcrptkrhp 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 674 -----------------------------------NENDSDMNAFK------------LCGLNIKFQIGKLNLILGSTGS 706
Cdd:PTZ00243 618 spsvvvedtdygspssasrhiveggtgggheatptSERSAKTPKMKtddffelepkvlLRDVSVSVPRGKLTVVLGATGS 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 707 GKSALLLGLLGELNLISGSIIVpslepkhdlipdceglTNSFAYCSQSAWLLNDTVKNNIIFDNFYNEDRYNKVIDACGL 786
Cdd:PTZ00243 698 GKSTLLQSLLSQFEISEGRVWA----------------ERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQL 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 787 KRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLmKNRTCILVTH 866
Cdd:PTZ00243 762 EADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGAL-AGKTRVLATH 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 867 NVSLTLRnAHFAIVLENGKVKNQGTITELQSKGLFKEKYVQLSSRDSINEKNANR-----------LKAPRKNDSQKIEP 935
Cdd:PTZ00243 841 QVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYATLAAELKENKDSKEGDADAevaevdaapggAVDHEPPVAKQEGN 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 936 VTEN--INFDAnfvNDGQLIEEEEKSNGAISPDVYKWYLKFFGGFKALTALFALYITAQILFISQSWWIRHWVNDtnvri 1013
Cdd:PTZ00243 920 AEGGdgAALDA---AAGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMWSTR----- 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1014 napgfamdtlplkgmtdssKNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVT 1093
Cdd:PTZ00243 992 -------------------SFKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTT 1052
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1094 PVGRIMNRFSKDIEGVDQEL-IPYLEV-TIFCLIqCASIifLITVITPRFLTVAVI-VFVLYFFVGKWYLTASRELKRLD 1170
Cdd:PTZ00243 1053 PLGRILNRFSRDIDILDNTLpMSYLYLlQCLFSI-CSSI--LVTSASQPFVLVALVpCGYLYYRLMQFYNSANREIRRIK 1129
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1171 SITKSPIFQHFSETLVGVCTIRAFGDERRFILENMNKIDQNNRAFFYLSVTVKWFSFRVDMIGAFIVLASgSFI-----L 1245
Cdd:PTZ00243 1130 SVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVI-ALIgvigtM 1208
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1246 LNIANIDSGLAGISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYS-SIEQENYLGHDE----------------GR 1308
Cdd:PTZ00243 1209 LRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDMPELDEevdalerrtgmaadvtGT 1288
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1309 ILLlnEPSWP--------KDGEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGC 1380
Cdd:PTZ00243 1289 VVI--EPASPtsaaphpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGE 1366
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1381 IKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNVDPYDEYDEKKIFKALSQVNLissheFEEVLNSEERFNSthnk 1460
Cdd:PTZ00243 1367 IRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGL-----RERVASESEGIDS---- 1437
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1461 flnlhtEIAEGGLNLSQGERQLLFIARSLL-REPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDY 1539
Cdd:PTZ00243 1438 ------RVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQY 1511
|
1370 1380 1390
....*....|....*....|....*....|.
gi 6321752 1540 DRIIVMDAGEVKEYDRPSELLKDERGIFYSM 1570
Cdd:PTZ00243 1512 DKIIVMDHGAVAEMGSPRELVMNRQSIFHSM 1542
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1317-1556 |
1.23e-122 |
|
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: 382.15 E-value: 1.23e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1317 WPKDGEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTL 1396
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1397 RRSITIIPQDPILFAGTIKSNVDPYDEYDEKKIFKALSqvnlisshefeevlnseerfnsthnkflnlhteIAEGGLNLS 1476
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR---------------------------------VSEGGLNLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1477 QGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRP 1556
Cdd:cd03369 128 QGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
982-1294 |
4.82e-121 |
|
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: 381.43 E-value: 4.82e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 982 TALFALYITAQILFISQSWWIRHWVNDTNVRINAPGfamdtlplkgmtdsskNKHNAFYYLTVYFLIGIIQAMLGGFKTM 1061
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPP----------------SEVSVLYYLGIYALISLLSVLLGTLRYL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1062 MTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPRF 1141
Cdd:cd18604 66 LFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1142 LTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRFILENMNKIDQNNRAFFYLSVT 1221
Cdd:cd18604 146 LLPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNL 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 1222 VKWFSFRVDMIGAFIVLASGSFILLNiANIDSGLAGISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYS 1294
Cdd:cd18604 226 NRWLSVRIDLLGALFSFATAALLVYG-PGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
407-1589 |
9.26e-120 |
|
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: 412.38 E-value: 9.26e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 407 ICLRIRAILIGEIYAKGLRRrlftspkTSSDSDSISanLGTIINLISIDSFKVSE---LANYLYVtvqAVIMIIVVVGLL 483
Cdd:TIGR01271 149 LGMQMRIALFSLIYKKTLKL-------SSRVLDKIS--TGQLVSLLSNNLNKFDEglaLAHFVWI---APLQVILLMGLI 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 484 FNFLGVSAFAGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRS 563
Cdd:TIGR01271 217 WELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 564 LLKKSLVWSVTSFLWFVTPTLVtgVTFAICTFVQHEDLNAPLAFTTLSLFTLLKTPLD-QLSNMLSFINQSKVSLKRISD 642
Cdd:TIGR01271 297 TRKIAYLRYFYSSAFFFSGFFV--VFLSVVPYALIKGIILRRIFTTISYCIVLRMTVTrQFPGAIQTWYDSLGAITKIQD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 643 FLRMDD--TEKYNQLTispdkNKIEFKNATLTWNE-----------NDSD-----------MNAFKLCG------LNIKF 692
Cdd:TIGR01271 375 FLCKEEykTLEYNLTT-----TEVEMVNVTASWDEgigelfekikqNNKArkqpngddglfFSNFSLYVtpvlknISFKL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 693 QIGKLNLILGSTGSGKSALLLgllgelnlisgsIIVPSLEPKHDLIPDceglTNSFAYCSQSAWLLNDTVKNNIIFDNFY 772
Cdd:TIGR01271 450 EKGQLLAVAGSTGSGKSSLLM------------MIMGELEPSEGKIKH----SGRISFSPQTSWIMPGTIKDNIIFGLSY 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 773 NEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCIT 852
Cdd:TIGR01271 514 DEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLC 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 853 gPLMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITELQ-------SKGLFKEKYVQLSS--RDSI--------- 914
Cdd:TIGR01271 594 -KLMSNKTRILVTSKLE-HLKKADKILLLHEGVCYFYGTFSELQakrpdfsSLLLGLEAFDNFSAerRNSIltetlrrvs 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 915 -------------------------NEKNANRL---------------KAPRKN---------------------DSQKI 933
Cdd:TIGR01271 672 idgdstvfsgpetikqsfkqpppefAEKRKQSIilnpiasarkfsfvqMGPQKAqattiedavrepserkfslvpEDEQG 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 934 EPVTENIN-------FDA-------NFV---NDGQLIEEEEKSN----GAISP--------DVYKWYLKFFGGF------ 978
Cdd:TIGR01271 752 EESLPRGNqyhhglqHQAqrrqsvlQLMthsNRGENRREQLQTSfrkkSSITQqnelaselDIYSRRLSKDSVYeiseei 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 979 --KALTALFAlyITAQILFISQSW--WIRHWVNDTN-------------VRINAP--------GFAMDTLPLKGMTDSSK 1033
Cdd:TIGR01271 832 neEDLKECFA--DERENVFETTTWntYLRYITTNRNlvfvlifclviflAEVAASllglwlitDNPSAPNYVDQQHANAS 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1034 NKHNAF--------YYLTVYFLIGIIQAML--GGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFS 1103
Cdd:TIGR01271 910 SPDVQKpviitptsAYYIFYIYVGTADSVLalGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFT 989
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1104 KDIEGVDqELIPyleVTIFCLIQCASI----IFLITVITPRFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQ 1179
Cdd:TIGR01271 990 KDMAIID-DMLP---LTLFDFIQLTLIvlgaIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFS 1065
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1180 HFSETLVGVCTIRAFGDERRFilENMNKIDQNNRA---FFYLSvTVKWFSFRVDMIGAFIVLASgSFILLNIANIDSGLA 1256
Cdd:TIGR01271 1066 HLITSLKGLWTIRAFGRQSYF--ETLFHKALNLHTanwFLYLS-TLRWFQMRIDIIFVFFFIAV-TFIAIGTNQDGEGEV 1141
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1257 GISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYSSIEQE------NYLGHDEGRILLLNEPS----WPKDGEIEIE 1326
Cdd:TIGR01271 1142 GIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEeprpsgGGGKYQLSTVLVIENPHaqkcWPSGGQMDVQ 1221
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1327 NLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEpITGCIKIDGQDISKIDLVTLRRSITIIPQD 1406
Cdd:TIGR01271 1222 GLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQK 1300
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1407 PILFAGTIKSNVDPYDEYDEKKIFKALSQVNLISSHE-FEEVLNseerfnsthnkflnlhTEIAEGGLNLSQGERQLLFI 1485
Cdd:TIGR01271 1301 VFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEqFPDKLD----------------FVLVDGGYVLSNGHKQLMCL 1364
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1486 ARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELLkDERG 1565
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETS 1443
|
1370 1380
....*....|....*....|....
gi 6321752 1566 IFYSMCRDSGGLELLKQIAKQSSK 1589
Cdd:TIGR01271 1444 LFKQAMSAADRLKLFPLHRRNSSK 1467
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1321-1556 |
4.25e-108 |
|
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: 342.55 E-value: 4.25e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1321 GEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSI 1400
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAGTIKSNVDPYDEYDEKKIFKALSQVNLISSHEfeevlnseerfnsthNKFLNLHTEIAEGGLNLSQGER 1480
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVE---------------SLPGGLDTVVEEGGENLSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 1481 QLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRP 1556
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
967-1572 |
5.18e-102 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 339.45 E-value: 5.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 967 VYKWYLKFFGGFKALTAL-FALYITAQILFISQSWWIRHWVNDTNVRINAPGFAMdtlplkgmtdssknkhnafyYLTVY 1045
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILaLLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLL--------------------LLLLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1046 FLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLI 1125
Cdd:COG1132 68 LGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1126 QCASIIFLITVITPRFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRFILENM 1205
Cdd:COG1132 148 TLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1206 NKIDQNNRAFFYLSVTVKWFSFRVDMIGAFIVLASGSFILLNIAN--IDSGLAGISLTYAILFTDGALWLVRLYSTFEMN 1283
Cdd:COG1132 228 EANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSgsLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1284 MNSVERLKEYssIEQENYLGHDEGRILLLnepswPKDGEIEIENLSLRYAPNlPPVIRNVSFKVDPQSKIGIVGRTGAGK 1363
Cdd:COG1132 308 LASAERIFEL--LDEPPEIPDPPGAVPLP-----PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1364 STIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNV---DPydEYDEKKIFKALSQVNLis 1440
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQA-- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1441 sHEFeeVLNSEERfnsthnkflnLHTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSE 1520
Cdd:COG1132 456 -HEF--IEALPDG----------YDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL 522
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 6321752 1521 FNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELLKdERGIFYSMCR 1572
Cdd:COG1132 523 MKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA-RGGLYARLYR 573
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
342-640 |
1.33e-100 |
|
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: 325.22 E-value: 1.33e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 342 MLWVLVNSIVNLLPTILMKRFLEIVDNPNRSSscMNLAWLYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILIGEIYA 421
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLEDPGEDA--TVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 422 KGLRRRLFTSP----------KTSSDSDSISANLGTIINLISIDSFKVSELANYLYVTVQAVIMIIVVVGLLFNFLGVSA 491
Cdd:cd18596 81 KALRRRDKSGSsksseskkkdKEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 492 FAGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSLLKKSLVW 571
Cdd:cd18596 161 LVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLD 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 572 SVTSFLWFVTPTLVTGVTFAICTFVQHEDLNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVSLKRI 640
Cdd:cd18596 241 LLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
664-885 |
8.66e-97 |
|
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: 309.78 E-value: 8.66e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDSDMNaFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSlepkhdlipdceg 743
Cdd:cd03250 1 ISVEDASFTWDSGEQETS-FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 744 ltnSFAYCSQSAWLLNDTVKNNIIFDNFYNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVY 823
Cdd:cd03250 67 ---SIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321752 824 SSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLtLRNAHFAIVLENGK 885
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
981-1294 |
1.63e-96 |
|
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: 312.90 E-value: 1.63e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 981 LTALFALYITAQILFISQSWWIRHWVNDTnvrinapgfamdtlplkgmtdSSKNKHNAFYYLTVYFLIGIIQAMLGGF-K 1059
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDW---------------------SSSPNSSSGYYLGVYAALLVLASVLLVLlR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1060 TMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITP 1139
Cdd:cd18580 60 WLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1140 RFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRFILENMNKIDQNNRAFFYLS 1219
Cdd:cd18580 140 YFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLL 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 1220 VTVKWFSFRVDMIGAFIVLASGSFILLNIANIDSGLAGISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYS 1294
Cdd:cd18580 220 AVQRWLGLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
985-1294 |
9.79e-92 |
|
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: 299.39 E-value: 9.79e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 985 FALYITAQILFISQSWWIRHWVNDTNvrinapgfamdtlplkgmTDSSKNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTF 1064
Cdd:cd18603 5 LLLYLLSQAFSVGSNIWLSEWSDDPA------------------LNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1065 LSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPRFLTV 1144
Cdd:cd18603 67 LGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1145 AVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRFILENMNKIDQNNRAFFYLSVTVKW 1224
Cdd:cd18603 147 IIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRW 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1225 FSFRVDMIGAFIVLASGSFILLNIANIDSGLAGISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYS 1294
Cdd:cd18603 227 LAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1036-1570 |
1.06e-84 |
|
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: 293.66 E-value: 1.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1036 HNAFYYLTVyflIGIIQAMLGGFKTMMTFLSG---MRASRKIF----NNLLDLVLHAQIRFFDVTPVGRIMNRFSkDIEG 1108
Cdd:COG2274 189 NQDLSTLWV---LAIGLLLALLFEGLLRLLRSyllLRLGQRIDlrlsSRFFRHLLRLPLSFFESRSVGDLASRFR-DVES 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1109 VdQELIPylEVTIFCLIQCASIIFLITVIT---PRFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETL 1185
Cdd:COG2274 265 I-REFLT--GSLLTALLDLLFVLIFLIVLFfysPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1186 VGVCTIRAFGDERRFILENMNK----IDQNNRAFFYLSVTVKWFSFrVDMIGAFIVLASGSFILLN--------IAnids 1253
Cdd:COG2274 342 RGIETIKALGAESRFRRRWENLlakyLNARFKLRRLSNLLSTLSGL-LQQLATVALLWLGAYLVIDgqltlgqlIA---- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1254 glagiSLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYSSIEQEnylgHDEGRILLLNEPswpKDGEIEIENLSLRYA 1333
Cdd:COG2274 417 -----FNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPE----REEGRSKLSLPR---LKGDIELENVSFRYP 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1334 PNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGT 1413
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGT 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1414 IKSNV---DPydEYDEKKIFKALSQVNLissHEFEEVLNseerfnsthnkfLNLHTEIAEGGLNLSQGERQLLFIARSLL 1490
Cdd:COG2274 565 IRENItlgDP--DATDEEIIEAARLAGL---HDFIEALP------------MGYDTVVGEGGSNLSGGQRQRLAIARALL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1491 REPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELLKdERGIFYSM 1570
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLA-RKGLYAEL 706
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
340-640 |
4.82e-82 |
|
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: 271.67 E-value: 4.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 340 IGMLWVLVNSIVNLLPTILMKRFLEIVDNPNRSSscMNLAWLYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILIGEI 419
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEP--LSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 420 YAKGLRRRLFTSPKTSSdsdsisanlGTIINLISIDSFKVSELANYLYVTVQAVIMIIVVVGLLFNFLGVSAFAGISIIL 499
Cdd:cd18579 79 YRKALRLSSSARQETST---------GEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 500 VMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSLLKKSLVWSVTSFLWF 579
Cdd:cd18579 150 LLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 580 VTPTLVTGVTFAICTFVQHEdLNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVSLKRI 640
Cdd:cd18579 230 STPVLVSLATFATYVLLGNP-LTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
984-1294 |
1.20e-79 |
|
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: 265.24 E-value: 1.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 984 LFALYITAQILFISQSWWIRHWVNdtnvriNAPGFAMDtlpLKGMTDSSKNKHNAFYYLTVYFLIGIIQAMLGGFKTMMT 1063
Cdd:cd18602 4 VLALALLKQGLRVATDFWLADWTE------ANHDVASV---VFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1064 FLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPRFLT 1143
Cdd:cd18602 75 ELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1144 VAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRFILENMNKIDQNNRAFFYLSVTVK 1223
Cdd:cd18602 155 ALIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANR 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 1224 WFSFRVDMIGAFIVLASGSFILL--NIANIDSGLAGISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYS 1294
Cdd:cd18602 235 WLGIRLDYLGAVIVFLAALSSLTaaLAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
981-1294 |
7.12e-78 |
|
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: 259.71 E-value: 7.12e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 981 LTALFALYITAQILFISQSWWIRHWVNDTnvrinapgfamdtlplkgmtdssKNKHNAFYyLTVYFLIGIIQAMLGGFKT 1060
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDF-----------------------FGLSQGFY-IGIYAGLGVLQAIFLFLFG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1061 MMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPR 1140
Cdd:cd18606 57 LLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPW 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1141 FLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRFILENMNKIDQNNRAFFYLSV 1220
Cdd:cd18606 137 FAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIA 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 1221 TVKWFSFRVDMIGAFIVLASGSFILLNIANIDSGLAGISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYS 1294
Cdd:cd18606 217 NQRWLAIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
989-1293 |
2.10e-68 |
|
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: 232.81 E-value: 2.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 989 ITAQILFISQSWWIRHWVNDTNVrinapgfamdtlplkgmTDSSKNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGM 1068
Cdd:cd18605 9 ILMQASRNLIDFWLSYWVSHSNN-----------------SFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1069 RASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPRFLTVAVIV 1148
Cdd:cd18605 72 RAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1149 FVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRFILENMNKIDQNNRAFFYLSVTVKWFSFR 1228
Cdd:cd18605 152 AFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIR 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321752 1229 VDMIGAFIVLASGSFILLNI---ANIDSGLAGISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEY 1293
Cdd:cd18605 232 LQLLGVLIVTFVALTAVVQHffgLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
980-1563 |
5.70e-66 |
|
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: 234.65 E-value: 5.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 980 ALTALFALyITAqILFISQSWWIrhwvndtnvrinapGFAMDTLPLKGMTDSSknkhnAFYYLTVYFLIGIIQAMLGGFK 1059
Cdd:COG4988 20 ALAVLLGL-LSG-LLIIAQAWLL--------------ASLLAGLIIGGAPLSA-----LLPLLGLLLAVLLLRALLAWLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1060 TMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFskdIEGVDQeLIPYLE-------------VTIFCLIQ 1126
Cdd:COG4988 79 ERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLL---TEGVEA-LDGYFArylpqlflaalvpLLILVAVF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1127 CAS----IIFLITVItprfltvAVIVFVLyfFVGKWYLTASRE----LKRLDSitkspifqHFSETLVGVCTIRAFGDER 1198
Cdd:COG4988 155 PLDwlsgLILLVTAP-------LIPLFMI--LVGKGAAKASRRqwraLARLSG--------HFLDRLRGLTTLKLFGRAK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1199 RFIlENMNKIDQNNR---------AFfyLSVTV-KWFSfrvdMIGAFIVLASGSFILLNianidsglAGISLTYAILFtd 1268
Cdd:COG4988 218 AEA-ERIAEASEDFRkrtmkvlrvAF--LSSAVlEFFA----SLSIALVAVYIGFRLLG--------GSLTLFAALFV-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1269 gaLWLV-------RLYSTF---EMN-MNSVERLKEYSSIEQENYLGHDEgrilllnEPSWPKDGEIEIENLSLRYaPNLP 1337
Cdd:COG4988 281 --LLLApefflplRDLGSFyhaRANgIAAAEKIFALLDAPEPAAPAGTA-------PLPAAGPPSIELEDVSFSY-PGGR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1338 PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSN 1417
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIREN 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1418 VDPYD-EYDEKKIFKALSQVNLissHEFEEVLNSEerfnsthnkflnLHTEIAEGGLNLSQGERQLLFIARSLLREPKII 1496
Cdd:COG4988 431 LRLGRpDASDEELEAALEAAGL---DEFVAALPDG------------LDTPLGEGGRGLSGGQAQRLALARALLRDAPLL 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 1497 LLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELLKDE 1563
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
340-640 |
8.04e-65 |
|
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: 221.96 E-value: 8.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 340 IGMLWVLVNSIVNLLPTILMKRFLEIVDNPNRSSscmnlaW---LYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILI 416
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPL------WkgyLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 417 GEIYAKGLRrrlftspkTSSDSDSiSANLGTIINLISIDSFKVSELANYLYVTVQAVIMIIVVVGLLFNFLGVSAFAGIS 496
Cdd:cd18595 75 SAIYRKALR--------LSNSARK-KSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 497 IILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSLLKKSLVWSVTSF 576
Cdd:cd18595 146 VMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSF 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 577 LWFVTPTLVTGVTFAicTFV---QHEDLNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVSLKRI 640
Cdd:cd18595 226 LWTCAPFLVSLATFA--TYVlsdPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1323-1570 |
9.65e-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: 216.71 E-value: 9.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPpVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAGTIKSNVDpYDEYD--EKKIFKALSQVNLissHefEEVLNSEERFNsthnkflnlhTEIAEGGLNLSQGER 1480
Cdd:cd03253 80 VPQDTVLFNDTIGYNIR-YGRPDatDEEVIEAAKAAQI---H--DKIMRFPDGYD----------TIVGERGLKLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1481 QLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELL 1560
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
250
....*....|
gi 6321752 1561 kDERGIFYSM 1570
Cdd:cd03253 224 -AKGGLYAEM 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1321-1561 |
3.20e-63 |
|
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: 215.17 E-value: 3.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1321 GEIEIENLSLRYAPNLPpVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSI 1400
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAGTIKSNVDPYDEY-DEKKIFKALSQVNLissHEFeeVLNSEErfnsthnkflNLHTEIAEGGLNLSQGE 1479
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGA---HDF--IMKLPN----------GYDTVLGENGGNLSQGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1480 RQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSEL 1559
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
..
gi 6321752 1560 LK 1561
Cdd:cd03254 225 LA 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
328-903 |
5.68e-63 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 226.20 E-value: 5.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 328 LALFESFKTYLLIGMLWVLVNSIVNLLPTILMKRfleIVDNPNRSSScMNLAWLYIIGMFICRLTLAICNSQGQFVSDKI 407
Cdd:COG1132 13 LRYLRPYRGLLILALLLLLLSALLELLLPLLLGR---IIDALLAGGD-LSALLLLLLLLLGLALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 408 CLRIRAILIGEIYAKGLRRRL--FTSPKTssdsdsisanlGTIINLISIDSFKVSELANYLYVT-VQAVIMIIVVVGLLF 484
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLsfFDRRRT-----------GDLLSRLTNDVDAVEQFLAHGLPQlVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 485 NFLGVSAFAGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSL 564
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 565 LKKSLVWSVTSFLWFVTPTLVTGVTFAI-CTFVQHEDLNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVSLKRISDF 643
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLGLALVLLVgGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 644 LRMDD--TEKYNQLTISPDKNKIEFKNATLTWNENDsdmNAFKlcGLNIKFQIGKLNLILGSTGSGKSalllgllgelnl 721
Cdd:COG1132 318 LDEPPeiPDPPGAVPLPPVRGEIEFENVSFSYPGDR---PVLK--DISLTIPPGETVALVGPSGSGKS------------ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 722 isgSIIvpslepkhDLIP--------------------DCEGLTNSFAYCSQSAWLLNDTVKNNIIFDNF-YNEDRynkV 780
Cdd:COG1132 381 ---TLV--------NLLLrfydptsgrilidgvdirdlTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPdATDEE---V 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 781 IDAC---GLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENciTGPLMK 857
Cdd:COG1132 447 EEAAkaaQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA--LERLMK 524
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 6321752 858 NRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITEL-QSKGLFKE 903
Cdd:COG1132 525 GRTTIVIAHRLS-TIRNADRILVLDDGRIVEQGTHEELlARGGLYAR 570
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
977-1294 |
2.40e-62 |
|
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: 215.89 E-value: 2.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 977 GFKALTALFALYITAQILFISQSWWIRHWVNDTNVRINAPgfamDTLPLKGMTDSSKNKHNAFY---YLTVYFLIGIIQA 1053
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNN----VDNSTVDSGNISDNPDLNFYqlvYGGSILVILLLSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1054 MLGGFKTMMTflsgMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFL 1133
Cdd:cd18599 77 IRGFVFVKVT----LRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1134 ITVITPRFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRFILENMNKIDQNNR 1213
Cdd:cd18599 153 IAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1214 AFFYLSVTVKWFSFRVDMIGAFIVLASGSFILLNIANIDSGLAGISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEY 1293
Cdd:cd18599 233 AFFLFNCAMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEY 312
|
.
gi 6321752 1294 S 1294
Cdd:cd18599 313 I 313
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
984-1294 |
5.78e-61 |
|
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: 211.80 E-value: 5.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 984 LFALYITAQILFISQSWWIRHWVNDTNVRINApgFAMDTLPLKGMTDSSKNKHNafYYLTVYFLIGIIQAMLGGFKTMMT 1063
Cdd:cd18601 8 LVLLNIAAQVLYVLSDWWLSYWANLEEKLNDT--TDRVQGENSTNVDIEDLDRD--FNLGIYAGLTAATFVFGFLRSLLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1064 FLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDqELIPY--LEVtIFCLIQCASIIFLITVITPRF 1141
Cdd:cd18601 84 FHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLD-DLLPLtfLDF-LQLLLQVVGVVLLAVVVNPWV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1142 LTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRFILENMNKIDQNNRAFFYLSVT 1221
Cdd:cd18601 162 LIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLAT 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 1222 VKWFSFRVDMIgAFIVLASGSFILLNIA-NIDSGLAGISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYS 1294
Cdd:cd18601 242 SRWLAVRLDAL-CALFVTVVAFGSLFLAeSLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1323-1549 |
3.29e-59 |
|
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: 201.07 E-value: 3.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAGTIKSNVdpydeydekkifkalsqvnlisshefeevlnseerfnsthnkflnlhteiaegglnLSQGERQL 1482
Cdd:cd03228 81 VPQDPFLFSGTIRENI--------------------------------------------------------LSGGQRQR 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 1483 LFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGE 1549
Cdd:cd03228 105 IAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1323-1571 |
6.86e-58 |
|
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: 200.15 E-value: 6.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAGTIKSNVdPY--DEYDEKKIFKALSQVNLissHEFeeVLNSEErfnsthnkflNLHTEIAEGGLNLSQGER 1480
Cdd:cd03251 81 VSQDVFLFNDTVAENI-AYgrPGATREEVEEAARAANA---HEF--IMELPE----------GYDTVIGERGVKLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1481 QLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELL 1560
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
250
....*....|.
gi 6321752 1561 KDErGIFYSMC 1571
Cdd:cd03251 225 AQG-GVYAKLH 234
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1321-1572 |
9.61e-58 |
|
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: 200.52 E-value: 9.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1321 GEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSI 1400
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAGTIKSNVDPYDEYDEKKIFKALsqvnlisshEFEEVLNSEERFNSthnkflNLHTEIAEGGLNLSQGER 1480
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEAL---------EIAQLKNMVKSLPG------GLDAVVTEGGENFSVGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1481 QLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELL 1560
Cdd:cd03288 163 QLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
250
....*....|..
gi 6321752 1561 KDERGIFYSMCR 1572
Cdd:cd03288 243 AQEDGVFASLVR 254
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1025-1570 |
1.85e-57 |
|
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: 209.96 E-value: 1.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1025 LKGMTDSSKNKHNAFYYLTV-YFLIGI--IQAMLGGFKTM-MTFLSGMRAS---RKIFNNLLDLvlhaQIRFFDVTPVGR 1097
Cdd:TIGR02203 37 LKPLLDDGFGGRDRSVLWWVpLVVIGLavLRGICSFVSTYlLSWVSNKVVRdirVRMFEKLLGL----PVSFFDRQPTGT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1098 IMNRFSKDIEGVDQELIPYLEVTIFcliQCASIIFLITVITPRFLTVAVIVFVLYFFVGkwyLTASRELKRLDSITK--- 1174
Cdd:TIGR02203 113 LLSRITFDSEQVASAATDAFIVLVR---ETLTVIGLFIVLLYYSWQLTLIVVVMLPVLS---ILMRRVSKRLRRISKeiq 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1175 ---SPIFQHFSETLVGVCTIRAFGDE----RRFilenmNKIDQNNRAFFYLSVTVKWFSFRVDMIGAFIVLASGSFILLN 1247
Cdd:TIGR02203 187 nsmGQVTTVAEETLQGYRVVKLFGGQayetRRF-----DAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1248 IANIDSGLAG---ISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYSSIEQEnylgHDEGRILLLNepswpKDGEIE 1324
Cdd:TIGR02203 262 QAQAGSLTAGdftAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE----KDTGTRAIER-----ARGDVE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1325 IENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIP 1404
Cdd:TIGR02203 333 FRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1405 QDPILFAGTIKSNVdPY---DEYDEKKIFKALSQVNLisshefEEVLNseerfnsthNKFLNLHTEIAEGGLNLSQGERQ 1481
Cdd:TIGR02203 413 QDVVLFNDTIANNI-AYgrtEQADRAEIERALAAAYA------QDFVD---------KLPLGLDTPIGENGVLLSGGQRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1482 LLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELLk 1561
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL- 555
|
570
....*....|..
gi 6321752 1562 DERGIF---YSM 1570
Cdd:TIGR02203 556 ARNGLYaqlHNM 567
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1063-1572 |
3.44e-57 |
|
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: 208.85 E-value: 3.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1063 TF--LSGMRAsrKIFNNLLDLVLHAQIRFFDvtpvGRIMNRFSKDIEGVDQElipYLEV---TIFCLIQCASIIFLITVI 1137
Cdd:COG4987 83 TLrlLADLRV--RLYRRLEPLAPAGLARLRS----GDLLNRLVADVDALDNL---YLRVllpLLVALLVILAAVAFLAFF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1138 TPRF-----LTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSpifqHFSETLVGVCTIRAFGDERRFiLENMNKIDQNN 1212
Cdd:COG4987 154 SPALalvlaLGLLLAGLLLPLLAARLGRRAGRRLAAARAALRA----RLTDLLQGAAELAAYGALDRA-LARLDAAEARL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1213 RAffyLSVTVKWFSFRVDMIGAFIVLASGSFILLnIANIDSGLAGISLTYAILFT-------DGALWLVRLYSTFEMNMN 1285
Cdd:COG4987 229 AA---AQRRLARLSALAQALLQLAAGLAVVAVLW-LAAPLVAAGALSGPLLALLVlaalalfEALAPLPAAAQHLGRVRA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1286 SVERLKEyssieqenyLGHDEGRILLLNEPSW-PKDGEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKS 1364
Cdd:COG4987 305 AARRLNE---------LLDAPPAVTEPAEPAPaPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1365 TIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNV---DPydEYDEKKIFKALSQVNLiss 1441
Cdd:COG4987 376 TLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGL--- 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1442 HEFEEVLNSeerfnsthnkflNLHTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDS-DHLIQGIIRSE 1520
Cdd:COG4987 451 GDWLAALPD------------GLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATeQALLADLLEAL 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 6321752 1521 FNKSTILtIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELLKDeRGIFYSMCR 1572
Cdd:COG4987 519 AGRTVLL-ITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ-NGRYRQLYQ 568
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
1022-1561 |
1.42e-56 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 207.25 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1022 TLPL--KGMTDSSKNKHNAfYYLTVYFLIGIIQAMLGGFKTMMTFLS----GMRAS----RKIFNNLLDLvlHAQirFFD 1091
Cdd:TIGR02204 36 SLPYavRLMIDHGFSKDSS-GLLNRYFAFLLVVALVLALGTAARFYLvtwlGERVVadirRAVFAHLISL--SPS--FFD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1092 VTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPRF--LTVAVIVFVLY--FFVGKWYLTASRELK 1167
Cdd:TIGR02204 111 KNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLtsLVLLAVPLVLLpiLLFGRRVRKLSRESQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1168 rlDSITKSPIFQhfSETLVGVCTIRAFGDErrfilenmnkidQNNRAFF------YLSVTVKWFSFRVDMIGAFIVLASG 1241
Cdd:TIGR02204 191 --DRIADAGSYA--GETLGAIRTVQAFGHE------------DAERSRFggavekAYEAARQRIRTRALLTAIVIVLVFG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1242 SFILLN-------IAN-IDSGLAGISLTYAILFTDGALWLVRLYSTFEMNMNSVERLKEYSSIEQEnylghdegrillLN 1313
Cdd:TIGR02204 255 AIVGVLwvgahdvIAGkMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPD------------IK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1314 EPSWPKD------GEIEIENLSLRYaPNLP--PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDG 1385
Cdd:TIGR02204 323 APAHPKTlpvplrGEIEFEQVNFAY-PARPdqPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1386 QDISKIDLVTLRRSITIIPQDPILFAGTIKSNV---DPyDEYDEKKIFKALSQVnlisSHEFEEVLnsEERFnsthnkfl 1462
Cdd:TIGR02204 402 VDLRQLDPAELRARMALVPQDPVLFAASVMENIrygRP-DATDEEVEAAARAAH----AHEFISAL--PEGY-------- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1463 nlHTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRI 1542
Cdd:TIGR02204 467 --DTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRI 544
|
570
....*....|....*....
gi 6321752 1543 IVMDAGEVKEYDRPSELLK 1561
Cdd:TIGR02204 545 VVMDQGRIVAQGTHAELIA 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1323-1570 |
2.14e-54 |
|
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: 190.06 E-value: 2.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYaPNLP--PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSI 1400
Cdd:cd03249 1 IEFKNVSFRY-PSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAGTIKSNV-----DPYDEYDEkkifKALSQVNLissHEFeeVLNSEERFNsthnkflnlhTEIAEGGLNL 1475
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDATDEEVE----EAAKKANI---HDF--IMSLPDGYD----------TLVGERGSQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1476 SQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDR 1555
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
250
....*....|....*
gi 6321752 1556 PSELLKdERGIFYSM 1570
Cdd:cd03249 221 HDELMA-QKGVYAKL 234
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
343-640 |
9.44e-54 |
|
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: 190.07 E-value: 9.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 343 LWVLVNSIVNLLPTILMKRFLEIVDNPNRSsscMNLAWLYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILIGEIYAK 422
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEP---LSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 423 GLRRRlftspktSSDSDSISAnlGTIINLISIDSFKVSELANYLYVTVQAVIMIIVVVGLLFNFLGVSAFAGISIILVMF 502
Cdd:cd18598 81 ALRVR-------SSSLSKFST--GEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 503 PLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSLLKKSLVWSVTSFLWFVTP 582
Cdd:cd18598 152 PINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTP 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 6321752 583 TLVTGVTFAICTFVQHeDLNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVSLKRI 640
Cdd:cd18598 232 VLISILTFATYVLMGN-TLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
340-640 |
3.78e-53 |
|
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: 188.43 E-value: 3.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 340 IGMLWVLVNSIVNLLPTILMKRFLEIVDN--PNRSSSCMNLAWLYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILIG 417
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDayLGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 418 EIYAKGLRrrlfTSPKTSSDSDSisanlGTIINLISIDSFKVSELANYLYVTVQAVIMIIVVVGLLFNFLGVSAFAGISI 497
Cdd:cd18597 81 AIYRKSLR----LSGKSRHEFPN-----GKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 498 ILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSLLKKSLVWSVTSFL 577
Cdd:cd18597 152 LILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 578 WFVTPTLVTGVTFAICTFVQHeDLNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVSLKRI 640
Cdd:cd18597 232 AFSLPVLASMLSFITYYATGH-TLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1319-1570 |
2.06e-52 |
|
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: 195.81 E-value: 2.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1319 KDGEIEIENLSLRYAPNlPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRR 1398
Cdd:COG5265 354 GGGEVRFENVSFGYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1399 SITIIPQDPILFAGTIKSNVdpydEY-----DEKKIFKALSQVNLissHEFEEVLnsEERFNsthnkflnlhTEIAEGGL 1473
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQI---HDFIESL--PDGYD----------TRVGERGL 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1474 NLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEY 1553
Cdd:COG5265 494 KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVER 573
|
250
....*....|....*..
gi 6321752 1554 DRPSELLKdERGIFYSM 1570
Cdd:COG5265 574 GTHAELLA-QGGLYAQM 589
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1323-1570 |
3.92e-51 |
|
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: 180.76 E-value: 3.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAGTIKSNVDPYDE-YDEKKIFKALSqvnLISSHEFeeVLNSEERFNsthnkflnlhTEIAEGGLNLSQGERQ 1481
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPgMSMERVIEAAK---LAGAHDF--ISELPEGYD----------TIVGEQGAGLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1482 LLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELLk 1561
Cdd:cd03252 146 RIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL- 224
|
....*....
gi 6321752 1562 DERGIFYSM 1570
Cdd:cd03252 225 AENGLYAYL 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1036-1570 |
3.73e-50 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 191.09 E-value: 3.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1036 HNAFYYLTvyfLIGIIQAMLGGFKT-MMTFLSGmRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELI 1114
Cdd:TIGR00958 201 ASAIFFMC---LLSIASSVSAGLRGgSFNYTMA-RINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1115 PYLEVTIFCLIQ-CASIIFLITViTPRFLTVAVIVFVLYFFV----GKWYLTASRELKrlDSITKSPifQHFSETLVGVC 1189
Cdd:TIGR00958 277 LNVNVLLRNLVMlLGLLGFMLWL-SPRLTMVTLINLPLVFLAekvfGKRYQLLSEELQ--EAVAKAN--QVAEEALSGMR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1190 TIRAFGDE----RRF--ILENMNKIDQNnRAFFYLSVTvkWFSFRVDMIGAFIVLASGSFILLNiANIDSGLAGISLTYA 1263
Cdd:TIGR00958 352 TVRSFAAEegeaSRFkeALEETLQLNKR-KALAYAGYL--WTTSVLGMLIQVLVLYYGGQLVLT-GKVSSGNLVSFLLYQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1264 ILFTDGALWLVRLYSTFEMNMNSVERLKEYssIEQENYLGHDEGRilllnEPSWPKdGEIEIENLSLRYaPNLP--PVIR 1341
Cdd:TIGR00958 428 EQLGEAVRVLSYVYSGMMQAVGASEKVFEY--LDRKPNIPLTGTL-----APLNLE-GLIEFQDVSFSY-PNRPdvPVLK 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1342 NVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNVdPY 1421
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENI-AY 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1422 --DEYDEKKIFKALSQVNlisSHEFeeVLNSEERFNsthnkflnlhTEIAEGGLNLSQGERQLLFIARSLLREPKIILLD 1499
Cdd:TIGR00958 578 glTDTPDEEIMAAAKAAN---AHDF--IMEFPNGYD----------TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILD 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1500 EATSSIDYDSDHLIQGIirSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELLKDErGIFYSM 1570
Cdd:TIGR00958 643 EATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ-GCYKHL 710
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1321-1550 |
5.03e-49 |
|
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: 173.93 E-value: 5.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1321 GEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSI 1400
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAGTIKSNVdpydeydekkifkALSQvnliSSHEFEEVLNSEERfnSTHNKFLNLH-----TEIAEGGLNL 1475
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNI-------------TLGA----PLADDERILRAAEL--AGVTDFVNKHpngldLQIGERGRGL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 1476 SQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEV 1550
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
383-640 |
1.25e-47 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 173.19 E-value: 1.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 383 IIGMFICRLTLAICNSQGQFVSDKICLRIRAILIGEIYAKGLRRRLFTSPktssdsdSISANLGTIINLISIDSFKVSEL 462
Cdd:cd18591 59 AVILFLALLLQATFSQASYHIVIREGIRLKTALQAMIYEKALRLSSWNLS-------SGSMTIGQITNHMSEDANNIMFF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 463 ---ANYLYVTVqavIMIIVVVGLLFNFLGVSAFAGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRI 539
Cdd:cd18591 132 fwlIHYLWAIP---LKIIVGLILLYLKLGVSALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 540 VKYFAWERNIINEIKSIRQKELRSLLKKSLVWSVTSFLWFVTPTLVTGVTFAICTFVQHEDLNAPLAFTTLSLFTLLKTP 619
Cdd:cd18591 209 LKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLMTFLTQASPILVTLVTFGLYPYLEGEPLTAAKAFSSLALFNQLTVP 288
|
250 260
....*....|....*....|.
gi 6321752 620 LDQLSNMLSFINQSKVSLKRI 640
Cdd:cd18591 289 LFIFPVVIPILINAVVSTRRL 309
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
328-903 |
4.51e-47 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 181.57 E-value: 4.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 328 LALFESFKTYLLIGMLWVLVNSIVNLLPTILMKRfleIVDN--PNRSsscMNLAWLYIIGMFI---CRLTLAICNSqgqF 402
Cdd:COG2274 148 LRLLRRYRRLLLQVLLASLLINLLALATPLFTQV---VIDRvlPNQD---LSTLWVLAIGLLLallFEGLLRLLRS---Y 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 403 VSDKICLRIRAILIGEIYAKGLRRRL--FTSPKTssdsdsisanlGTIINLI----SIDSFkvseLANYLYVTVQAVIMI 476
Cdd:COG2274 219 LLLRLGQRIDLRLSSRFFRHLLRLPLsfFESRSV-----------GDLASRFrdveSIREF----LTGSLLTALLDLLFV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 477 IVVVGLLFnFLGVSAFAgisIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLN----ECLQNIRIVKYFAWERNIINE 552
Cdd:COG2274 284 LIFLIVLF-FYSPPLAL---VVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQsllvETLRGIETIKALGAESRFRRR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 553 IKSIRQKELRSLLKKSLVWSVTSFLWFVTPTLVTGVTFAICTF-VQHEDLNAP--LAFTTLSLFTLlkTPLDQLSNMLSF 629
Cdd:COG2274 360 WENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYlVIDGQLTLGqlIAFNILSGRFL--APVAQLIGLLQR 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 630 INQSKVSLKRISDFLRMDDTEKYNQLTISPD--KNKIEFKNATLTWNENDSDMnafkLCGLNIKFQIGKLNLILGSTGSG 707
Cdd:COG2274 438 FQDAKIALERLDDILDLPPEREEGRSKLSLPrlKGDIELENVSFRYPGDSPPV----LDNISLTIKPGERVAIVGRSGSG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 708 KSALLLGLLGELNLISGSIIV-----PSLEPKHdlipdcegLTNSFAYCSQSAWLLNDTVKNNI-IFDNFYNEDRYNKVI 781
Cdd:COG2274 514 KSTLLKLLLGLYEPTSGRILIdgidlRQIDPAS--------LRRQIGVVLQDVFLFSGTIRENItLGDPDATDEEIIEAA 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 782 DACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENcITGpLMKNRTC 861
Cdd:COG2274 586 RLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRR-LLKGRTV 663
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 6321752 862 ILVTHNVSlTLRNAHFAIVLENGKVKNQGTITEL-QSKGLFKE 903
Cdd:COG2274 664 IIIAHRLS-TIRLADRIIVLDKGRIVEDGTHEELlARKGLYAE 705
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
980-1545 |
1.31e-46 |
|
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: 176.71 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 980 ALTALFALyITAqILFISQSWWIRHWVndtnVRINAPGFAMDTLplkgmtdssknkhnAFYYLTVyFLIGIIQAMLGGFK 1059
Cdd:TIGR02857 6 ALLALLGV-LGA-LLIIAQAWLLARVV----DGLISAGEPLAEL--------------LPALGAL-ALVLLLRALLGWLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1060 TMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIqcASIIFLItVITP 1139
Cdd:TIGR02857 65 ERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVI--VPLAILA-AVFP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1140 RFLTVAVIVFV----LYFF---VGkwYLTASRELKRLDSITKspIFQHFSETLVGVCTIRAFGDERRFIlENMNKIDQNN 1212
Cdd:TIGR02857 142 QDWISGLILLLtaplIPIFmilIG--WAAQAAARKQWAALSR--LSGHFLDRLRGLPTLKLFGRAKAQA-AAIRRSSEEY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1213 R---------AF-------FY--LSVTVKWFSFRVDMIGAFIVLASGSFILlnianidsglagisltyaILFTDGALWLV 1274
Cdd:TIGR02857 217 RertmrvlriAFlssavleLFatLSVALVAVYIGFRLLAGDLDLATGLFVL------------------LLAPEFYLPLR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1275 RLYSTFEMNMNSVERLKEYSSIEQENylghdeGRILLLNEPS-WPKDGEIEIENLSLRYaPNLPPVIRNVSFKVDPQSKI 1353
Cdd:TIGR02857 279 QLGAQYHARADGVAAAEALFAVLDAA------PRPLAGKAPVtAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1354 GIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNVDPYD-EYDEKKIFKA 1432
Cdd:TIGR02857 352 ALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREA 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1433 LSQVNLissHEFEEVLNseerfnsthnkfLNLHTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHL 1512
Cdd:TIGR02857 432 LERAGL---DEFVAALP------------QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAE 496
|
570 580 590
....*....|....*....|....*....|...
gi 6321752 1513 IQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVM 1545
Cdd:TIGR02857 497 VLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1321-1575 |
4.67e-46 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 176.30 E-value: 4.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1321 GEIEIENLSLRYaPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSI 1400
Cdd:PRK13657 333 GAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAGTIKSN--VDPYDEYDEkKIFKALSQVnliSSHEFeeVLNSEERFNsthnkflnlhTEIAEGGLNLSQG 1478
Cdd:PRK13657 412 AVVFQDAGLFNRSIEDNirVGRPDATDE-EMRAAAERA---QAHDF--IERKPDGYD----------TVVGERGRQLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1479 ERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSE 1558
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDE 555
|
250
....*....|....*..
gi 6321752 1559 LLkDERGIFYSMCRDSG 1575
Cdd:PRK13657 556 LV-ARGGRFAALLRAQG 571
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1321-1572 |
1.44e-43 |
|
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: 170.52 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1321 GEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTiitaLFRLL----EPITGCIKIDGQDISKIDLVTL 1396
Cdd:TIGR03797 450 GAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKST----LLRLLlgfeTPESGSVFYDGQDLAGLDVQAV 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1397 RRSITIIPQDPILFAGTIKSNVDPYDEYDEKKIFKALSQVNLisshefeevlnsEERFNSTHnkfLNLHTEIAEGGLNLS 1476
Cdd:TIGR03797 526 RRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGL------------AEDIRAMP---MGMHTVISEGGGTLS 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1477 QGERQLLFIARSLLREPKIILLDEATSSIDYDSdhliQGIIRSEFN--KSTILTIAHRLRSVIDYDRIIVMDAGEVKEYD 1554
Cdd:TIGR03797 591 GGQRQRLLIARALVRKPRILLFDEATSALDNRT----QAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQG 666
|
250
....*....|....*...
gi 6321752 1555 RPSELLKDErGIFYSMCR 1572
Cdd:TIGR03797 667 TYDELMARE-GLFAQLAR 683
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
664-884 |
3.33e-43 |
|
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: 157.11 E-value: 3.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDSdmnafKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKHDLIPDCEG 743
Cdd:cd03290 1 VQVTNGYFSWGSGLA-----TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 744 LTN-SFAYCSQSAWLLNDTVKNNIIFDNFYNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAV 822
Cdd:cd03290 76 RNRySVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 823 YSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKN-RTCILVTHNVSLtLRNAHFAIVLENG 884
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDkRTLVLVTHKLQY-LPHADWIIAMKDG 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1043-1570 |
1.47e-42 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 166.05 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1043 TVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDiegvdQELIPYLEVTIF 1122
Cdd:PRK10790 69 AAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTND-----TEVIRDLYVTVV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1123 -CLIQCASII--FLITVITP--RFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDE 1197
Cdd:PRK10790 144 aTVLRSAALIgaMLVAMFSLdwRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1198 RRFilenMNKIDQNNRAFFylsvTVKWFSFRVD---------MIGAFIVlaSGSFILLNIANidSGLAGISLTYAILFTD 1268
Cdd:PRK10790 224 ARF----GERMGEASRSHY----MARMQTLRLDgfllrpllsLFSALIL--CGLLMLFGFSA--SGTIEVGVLYAFISYL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1269 GAL--WLVRLYSTFEMNMNSV---ERLKEYSSIEQENYlGHDEgRILllnepswpKDGEIEIENLSLRYAPNlPPVIRNV 1343
Cdd:PRK10790 292 GRLnePLIELTTQQSMLQQAVvagERVFELMDGPRQQY-GNDD-RPL--------QSGRIDIDNVSFAYRDD-NLVLQNI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1344 SFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNVDPYDE 1423
Cdd:PRK10790 361 NLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1424 YDEKKIFKALSQVNLIS-SHEFEEvlnseerfnsthnkflNLHTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEAT 1502
Cdd:PRK10790 441 ISEEQVWQALETVQLAElARSLPD----------------GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321752 1503 SSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELLKdERGIFYSM 1570
Cdd:PRK10790 505 ANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA-AQGRYWQM 571
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1321-1589 |
1.38e-41 |
|
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: 154.63 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1321 GEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEpITGCIKIDGQDISKIDLVTLRRSI 1400
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAGTIKSNVDPYDEYDEKKIFKALSQVNLISshefeeVLnseERFNSthnkflNLHTEIAEGGLNLSQGER 1480
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKS------VI---EQFPG------QLDFVLVDGGCVLSHGHK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1481 QLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELL 1560
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
250 260
....*....|....*....|....*....
gi 6321752 1561 kDERGIFYSMCRDSGGLELLKQIAKQSSK 1589
Cdd:cd03289 225 -NEKSHFKQAISPSDRLKLFPRRNSSKSK 252
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
353-640 |
2.59e-41 |
|
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: 154.26 E-value: 2.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 353 LLPTILMKRFLEIVDNpnrSSSCMNLAWLYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILIGEIYAKGLRRRlftSP 432
Cdd:cd18592 15 IGPTILIRKLLEYLED---SDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLR---SL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 433 KTSSdsdsisanLGTIINLISIDSFKVSELANYLYVTVQAVIMIIVVVGLLFNFLGVSAFAGISIILVMFPLNFLLANLL 512
Cdd:cd18592 89 GDKS--------VGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 513 GKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSLLKKSLVWSVTSFLWFVTPTLVTGVTFAI 592
Cdd:cd18592 161 GKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6321752 593 CTFVQHeDLNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVSLKRI 640
Cdd:cd18592 241 HVALGN-DLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1323-1564 |
3.91e-41 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 151.72 E-value: 3.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYaPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPI--LFAGTIKSNVD--------PYDEYDEkKIFKALSQVNLisshefEEVLNSeerfnSTHnkflnlhteiaegg 1472
Cdd:COG1122 80 VFQNPDdqLFAPTVEEDVAfgpenlglPREEIRE-RVEEALELVGL------EHLADR-----PPH-------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1473 lNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS--TILTIAHRLRSVIDY-DRIIVMDAGE 1549
Cdd:COG1122 134 -ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLK-RLNKEgkTVIIVTHDLDLVAELaDRVIVLDDGR 211
|
250
....*....|....*
gi 6321752 1550 VKEYDRPSELLKDER 1564
Cdd:COG1122 212 IVADGTPREVFSDYE 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1323-1550 |
1.26e-40 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 148.13 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAGTIKSNVdpydeydekkifkalsqvnlisshefeevlnseerfnsthnkflnlhteiaegglnLSQGERQL 1482
Cdd:cd03246 81 LPQDDELFSGSIAENI--------------------------------------------------------LSGGQRQR 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 1483 LFIARSLLREPKIILLDEATSSIDYDSDHLI-QGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEV 1550
Cdd:cd03246 105 LGLARALYGNPRILVLDEPNSHLDVEGERALnQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1320-1550 |
2.02e-39 |
|
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: 146.85 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1320 DGEIEIENLSLRYaPNLP--PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLR 1397
Cdd:cd03248 9 KGIVKFQNVTFAY-PTRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1398 RSITIIPQDPILFAGTIKSNvdpydeydekkIFKALSQVnlisshEFEEVLNSEERFNsTHNKFLNL----HTEIAEGGL 1473
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDN-----------IAYGLQSC------SFECVKEAAQKAH-AHSFISELasgyDTEVGEKGS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 1474 NLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEV 1550
Cdd:cd03248 150 QLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1318-1572 |
6.04e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 154.60 E-value: 6.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1318 PKDGEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLR 1397
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1398 RSITIIPQDPILFAGTIKSNV---DPyDEYDEKKIfKALSQVNLisshefEEVLNSEERfnsthnkflnLHTEIAEGGLN 1474
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAP-NASDEALI-EVLQQVGL------EKLLEDDKG----------LNAWLGEGGRQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1475 LSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYD 1554
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQG 555
|
250
....*....|....*...
gi 6321752 1555 RPSELLKDErGIFYSMCR 1572
Cdd:PRK11160 556 THQELLAQQ-GRYYQLKQ 572
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
486-1567 |
8.82e-38 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 155.57 E-value: 8.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 486 FLGVSAFAGISI------------ILVMFPLNFL---LANLLGKFQKQT-LKCTDQRISKLNECLQNIRIVKYFAWERNI 549
Cdd:PTZ00265 179 FTYASAFLGLYIwslfknarltlcITCVFPLIYIcgvICNKKVKINKKTsLLYNNNTMSIIEEALVGIRTVVSYCGEKTI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 550 INEIKSIRQKELRSLLKKSLVWS-----VTSFL--------WFVTPTLVTGVTFAictfVQHEDLNAPLAFTTL-----S 611
Cdd:PTZ00265 259 LKKFNLSEKLYSKYILKANFMESlhigmINGFIlasyafgfWYGTRIIISDLSNQ----QPNNDFHGGSVISILlgvliS 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 612 LFTLLKTpldqLSNMLSFIN--QSKVSLKRISDflRMDDTEKYNQLTISPDKNKIEFKNATLTWNENdSDMNAFKlcGLN 689
Cdd:PTZ00265 335 MFMLTII----LPNITEYMKslEATNSLYEIIN--RKPLVENNDDGKKLKDIKKIQFKNVRFHYDTR-KDVEIYK--DLN 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 690 IKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKHDLipDCEGLTNSFAYCSQSAWLLNDTVKNNIIF- 768
Cdd:PTZ00265 406 FTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDI--NLKWWRSKIGVVSQDPLLFSNSIKNNIKYs 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 769 ----------DNFYNEDRYN-----------------------KVIDACGL---KRDLEILPAGDL-------------- 798
Cdd:PTZ00265 484 lyslkdlealSNYYNEDGNDsqenknkrnscrakcagdlndmsNTTDSNELiemRKNYQTIKDSEVvdvskkvlihdfvs 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 799 -------TEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSlT 871
Cdd:PTZ00265 564 alpdkyeTLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-T 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 872 LRNAHFAIVL----------------------------------------ENGKVKNQGT--ITELQSKGLFKEK----Y 905
Cdd:PTZ00265 643 IRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnNNNKINNAGSyiIEQGTHDALMKNKngiyY 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 906 V-----QLSSRDSINEKNAN--------RLKAPRKNDSQKIEPVTENINFDANFVNDGQLIEEEEKSNGA---------- 962
Cdd:PTZ00265 723 TminnqKVSSKKSSNNDNDKdsdmkssaYKDSERGYDPDEMNGNSKHENESASNKKSCKMSDENASENNAggklpflrnl 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 963 -----ISPDVYKW-YLKFFGGFKALTALFALYITAQILFisqswwirhwvndtnvrinaPGFAMDTLPLKG-MTDSSKNK 1035
Cdd:PTZ00265 803 fkrkpKAPNNLRIvYREIFSYKKDVTIIALSILVAGGLY--------------------PVFALLYAKYVStLFDFANLE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1036 HNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDV---TPvGRIMNRFSKDIEGVDQE 1112
Cdd:PTZ00265 863 ANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTG 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1113 LIPylEVTIFCLIqcaSIIFLITVITPRFL--TVAVIVFVLYF-----FVGKWYLTASRELKRL--------------DS 1171
Cdd:PTZ00265 942 LVN--NIVIFTHF---IVLFLVSMVMSFYFcpIVAAVLTGTYFifmrvFAIRARLTANKDVEKKeinqpgtvfaynsdDE 1016
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1172 ITKSPIFQhFSETLVGVCTIRAFGDERRFILENMNKIDQNNR----------AFFYLSVTVKWFsfrvdmIGAFIVLASG 1241
Cdd:PTZ00265 1017 IFKDPSFL-IQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKgqkrktlvnsMLWGFSQSAQLF------INSFAYWFGS 1089
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1242 SFILLNIANIDSGLAGIsltYAILFTDG-ALWLVRLYSTFEMNMNSVERLkeYSSIEQENYLG-HDEGRILLLNEPSWpk 1319
Cdd:PTZ00265 1090 FLIRRGTILVDDFMKSL---FTFLFTGSyAGKLMSLKGDSENAKLSFEKY--YPLIIRKSNIDvRDNGGIRIKNKNDI-- 1162
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1320 DGEIEIENLSLRYA--PNLPpVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLE---------------------- 1375
Cdd:PTZ00265 1163 KGKIEIMDVNFRYIsrPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqd 1241
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1376 --------------------------------PITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNVDPYDE 1423
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1321
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1424 YDEKKIFKALSQVNLISshEFEEvlnseerfnSTHNKFlnlHTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATS 1503
Cdd:PTZ00265 1322 DATREDVKRACKFAAID--EFIE---------SLPNKY---DTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1504 SIDYDSDHLIQGIIRSEFNKS--TILTIAHRLRSVIDYDRIIVMDAGE-----VKEYDRPSELLKDERGIF 1567
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVY 1458
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1323-1550 |
9.76e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.11 E-value: 9.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYapNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:COG4619 1 LELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAGTIKSNVD-PY----DEYDEKKIFKALSQVNLisSHEFeevlnseerfnsthnkflnLHTEIAEgglnLSQ 1477
Cdd:COG4619 79 VPQEPALWGGTVRDNLPfPFqlreRKFDRERALELLERLGL--PPDI-------------------LDKPVER----LSG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1478 GERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKS--TILTIAH------RLRsvidyDRIIVMDAGE 1549
Cdd:COG4619 134 GERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRVA-----DRVLTLEAGR 208
|
.
gi 6321752 1550 V 1550
Cdd:COG4619 209 L 209
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
660-920 |
1.59e-37 |
|
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: 143.07 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 660 DKNKIEFKNATLTWNENDSDMNAFKLCG------LNIKFQIGKLNLILGSTGSGKSALLLgllgelnlisgsIIVPSLEP 733
Cdd:cd03291 22 EKAKQENNDRKHSSDDNNLFFSNLCLVGapvlknINLKIEKGEMLAITGSTGSGKTSLLM------------LILGELEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 734 KHDLIPDceglTNSFAYCSQSAWLLNDTVKNNIIFDNFYNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQK 813
Cdd:cd03291 90 SEGKIKH----SGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 814 QRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITgPLMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTIT 893
Cdd:cd03291 166 ARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVC-KLMANKTRILVTSKME-HLKKADKILILHEGSSYFYGTFS 243
|
250 260
....*....|....*....|....*...
gi 6321752 894 ELQS-KGLFKEKYVQLSSRDSINEKNAN 920
Cdd:cd03291 244 ELQSlRPDFSSKLMGYDTFDQFSAERRN 271
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1068-1560 |
2.07e-37 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 150.17 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1068 MRASRKIFNNLLdlvlHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLeVTIfcLIQCASIIFLITV-------ITPR 1140
Cdd:PRK11176 98 MTMRRRLFGHMM----GMPVSFFDKQSTGTLLSRITYDSEQVASSSSGAL-ITV--VREGASIIGLFIMmfyyswqLSLI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1141 FLTVAVIVFVLYFFVGKWYLTASRELKR-LDSITKSPifqhfSETLVGVCTIRAFG----DERRFilenmNKIDQNNRAF 1215
Cdd:PRK11176 171 LIVIAPIVSIAIRVVSKRFRNISKNMQNtMGQVTTSA-----EQMLKGHKEVLIFGgqevETKRF-----DKVSNRMRQQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1216 FYLSVTVKWFSFRVDMIGAFIVLAsgsfILLNIANIDSGLAGISL-TYAILFTdGALWLVR-------LYSTFEMNMNSV 1287
Cdd:PRK11176 241 GMKMVSASSISDPIIQLIASLALA----FVLYAASFPSVMDTLTAgTITVVFS-SMIALMRplksltnVNAQFQRGMAAC 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1288 ERLKEYSSIEQENylghDEGRILLlnEPSwpkDGEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTII 1367
Cdd:PRK11176 316 QTLFAILDLEQEK----DEGKRVI--ERA---KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1368 TALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNVdPY---DEYDEKKIFKAlsqVNLISSHEF 1444
Cdd:PRK11176 387 NLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNI-AYartEQYSREQIEEA---ARMAYAMDF 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1445 EEVLNSeerfnsthnkflNLHTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIrSEFNKS 1524
Cdd:PRK11176 463 INKMDN------------GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL-DELQKN 529
|
490 500 510
....*....|....*....|....*....|....*..
gi 6321752 1525 -TILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELL 1560
Cdd:PRK11176 530 rTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1313-1572 |
2.36e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 146.91 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1313 NEPSWPKDGEIEIENLSLrYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLePITGCIKIDGQDISKID 1392
Cdd:PRK11174 340 KELASNDPVTIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1393 LVTLRRSITIIPQDPILFAGTIKSNV---DPydEYDEKKIFKALSQVNLissHEFEEVLNseerfnsthnkfLNLHTEIA 1469
Cdd:PRK11174 418 PESWRKHLSWVGQNPQLPHGTLRDNVllgNP--DASDEQLQQALENAWV---SEFLPLLP------------QGLDTPIG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1470 EGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGE 1549
Cdd:PRK11174 481 DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQ 560
|
250 260
....*....|....*....|...
gi 6321752 1550 VKEYDRPSELLKDErGIFYSMCR 1572
Cdd:PRK11174 561 IVQQGDYAELSQAG-GLFATLLA 582
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1324-1549 |
1.89e-35 |
|
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: 134.52 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1324 EIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITII 1403
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1404 PQDP--ILFAGTIKSNVdpydeydekkifkALSQVNL-ISSHEFEE-VLNSEERFNSTHNKFLNLHTeiaegglnLSQGE 1479
Cdd:cd03225 81 FQNPddQFFGPTVEEEV-------------AFGLENLgLPEEEIEErVEEALELVGLEGLRDRSPFT--------LSGGQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 1480 RQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS--TILTIAHRLRSVIDY-DRIIVMDAGE 1549
Cdd:cd03225 140 KQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEgkTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1323-1553 |
3.65e-35 |
|
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: 134.56 E-value: 3.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPV--IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTL---R 1397
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1398 RSITIIPQDPI-----------LFAGTIKSNVDPYDEYDEKKIFKALsqvnlissheFEEVLNSEERFNSthnkflnLHT 1466
Cdd:cd03257 82 KEIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARKEAVLLL----------LVGVGLPEEVLNR-------YPH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1467 EiaegglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGI---IRSEFNKsTILTIAHRLrSVIDY--DR 1541
Cdd:cd03257 145 E-------LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLlkkLQEELGL-TLLFITHDL-GVVAKiaDR 215
|
250
....*....|..
gi 6321752 1542 IIVMDAGEVKEY 1553
Cdd:cd03257 216 VAVMYAGKIVEE 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1318-1561 |
1.60e-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: 141.04 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1318 PKdGEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLR 1397
Cdd:COG4618 327 PK-GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1398 RSITIIPQDPILFAGTIKSNVDPYDEYDEKKIFKALSQVNLissHEFeevlnseerfnsthnkFLNL----HTEIAEGGL 1473
Cdd:COG4618 406 RHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGV---HEM----------------ILRLpdgyDTRIGEGGA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1474 NLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSD-HLIQGIIRSEFNKSTILTIAHR---LRSVidyDRIIVMDAGE 1549
Cdd:COG4618 467 RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEaALAAAIRALKARGATVVVITHRpslLAAV---DKLLVLRDGR 543
|
250
....*....|..
gi 6321752 1550 VKEYDRPSELLK 1561
Cdd:COG4618 544 VQAFGPRDEVLA 555
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
379-640 |
2.74e-34 |
|
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: 133.91 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 379 AWLYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILIGEIYAKGLRRrlftspkTSSDSDSISAnlGTIINLISIDSFK 458
Cdd:cd18594 38 AYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKL-------SSSALSKITT--GHIVNLLSNDVQK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 459 VSELANYLYVTVQAVIMIIVVVGLLFNFLGVSAFAGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIR 538
Cdd:cd18594 109 FDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 539 IVKYFAWERNIINEIKSIRQKELRSLLKKSLVWSVTSFLWFVTPTLVTGVTFAICTFVQHEdLNAPLAFTTLSLFTLLKT 618
Cdd:cd18594 189 VIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNT-LTARKVFTVISLLNALRM 267
|
250 260
....*....|....*....|...
gi 6321752 619 PLD-QLSNMLSFINQSKVSLKRI 640
Cdd:cd18594 268 TITrFFPESIQTLSESRVSLKRI 290
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1323-1564 |
1.68e-33 |
|
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: 130.55 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPIL-FAGTI-----------KSNVDPYDEYDEKKIFKALSQVNLissHEFeevlnSEERFNSthnkflnlhteiae 1470
Cdd:COG1120 80 VPQEPPApFGLTVrelvalgryphLGLFGRPSAEDREAVEEALERTGL---EHL-----ADRPVDE-------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1471 gglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS---EFNKSTILTIaHRLRSVIDY-DRIIVMD 1546
Cdd:COG1120 138 ----LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlarERGRTVVMVL-HDLNLAARYaDRLVLLK 212
|
250
....*....|....*...
gi 6321752 1547 AGEVKEYDRPSELLKDER 1564
Cdd:COG1120 213 DGRIVAQGPPEEVLTPEL 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1324-1550 |
3.76e-33 |
|
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: 126.78 E-value: 3.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1324 EIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITII 1403
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1404 PQdpilfagtiksnvdpydeydekkifkALSQVNLisshefeEVLnSEERFNSthnkflnlhteiaegglnLSQGERQLL 1483
Cdd:cd03214 79 PQ--------------------------ALELLGL-------AHL-ADRPFNE------------------LSGGERQRV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1484 FIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS---EFNKSTILTIaHRLRSVIDY-DRIIVMDAGEV 1550
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRlarERGKTVVMVL-HDLNLAARYaDRVILLKDGRI 176
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1324-1549 |
1.10e-32 |
|
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: 124.66 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1324 EIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITII 1403
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1404 PQdpilfagtiksnvdpydeydekkifkalsqvnlisshefeevlnseerfnsthnkflnlhteiaegglnLSQGERQLL 1483
Cdd:cd00267 79 PQ---------------------------------------------------------------------LSGGQRQRV 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321752 1484 FIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNK-STILTIAHRLRSVIDY-DRIIVMDAGE 1549
Cdd:cd00267 90 ALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
1039-1294 |
2.12e-32 |
|
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: 128.49 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1039 FYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDqELIPYLE 1118
Cdd:cd18559 38 QVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVD-SMAPQVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1119 VTIFCLIQCA-SIIFLITVITPRFLtVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDE 1197
Cdd:cd18559 117 KMWMGPLQNViGLYLLILLAGPMAA-VGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1198 RRFIlENMNKIDQNNRAFFYLSVTVKWFSFRVDMIGAFIVLASgSFILLNIANIDSGLAGISLTYAILFTDGALWLVRLY 1277
Cdd:cd18559 196 EAFI-RQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFA-SFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMS 273
|
250
....*....|....*..
gi 6321752 1278 STFEMNMNSVERLKEYS 1294
Cdd:cd18559 274 PEVITNIVAAEVSLERS 290
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1323-1564 |
2.25e-32 |
|
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: 133.88 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRY---APNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKI---DLVTL 1396
Cdd:COG1123 261 LEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1397 RRSITIIPQDP-------------ILFAGTIKSNVDPydEYDEKKIFKALSQVNLISSHefeevlnsEERFnsthnkfln 1463
Cdd:COG1123 341 RRRVQMVFQDPysslnprmtvgdiIAEPLRLHGLLSR--AERRERVAELLERVGLPPDL--------ADRY--------- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1464 lhteIAEgglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYdsdhLIQGII-------RSEFNKsTILTIAHRLRSV 1536
Cdd:COG1123 402 ----PHE----LSGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQIlnllrdlQRELGL-TYLFISHDLAVV 468
|
250 260
....*....|....*....|....*....
gi 6321752 1537 IDY-DRIIVMDAGEVKEYDRPSELLKDER 1564
Cdd:COG1123 469 RYIaDRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
663-899 |
4.30e-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: 125.80 E-value: 4.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 663 KIEFKNATLTWNENDSdmnafKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVpslepkhDLIP--- 739
Cdd:cd03254 2 EIEFENVNFSYDEKKP-----VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI-------DGIDird 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 740 -DCEGLTNSFAYCSQSAWLLNDTVKNNIIFDNFYNEDryNKVIDAC---GLKRDLEILPAGDLTEIGEKGITLSGGQKQR 815
Cdd:cd03254 70 iSRKSLRSMIGVVLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAkeaGAHDFIMKLPNGYDTVLGENGGNLSQGERQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 816 ISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENciTGPLMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITEL 895
Cdd:cd03254 148 LAIARAMLRDPKILILDEATSNIDTETEKLIQEA--LEKLMKGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDEL 224
|
....
gi 6321752 896 QSKG 899
Cdd:cd03254 225 LAKK 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1323-1562 |
7.80e-32 |
|
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: 125.69 E-value: 7.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRY--APNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSI 1400
Cdd:COG1124 2 LEVRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPIlfagtikSNVDPYdeydeKKIFKALSqvnlisshefeEVLnseerfnsTHNKFLNLHTEIAEG----GLN-- 1474
Cdd:COG1124 82 QMVFQDPY-------ASLHPR-----HTVDRILA-----------EPL--------RIHGLPDREERIAELleqvGLPps 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1475 --------LSQGERQLLFIARSLLREPKIILLDEATSSIDYdsdhLIQGII-------RSEFNkSTILTIAHRLRsVIDY 1539
Cdd:COG1124 131 fldryphqLSGGQRQRVAIARALILEPELLLLDEPTSALDV----SVQAEIlnllkdlREERG-LTYLFVSHDLA-VVAH 204
|
250 260
....*....|....*....|....*
gi 6321752 1540 --DRIIVMDAGEVKEYDRPSELLKD 1562
Cdd:COG1124 205 lcDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
340-640 |
1.28e-31 |
|
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: 126.18 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 340 IGMLWVLVNSIVNLLPTILMKRFLEIVDNPNRSSSCMNlAWLYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILIGEI 419
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSSISLTE-AYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 420 YAKGLRRRLFTSPKTSSdsdsisanlGTIINLISIDSFKVSELA---NYLYVtvqAVIMIIVVVGLLFNFLGVSAFAGIS 496
Cdd:cd18593 80 YRKALRLSQAALGKTTV---------GQIVNLLSNDVNRFDQAVlflHYLWV---APLQLIAVIYILWFEIGWSCLAGLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 497 IILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSLLKKSLVWSVTSF 576
Cdd:cd18593 148 VLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMG 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 577 LWFVTPTLVTGVTFAICTFVQhEDLNAPLAFTTLSLFTLLKTPLDQ-LSNMLSFINQSKVSLKRI 640
Cdd:cd18593 228 LFFVSSKLILFLTFLAYILLG-NILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1096-1533 |
1.48e-31 |
|
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: 131.33 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1096 GRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPRFLTVAVIVFVLYFFVGKWYL-----TASRELKRLd 1170
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSlraarAAEQALARL- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1171 sitKSPIFQHFSETLVGVCTIRAFGDERRFIlenmNKIDQNNRAFFYLSVTVKWFsfrvDMIG-AFIVLASGSFILLNI- 1248
Cdd:TIGR02868 189 ---RGELAAQLTDALDGAAELVASGALPAAL----AQVEEADRELTRAERRAAAA----TALGaALTLLAAGLAVLGALw 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1249 ----ANIDSGLAGISLTYAIL-----------FTDGALWLVRLystfemnMNSVERLKEYSSIEQENYLGHDEGrilllN 1313
Cdd:TIGR02868 258 aggpAVADGRLAPVTLAVLVLlplaafeafaaLPAAAQQLTRV-------RAAAERIVEVLDAAGPVAEGSAPA-----A 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1314 EPSWPKDGEIEIENLSLRYAPNlPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDL 1393
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1394 VTLRRSITIIPQDPILFAGTIKSNV-----DPYDEydekKIFKALSQVNLissHEFEEVLNSeerfnsthnkflNLHTEI 1468
Cdd:TIGR02868 405 DEVRRRVSVCAQDAHLFDTTVRENLrlarpDATDE----ELWAALERVGL---ADWLRALPD------------GLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 1469 AEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYD-SDHLIQGIIRSEFNKSTILtIAHRL 1533
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGRTVVL-ITHHL 530
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1323-1559 |
3.16e-31 |
|
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: 123.06 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLE-----PITGCIKIDGQDI--SKIDLVT 1395
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1396 LRRSITIIPQDPILFAGTIKSNVD---PYDEYDEKKIFKALSQVNLISSHEFEEVLNseerfnsthnkflNLHteiaegG 1472
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglRLHGIKLKEELDERVEEALRKAALWDEVKD-------------RLH------A 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1473 LNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS-TILTIAHRLRSVIDY-DRIIVMDAGEV 1550
Cdd:cd03260 140 LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIA-ELKKEyTIVIVTHNMQQAARVaDRTAFLLNGRL 218
|
....*....
gi 6321752 1551 KEYDRPSEL 1559
Cdd:cd03260 219 VEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1323-1565 |
4.31e-31 |
|
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: 130.02 E-value: 4.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEP---ITGCIKIDGQDISKIDLVTLRRS 1399
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQDPilfagtiKSNVDPYDEYDEkkIFKALSQVNLISSHEFEEVLNSEERFNSTHNKFLNLHTeiaegglnLSQGE 1479
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVTVGDQ--IAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQ--------LSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1480 RQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS---EFNKsTILTIAHRLRSVIDY-DRIIVMDAGEVKEYDR 1555
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqrERGT-TVLLITHDLGVVAEIaDRVVVMDDGRIVEDGP 226
|
250
....*....|
gi 6321752 1556 PSELLKDERG 1565
Cdd:COG1123 227 PEEILAAPQA 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1323-1561 |
9.38e-31 |
|
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: 122.27 E-value: 9.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYapNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKiDLVTLRRSITI 1402
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAG-TIKSNVdpydeydekKIFKALSQVNLISSHE-FEEVLnseerfnsthnKFLNLhTEIAEGGL-NLSQGE 1479
Cdd:COG4555 79 LPDERGLYDRlTVRENI---------RYFAELYGLFDEELKKrIEELI-----------ELLGL-EEFLDRRVgELSTGM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1480 RQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS--EFNKSTILT--IAHRLRSVIdyDRIIVMDAGEVKEYDR 1555
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAlkKEGKTVLFSshIMQEVEALC--DRVVILHKGKVVAQGS 215
|
....*.
gi 6321752 1556 PSELLK 1561
Cdd:COG4555 216 LDELRE 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1323-1552 |
1.45e-30 |
|
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: 119.34 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDlVTLRRSITI 1402
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAGTIKSNVdpydeydekkifkalsqvnlisshefeevlnseerfnsthnkflnlhteiaegGLNLSQGERQL 1482
Cdd:cd03247 80 LNQRPYLFDTTLRNNL-----------------------------------------------------GRRFSGGERQR 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1483 LFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKE 1552
Cdd:cd03247 107 LALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
472-903 |
1.97e-30 |
|
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: 128.73 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 472 AVIMIIVVVGLLFNF---LGVSAFAGISIILVMFPLnflLANLLGKFQKQTLKCTDQRI-SKLNECLQNIRIVKYF-AWE 546
Cdd:COG4987 139 ALLVILAAVAFLAFFspaLALVLALGLLLAGLLLPL---LAARLGRRAGRRLAAARAALrARLTDLLQGAAELAAYgALD 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 547 RniinEIKSIRQ--KELRSLLKKS--LVWSVTSFLWFVTPTLVTGVTFAICTFVQHEDLNAP----LAFTTLSLFTllkt 618
Cdd:COG4987 216 R----ALARLDAaeARLAAAQRRLarLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPllalLVLAALALFE---- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 619 PLDQLSNMLSFINQSKVSLKRISDFLRMDDTEKY-NQLTISPDKNKIEFKNATLTWNENDSDmnAFKlcGLNIKFQIGKL 697
Cdd:COG4987 288 ALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEpAEPAPAPGGPSLELEDVSFRYPGAGRP--VLD--GLSLTLPPGER 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 698 NLILGSTGSGKSALLLGLLGELNLISGSIivpSL--EPKHDLIPDCegLTNSFAYCSQSAWLLNDTVKNNI-IFDNFYNE 774
Cdd:COG4987 364 VAIVGPSGSGKSTLLALLLRFLDPQSGSI---TLggVDLRDLDEDD--LRRRIAVVPQRPHLFDTTLRENLrLARPDATD 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 775 DRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITgp 854
Cdd:COG4987 439 EELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-- 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 6321752 855 LMKNRTCILVTHNVSLtLRNAHFAIVLENGKVKNQGTITEL-QSKGLFKE 903
Cdd:COG4987 517 ALAGRTVLLITHRLAG-LERMDRILVLEDGRIVEQGTHEELlAQNGRYRQ 565
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1340-1503 |
2.77e-30 |
|
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: 117.75 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1340 IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAG-TIKSNV 1418
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1419 -------DPYDEYDEKKIFKALSQVNLIsshefeevlnseerfnsthnkfLNLHTEIAEGGLNLSQGERQLLFIARSLLR 1491
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLG----------------------DLADRPVGERPGTLSGGQRQRVAIARALLT 138
|
170
....*....|..
gi 6321752 1492 EPKIILLDEATS 1503
Cdd:pfam00005 139 KPKLLLLDEPTA 150
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
402-899 |
2.88e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 129.46 E-value: 2.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 402 FVSDKICLRIRailiGEIYAKGLRRRL--FTSPKTssdsdsisanlGTIINLISIDSFKVSE-LANYLYVTVQAVIMiiV 478
Cdd:TIGR00958 227 YTMARINLRIR----EDLFRSLLRQDLgfFDENKT-----------GELTSRLSSDTQTMSRsLSLNVNVLLRNLVM--L 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 479 VVGLLFNFLGVSAFAGISIILVmfPLNFLLANLLGKFQKQTLKCTDQRISKLN----ECLQNIRIVKYFAWE-------R 547
Cdd:TIGR00958 290 LGLLGFMLWLSPRLTMVTLINL--PLVFLAEKVFGKRYQLLSEELQEAVAKANqvaeEALSGMRTVRSFAAEegeasrfK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 548 NIINEIKSIRQKELRSLLKKSLVWSVTSFLWFVTpTLVTGVTFAICTFVQHEDLnaplafTTLSLFTL-LKTPLDQLSNM 626
Cdd:TIGR00958 368 EALEETLQLNKRKALAYAGYLWTTSVLGMLIQVL-VLYYGGQLVLTGKVSSGNL------VSFLLYQEqLGEAVRVLSYV 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 627 LSFINQSKVSLKRISDFL-RMDDTEKYNQLTISPDKNKIEFKNATLTWnENDSDMNAFKlcGLNIKFQIGKLNLILGSTG 705
Cdd:TIGR00958 441 YSGMMQAVGASEKVFEYLdRKPNIPLTGTLAPLNLEGLIEFQDVSFSY-PNRPDVPVLK--GLTFTLHPGEVVALVGPSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 706 SGKSALLLGLLGELNLISGSIIVPSlEPKHDLipDCEGLTNSFAYCSQSAWLLNDTVKNNIIFD-NFYNEDRYNKVIDAC 784
Cdd:TIGR00958 518 SGKSTVAALLQNLYQPTGGQVLLDG-VPLVQY--DHHYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAA 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 785 GLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENcitgPLMKNRTCILV 864
Cdd:TIGR00958 595 NAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES----RSRASRTVLLI 670
|
490 500 510
....*....|....*....|....*....|....*
gi 6321752 865 THNVSlTLRNAHFAIVLENGKVKNQGTITELQSKG 899
Cdd:TIGR00958 671 AHRLS-TVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1323-1563 |
2.95e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.96 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKidlvtLRRSITI 1402
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQdpilfagtiKSNVDP-----------------------YDEYDEKKIFKALSQVNLissHEFEevlnseerfnsthn 1459
Cdd:COG1121 80 VPQ---------RAEVDWdfpitvrdvvlmgrygrrglfrrPSRADREAVDEALERVGL---EDLA-------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1460 kflnlHTEIAEgglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS--TILTIAHRLRSVI 1537
Cdd:COG1121 134 -----DRPIGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRREgkTILVVTHDLGAVR 203
|
250 260
....*....|....*....|....*..
gi 6321752 1538 DY-DRIIVMDaGEVKEYDRPSELLKDE 1563
Cdd:COG1121 204 EYfDRVLLLN-RGLVAHGPPEEVLTPE 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
321-899 |
1.82e-29 |
|
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: 125.64 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 321 KHINNLTLALFESFKTYLLIGMLWVLVNSIVNLLPTILMKRFLE--IVDNPNRSSscmnlAWLYIIGMFICRLTLAICNS 398
Cdd:COG4988 2 KPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAglIIGGAPLSA-----LLPLLGLLLAVLLLRALLAW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 399 QGQFVSDKICLRIRAILIGEIYAKGLRRRLFTSPKTSSdsdsisanlGTIINLI-----SIDSFkvseLANYLYVTVQAV 473
Cdd:COG4988 77 LRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKST---------GELATLLtegveALDGY----FARYLPQLFLAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 474 IMIIVVVGLLFnflGVSAFAGIsIILVMFPLNFLLANLLGKFQKQTlkcTDQRISKLN-------ECLQNIRIVKYF--- 543
Cdd:COG4988 144 LVPLLILVAVF---PLDWLSGL-ILLVTAPLIPLFMILVGKGAAKA---SRRQWRALArlsghflDRLRGLTTLKLFgra 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 544 AWERNIINEI-KSIRQKELRsLLKKSLVWS-VTSFLWFVTPTLV---TGVTFaictfvqhedLNAPLAFTTLsLFTLLKT 618
Cdd:COG4988 217 KAEAERIAEAsEDFRKRTMK-VLRVAFLSSaVLEFFASLSIALVavyIGFRL----------LGGSLTLFAA-LFVLLLA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 619 -----PLDQLSN-----MlsfinQSKVSLKRISDFLRMDDTEKYNQLTISPDKNK--IEFKNATLTWnenDSDMNAfkLC 686
Cdd:COG4988 285 pefflPLRDLGSfyharA-----NGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPpsIELEDVSFSY---PGGRPA--LD 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 687 GLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVpSLEPKHDLIPDceGLTNSFAYCSQSAWLLNDTVKNNI 766
Cdd:COG4988 355 GLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI-NGVDLSDLDPA--SWRRQIAWVPQNPYLFAGTIRENL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 767 IFDNF-YNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVW 845
Cdd:COG4988 432 RLGRPdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAE 511
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 6321752 846 IYEncITGPLMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITELQSKG 899
Cdd:COG4988 512 ILQ--ALRRLAKGRTVILITHRLA-LLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
664-903 |
3.85e-29 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 117.26 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENdSDMNAFKlcGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKhDLipDCEG 743
Cdd:cd03249 1 IEFKNVSFRYPSR-PDVPILK--GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIR-DL--NLRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 744 LTNSFAYCSQSAWLLNDTVKNNIIFDNFYNEDryNKVIDACglkRDLEI------LPAGDLTEIGEKGITLSGGQKQRIS 817
Cdd:cd03249 75 LRSQIGLVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAA---KKANIhdfimsLPDGYDTLVGERGSQLSGGQKQRIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 818 LARAVYSSAKHVLLDDCLSAVDSHTAVWIYENciTGPLMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITEL-Q 896
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEA--LDRAMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELmA 226
|
....*..
gi 6321752 897 SKGLFKE 903
Cdd:cd03249 227 QKGVYAK 233
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1285-1560 |
4.12e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 124.44 E-value: 4.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1285 NSVER-LKEYSSIEQenylghdegrilLLNEPSWPKDGE---------IEIENLSLRYAPNLPPVIRNVSFKVDPQSKIG 1354
Cdd:PRK10789 278 NIVERgSAAYSRIRA------------MLAEAPVVKDGSepvpegrgeLDVNIRQFTYPQTDHPALENVNFTLKPGQMLG 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1355 IVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNVdpydeydekkifkALS 1434
Cdd:PRK10789 346 ICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI-------------ALG 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1435 QVNlISSHEFEEVlnseERFNSTHNKFLNL----HTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSD 1510
Cdd:PRK10789 413 RPD-ATQQEIEHV----ARLASVHDDILRLpqgyDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE 487
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6321752 1511 HLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELL 1560
Cdd:PRK10789 488 HQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
664-899 |
4.30e-29 |
|
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: 116.95 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDSdmNAFKlcglNIKFQI--GKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSlepkHDlIPDC 741
Cdd:cd03251 1 VEFKNVTFRYPGDGP--PVLR----DISLDIpaGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG----HD-VRDY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 742 E--GLTNSFAYCSQSAWLLNDTVKNNIIFDNFyNEDRyNKVIDACGLKRDLEI---LPAGDLTEIGEKGITLSGGQKQRI 816
Cdd:cd03251 70 TlaSLRRQIGLVSQDVFLFNDTVAENIAYGRP-GATR-EEVEEAARAANAHEFimeLPEGYDTVIGERGVKLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 817 SLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENciTGPLMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITELQ 896
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAA--LERLMKNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
...
gi 6321752 897 SKG 899
Cdd:cd03251 225 AQG 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1319-1564 |
4.90e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.17 E-value: 4.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1319 KDGEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRR 1398
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1399 SITIIPQDP------------ILFaGTIKSNVDPydEYDEKKIFKALSQVNLisshefEEVLNSEErfnsthnkflnlht 1466
Cdd:PRK13632 84 KIGIIFQNPdnqfigatveddIAF-GLENKKVPP--KKMKDIIDDLAKKVGM------EDYLDKEP-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1467 eiaeggLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS--EFNKSTILTIAHRLRSVIDYDRIIV 1544
Cdd:PRK13632 141 ------QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIV 214
|
250 260
....*....|....*....|
gi 6321752 1545 MDAGEVKEYDRPSELLKDER 1564
Cdd:PRK13632 215 FSEGKLIAQGKPKEILNNKE 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1323-1561 |
9.54e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 116.32 E-value: 9.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKiDLVTLRRSITI 1402
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAG-TIKSNVDpydeydekkIFKALSQVNLISSHE-FEEVLnseERFNSTHNKflnlHTEIAegglNLSQGER 1480
Cdd:COG1131 78 VPQEPALYPDlTVRENLR---------FFARLYGLPRKEARErIDELL---ELFGLTDAA----DRKVG----TLSGGMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1481 QLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNK-STILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPSE 1558
Cdd:COG1131 138 QRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDE 217
|
...
gi 6321752 1559 LLK 1561
Cdd:COG1131 218 LKA 220
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
381-640 |
2.53e-28 |
|
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: 116.55 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 381 LYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILIGEIYAKGLRrrlftspktSSDSDSISANLGTIINLISIDSFKVS 460
Cdd:cd18559 39 VYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALR---------SPISFFERTPSGELVNLFSKDLDRVD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 461 ELANYLYVTVQAVIMIIVVVGLLFNFLGVSAFAGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIV 540
Cdd:cd18559 110 SMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 541 KYFAWERNIINEIKSIRQKELRSLLKKSLVWSVTSFLWFVTPTLVTGVTFAICTFVQHED-LNAPLAFTTLSLFTLLKTP 619
Cdd:cd18559 190 KAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLAgLVALKVFYSLALTTYLNWP 269
|
250 260
....*....|....*....|.
gi 6321752 620 LDQLSNMLSFINQSKVSLKRI 640
Cdd:cd18559 270 LNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1323-1564 |
2.96e-28 |
|
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: 114.97 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYaPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKI---DLVTLRRS 1399
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQDP-----------ILFA-----GTIKSNVDPYDEYDEKKIFKALSQVNLISSHefeevlnseerfnsthnkfln 1463
Cdd:cd03256 80 IGMIFQQFnlierlsvlenVLSGrlgrrSTWRSLFGLFPKEEKQRALAALERVGLLDKA--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1464 lHTEIAEgglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS---EFNKSTILTIaHRLRSVIDY- 1539
Cdd:cd03256 139 -YQRADQ----LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinrEEGITVIVSL-HQVDLAREYa 212
|
250 260
....*....|....*....|....*
gi 6321752 1540 DRIIVMDAGEVKeYDRPSELLKDER 1564
Cdd:cd03256 213 DRIVGLKDGRIV-FDGPPAELTDEV 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1323-1560 |
3.16e-28 |
|
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: 114.60 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLP--PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITaLFRLLE-PITGCIKIDGQDI---SKIDLVTL 1396
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLErPTSGSVLVDGTDLtllSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1397 RRSITIIPQDPILFAG-TIKSNVD-PY------DEYDEKKIFKALSQVNLisSHEfeevlnsEERFNSthnkflnlhtei 1468
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGL--EDK-------ADAYPA------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1469 aegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS---TILTIAHRLRSVIDY-DRIIV 1544
Cdd:cd03258 140 -----QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLR-DINRElglTIVLITHEMEVVKRIcDRVAV 213
|
250
....*....|....*.
gi 6321752 1545 MDAGEVKEYDRPSELL 1560
Cdd:cd03258 214 MEKGEVVEEGTVEEVF 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1324-1546 |
5.34e-28 |
|
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: 113.40 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1324 EIENLSLRYapNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIdlvtlRRSITII 1403
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1404 PQ----D---PILFAGTIKSNVDP-------YDEYDEKKIFKALSQVNLisshefeevlnseerfnsthNKFLNLHteIA 1469
Cdd:cd03235 74 PQrrsiDrdfPISVRDVVLMGLYGhkglfrrLSKADKAKVDEALERVGL--------------------SELADRQ--IG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1470 EgglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS--TILTIAHRLRSVIDY-DRIIVMD 1546
Cdd:cd03235 132 E----LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR-ELRREgmTILVVTHDLGLVLEYfDRVLLLN 206
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
664-903 |
1.35e-27 |
|
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: 112.71 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENdsdmnAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSlepkHDLIP-DCE 742
Cdd:cd03253 1 IEFENVTFAYDPG-----RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG----QDIREvTLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 743 GLTNSFAYCSQSAWLLNDTVKNNIIF--DNFYNEDrynkVIDAC---GLKRDLEILPAGDLTEIGEKGITLSGGQKQRIS 817
Cdd:cd03253 72 SLRRAIGVVPQDTVLFNDTIGYNIRYgrPDATDEE----VIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 818 LARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITgpLMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITEL-Q 896
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRD--VSKGRTTIVIAHRLS-TIVNADKIIVLKDGRIVERGTHEELlA 224
|
....*..
gi 6321752 897 SKGLFKE 903
Cdd:cd03253 225 KGGLYAE 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1323-1550 |
3.21e-27 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 109.79 E-value: 3.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKiDLVTLRRSITI 1402
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILfagtiksnvdpYDEYdekkifkalsqvnliSSHEFeevlnseerfnsthnkflnlhteiaeggLNLSQGERQL 1482
Cdd:cd03230 78 LPEEPSL-----------YENL---------------TVREN----------------------------LKLSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1483 LFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS--TILTIAHRLRSVIDY-DRIIVMDAGEV 1550
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLR-ELKKEgkTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
981-1267 |
3.58e-27 |
|
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: 112.74 E-value: 3.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 981 LTALFALYITAQILFISQSWWIRHWVNDtnvrinapgfamdtlplkGMTDSSKNKHNAFYYLTVYFLIGIIQAMLGGFKT 1060
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDV------------------LLPDGDPETQALNVYSLALLLLGLAQFILSFLQS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1061 MMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPR 1140
Cdd:pfam00664 63 YLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1141 FLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRFILENMNKIDQNNRAFFYLSV 1220
Cdd:pfam00664 143 LTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAV 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6321752 1221 TVKWFSFRVDMIGAFIVLASGSF-ILLNIAN-IDSGLAGISLTYAILFT 1267
Cdd:pfam00664 223 ANGLSFGITQFIGYLSYALALWFgAYLVISGeLSVGDLVAFLSLFAQLF 271
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1323-1558 |
1.14e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 109.76 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYaPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKI---DLVTLRRS 1399
Cdd:COG2884 2 IRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQD-PILFAGTIKSNVD--------PYDEYdEKKIFKALSQVNLisshefeevLNSEERFNSThnkflnlhteiae 1470
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENVAlplrvtgkSRKEI-RRRVREVLDLVGL---------SDKAKALPHE------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1471 gglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDsdhLIQGIIR--SEFNKS--TILtIA-HRLRSVIDYD-RIIV 1544
Cdd:COG2884 138 ----LSGGEQQRVAIARALVNRPELLLADEPTGNLDPE---TSWEIMEllEEINRRgtTVL-IAtHDLELVDRMPkRVLE 209
|
250
....*....|....
gi 6321752 1545 MDAGEVKEYDRPSE 1558
Cdd:COG2884 210 LEDGRLVRDEARGV 223
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
969-1290 |
1.39e-26 |
|
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: 112.59 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 969 KW--YLKFFGGFKALtalfaLYITAQILFISQSWWIRHWVNDTNVRINAPGFAMDTLPLKGMTDSSKNKHNAFYYLtVYF 1046
Cdd:cd18600 2 TWntYLRYITSHKSL-----IFVLILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSSYYV-FYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1047 LIGIIQAML--GGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDqELIPyleVTIFCL 1124
Cdd:cd18600 76 YVGVADSLLamGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILD-DLLP---LTIFDF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1125 IQCASI----IFLITVITPRFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRF 1200
Cdd:cd18600 152 IQLFLIvigaITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1201 ilENMNKIDQNNRA---FFYLSvTVKWFSFRVDMIGAFIVLASgSFILLNIANIDSGLAGISLTYAILFTDGALWLVRLY 1277
Cdd:cd18600 232 --ETLFHKALNLHTanwFLYLS-TLRWFQMRIEMIFVIFFTAV-TFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTS 307
|
330
....*....|...
gi 6321752 1278 STFEMNMNSVERL 1290
Cdd:cd18600 308 IDVDSLMRSVSRI 320
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1323-1560 |
2.24e-26 |
|
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: 109.70 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYaPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAG-TIKSN---VDPYDEYDEKKIFK----ALSQVNLiSSHEFEEVLNSEerfnsthnkflnlhteiaeggln 1474
Cdd:cd03295 80 VIQQIGLFPHmTVEENialVPKLLKWPKEKIREradeLLALVGL-DPAEFADRYPHE----------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1475 LSQGERQLLFIARSLLREPKIILLDEATSSID-YDSDHLIQGIIR--SEFNKsTILTIAHRLRSVIDY-DRIIVMDAGEV 1550
Cdd:cd03295 136 LSGGQQQRVGVARALAADPPLLLMDEPFGALDpITRDQLQEEFKRlqQELGK-TIVFVTHDIDEAFRLaDRIAIMKNGEI 214
|
250
....*....|
gi 6321752 1551 KEYDRPSELL 1560
Cdd:cd03295 215 VQVGTPDEIL 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
664-885 |
3.36e-26 |
|
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: 106.70 E-value: 3.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDsdmnAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSlepkHDL-IPDCE 742
Cdd:cd03228 1 IEFKNVSFSYPGRP----KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG----VDLrDLDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 743 GLTNSFAYCSQSAWLLNDTVKNNIifdnfynedrynkvidacglkrdleilpagdlteigekgitLSGGQKQRISLARAV 822
Cdd:cd03228 73 SLRKNIAYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 823 YSSAKHVLLDDCLSAVDSHTAVWIYENCITgpLMKNRTCILVTHNVSlTLRNAHFAIVLENGK 885
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRA--LAKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1323-1549 |
2.28e-25 |
|
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: 105.24 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPN---LPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGcikidgqdiskidLVTLRRS 1399
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG-------------SVSVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQDPILFAGTIKSNV---DPYDEYDEKKIFKA--LSQvnlisshEFEEVLNSEErfnsthnkflnlhTEIAEGGLN 1474
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFDEERYEKVIKAcaLEP-------DLEILPDGDL-------------TEIGEKGIN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1475 LSQGERQLLFIARSLLREPKIILLDEATSSIDYDS-----DHLIQGIIRsefNKSTILTIAHRLRSVIDYDRIIVMDAGE 1549
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLLL---NNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1323-1550 |
2.63e-25 |
|
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: 105.68 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISkiDLVTLRRSITI 1402
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILF-----AGTI----KSNVDPYDEYDEKKIfKALSQVNLisshefeevLNSEERFNSThnkflnlhteiaeggl 1473
Cdd:cd03259 77 VFQDYALFphltvAENIafglKLRGVPKAEIRARVR-ELLELVGL---------EGLLNRYPHE---------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1474 nLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSD----HLIQGIIRSefNKSTILTIAHRLRSVIDY-DRIIVMDAG 1548
Cdd:cd03259 131 -LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLReelrEELKELQRE--LGITTIYVTHDQEEALALaDRIAVMNEG 207
|
..
gi 6321752 1549 EV 1550
Cdd:cd03259 208 RI 209
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
611-908 |
2.76e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 112.80 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 611 SLFTLLKtPLDQLSNMLSFINQSKVSLKRISDFLRMDdTEKYN-QLTISPDKNKIEFKNATLTWNENDSDmnafKLCGLN 689
Cdd:PRK11176 290 SMIALMR-PLKSLTNVNAQFQRGMAACQTLFAILDLE-QEKDEgKRVIERAKGDIEFRNVTFTYPGKEVP----ALRNIN 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 690 IKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSlepkHDLIP-DCEGLTNSFAYCSQSAWLLNDTVKNNIIF 768
Cdd:PRK11176 364 FKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG----HDLRDyTLASLRNQVALVSQNVHLFNDTIANNIAY 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 769 DNfynEDRYNK--VIDACGLKRDLEI---LPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTA 843
Cdd:PRK11176 440 AR---TEQYSReqIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 844 VWIYENCITgpLMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITELQSKglfKEKYVQL 908
Cdd:PRK11176 517 RAIQAALDE--LQKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELLAQ---NGVYAQL 575
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1323-1561 |
7.28e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 106.25 E-value: 7.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPI-LFAGT---------IKSNVDPYDEYDEkKIFKALSQVNLisshefeevlnseERFnsthnkflnLHTEIAegg 1472
Cdd:PRK13635 86 VFQNPDnQFVGAtvqddvafgLENIGVPREEMVE-RVDQALRQVGM-------------EDF---------LNREPH--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1473 lNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKS--TILTIAHRLRSVIDYDRIIVMDAGEV 1550
Cdd:PRK13635 140 -RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEI 218
|
250
....*....|.
gi 6321752 1551 KEYDRPSELLK 1561
Cdd:PRK13635 219 LEEGTPEEIFK 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1323-1564 |
8.49e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.50 E-value: 8.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGC-----IKIDGQDI--SKIDLVT 1395
Cdd:COG1117 12 IEVRNLNVYYGDK--QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1396 LRRSITIIPQDPILFAGTIKSNV---------DPYDEYDEKkIFKALSQVNLissheFEEVLNseerfnsthnkflNLHt 1466
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVayglrlhgiKSKSELDEI-VEESLRKAAL-----WDEVKD-------------RLK- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1467 eiaEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLR-----SvidyDR 1541
Cdd:COG1117 150 ---KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqaarvS----DY 222
|
250 260
....*....|....*....|....*.
gi 6321752 1542 IIVMDAGEVKEYDRPSELL---KDER 1564
Cdd:COG1117 223 TAFFYLGELVEFGPTEQIFtnpKDKR 248
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1323-1549 |
1.77e-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: 101.88 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLppVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISK--IDLVTLRRSI 1400
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAG-TIKSNVdpydeydekkifkalsqvnlisshefeevlnseerfnsthnkflnlhteiaegGLNLSQGE 1479
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI-----------------------------------------------------ALGLSGGQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 1480 RQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKS--TILTIAHRLRSVIDY-DRIIVMDAGE 1549
Cdd:cd03229 106 QQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1323-1562 |
2.60e-24 |
|
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: 102.90 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKI---DLVtlRRS 1399
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpphERA--RAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQDPILFAG-TIKSNVDPYDEYDEKKIFKAlsqvnlisshEFEEVLnseerfnsthNKFLNLHTEIAEGGLNLSQG 1478
Cdd:cd03224 77 IGYVPEGRRIFPElTVEENLLLGAYARRRAKRKA----------RLERVY----------ELFPRLKERRKQLAGTLSGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1479 ERQLLFIARSLLREPKIILLDEATS----SIDYDsdhlIQGIIRsEFNKS--TILTIAHRLRSVIDY-DRIIVMDAGEVK 1551
Cdd:cd03224 137 EQQMLAIARALMSRPKLLLLDEPSEglapKIVEE----IFEAIR-ELRDEgvTILLVEQNARFALEIaDRAYVLERGRVV 211
|
250
....*....|.
gi 6321752 1552 EYDRPSELLKD 1562
Cdd:cd03224 212 LEGTAAELLAD 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
664-908 |
4.83e-24 |
|
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: 102.56 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDSDMnafkLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSlepkHDL-IPDCE 742
Cdd:cd03252 1 ITFEHVRFRYKPDGPVI----LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG----HDLaLADPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 743 GLTNSFAYCSQSAWLLNDTVKNNIIFDNFYNEDRynKVIDACGLKRDLEI---LPAGDLTEIGEKGITLSGGQKQRISLA 819
Cdd:cd03252 73 WLRRQVGVVLQENVLFNRSIRDNIALADPGMSME--RVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 820 RAVYSSAKHVLLDDCLSAVDSHTAVWIYENciTGPLMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITELQSKG 899
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRN--MHDICAGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
....*....
gi 6321752 900 LFKEKYVQL 908
Cdd:cd03252 228 GLYAYLYQL 236
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1323-1561 |
2.15e-23 |
|
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: 100.82 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKID---LVTLRRS 1399
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQDPILFAG-TIKSNVD-PYDEY---DEKKIFK----ALSQVNLissHEFEEVLNSEerfnsthnkflnlhteiae 1470
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAfPLREHtdlSEAEIRElvleKLELVGL---PGAADKMPSE------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1471 gglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDS----DHLIQGiIRSEFNkSTILTIAHRLRSVIDY-DRIIVM 1545
Cdd:COG1127 142 ----LSGGMRKRVALARALALDPEILLYDEPTAGLDPITsaviDELIRE-LRDELG-LTSVVVTHDLDSAFAIaDRVAVL 215
|
250
....*....|....*.
gi 6321752 1546 DAGEVKEYDRPSELLK 1561
Cdd:COG1127 216 ADGKIIAEGTPEELLA 231
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
689-908 |
3.49e-23 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 105.95 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 689 NIKFQI--GKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLePKHDLIPDceGLTNSFAYCSQSAWLLNDTVKNNI 766
Cdd:PRK10789 333 NVNFTLkpGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI-PLTKLQLD--SWRSRLAVVSQTPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 767 IFDN-FYNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVW 845
Cdd:PRK10789 410 ALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQ 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 846 IYENCITgpLMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITEL-QSKGLFKE--KYVQL 908
Cdd:PRK10789 490 ILHNLRQ--WGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLaQQSGWYRDmyRYQQL 552
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
328-873 |
3.70e-23 |
|
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: 105.83 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 328 LALFESFKTYLLIGMLWVLVNSIVNLlptilmkrfleIVDNPNRSSscmnLAWLyIIGMFICRLTLAICNSQGQFVSDKI 407
Cdd:TIGR02857 8 LALLGVLGALLIIAQAWLLARVVDGL-----------ISAGEPLAE----LLPA-LGALALVLLLRALLGWLQERAAARA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 408 CLRIRailigeiyaKGLRRRLFTSPKTSSDSDSISANLGTIINLI-----SIDSFkvseLANYLYVTVQAVI--MIIVVV 480
Cdd:TIGR02857 72 AAAVK---------SQLRERLLEAVAALGPRWLQGRPSGELATLAlegveALDGY----FARYLPQLVLAVIvpLAILAA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 481 GLLFNFLgvsafAGIsIILVMFPLNFLLANLLGKF-----QKQtLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKS 555
Cdd:TIGR02857 139 VFPQDWI-----SGL-ILLLTAPLIPIFMILIGWAaqaaaRKQ-WAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 556 I----RQKELRSLLkkslvwsvTSFLWFVTPTLVTGVTFA-ICTFVQHEDLNAPLAFTTlSLFTLLKTP-----LDQLSN 625
Cdd:TIGR02857 212 SseeyRERTMRVLR--------IAFLSSAVLELFATLSVAlVAVYIGFRLLAGDLDLAT-GLFVLLLAPefylpLRQLGA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 626 MLSFINQSKVSLKRISDFLRMDDTEKYNQLTI-SPDKNKIEFKNATLTWNENDSdmnafKLCGLNIKFQIGKLNLILGST 704
Cdd:TIGR02857 283 QYHARADGVAAAEALFAVLDAAPRPLAGKAPVtAAPASSLEFSGVSVAYPGRRP-----ALRPVSFTVPPGERVALVGPS 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 705 GSGKSALLLGLLGELNLISGSIIVPSlEPKHDLIPDceGLTNSFAYCSQSAWLLNDTVKNNIIF-DNFYNEDRYNKVIDA 783
Cdd:TIGR02857 358 GAGKSTLLNLLLGFVDPTEGSIAVNG-VPLADADAD--SWRDQIAWVPQHPFLFAGTIAENIRLaRPDASDAEIREALER 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 784 CGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncITGPLMKNRTCIL 863
Cdd:TIGR02857 435 AGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLE--ALRALAQGRTVLL 512
|
570
....*....|
gi 6321752 864 VTHNVSLTLR 873
Cdd:TIGR02857 513 VTHRLALAAL 522
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
338-620 |
4.19e-23 |
|
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: 100.80 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 338 LLIGMLWVLVNSIVNLLPTILMKRFLEIVdNPNRSSSCMNLAwLYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILIG 417
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL-LPDGDPETQALN-VYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 418 EIYAKGLRRRLftspktsSDSDSISAnlGTIINLISIDSFKVSELANY-LYVTVQAVIMIIVVVGLLFNFLGVSAFAGIS 496
Cdd:pfam00664 79 KLFKKILRQPM-------SFFDTNSV--GELLSRLTNDTSKIRDGLGEkLGLLFQSLATIVGGIIVMFYYGWKLTLVLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 497 IILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSLLKKSLVWSVT-S 575
Cdd:pfam00664 150 VLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSfG 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6321752 576 FLWFVTPTLVTGVTFAICTFVQHEDLNAPLAFTTLSLFTLLKTPL 620
Cdd:pfam00664 230 ITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1323-1550 |
6.74e-23 |
|
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: 98.72 E-value: 6.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLP--PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTL---- 1396
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1397 RRSITIIPQD----PILfagTIKSNV--------DPYDEYDEKKIfKALSQVNLisshefeevlnsEERfnstHNKFLNl 1464
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVelplllagVPKKERRERAE-ELLERVGL------------GDR----LNHYPS- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1465 hteiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS---EFNKsTILTIAHRLRSVIDYDR 1541
Cdd:cd03255 140 ---------ELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnkEAGT-TIVVVTHDPELAEYADR 209
|
....*....
gi 6321752 1542 IIVMDAGEV 1550
Cdd:cd03255 210 IIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1324-1551 |
9.44e-23 |
|
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: 97.71 E-value: 9.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1324 EIENLSLRYAPNlPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDlvtLRRSITII 1403
Cdd:cd03226 1 RIENISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1404 PQDP--ILFAGTIKSNV----DPYDEYDEKKifkalsqvnlisshefEEVLnseerfnsthnKFLNLHTEIAEGGLNLSQ 1477
Cdd:cd03226 77 MQDVdyQLFTDSVREELllglKELDAGNEQA----------------ETVL-----------KDLDLYALKERHPLSLSG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 1478 GERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFN-KSTILTIAHRLRSVIDY-DRIIVMDAGEVK 1551
Cdd:cd03226 130 GQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1323-1561 |
1.07e-22 |
|
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: 98.56 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlppVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISkiDLVTLRRSITI 1402
Cdd:cd03299 1 LKVENLSKDWKEF---KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAG-TIKSNVdpydEYDEKKIFKALSQVNlisshefEEVLNSEERFNSTHnkFLNLHTEiaegglNLSQGERQ 1481
Cdd:cd03299 76 VPQNYALFPHmTVYKNI----AYGLKKRKVDKKEIE-------RKVLEIAEMLGIDH--LLNRKPE------TLSGGEQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1482 LLFIARSLLREPKIILLDEATSSIDYdsdhLIQGIIRSEF------NKSTILTIAHRLRSV-IDYDRIIVMDAGEVKEYD 1554
Cdd:cd03299 137 RVAIARALVVNPKILLLDEPFSALDV----RTKEKLREELkkirkeFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVG 212
|
....*..
gi 6321752 1555 RPSELLK 1561
Cdd:cd03299 213 KPEEVFK 219
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
632-909 |
2.63e-22 |
|
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: 104.05 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 632 QSKVSLKRISDFLRmDDTEKYNQ--LTISPDKNKIEFKNATLTWNENDSDMnafkLCGLNIKFQIGKLNLILGSTGSGKS 709
Cdd:TIGR01846 423 QTGIALERLGDILN-SPTEPRSAglAALPELRGAITFENIRFRYAPDSPEV----LSNLNLDIKPGEFIGIVGPSGSGKS 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 710 ALLLGLLGELNLISGSIIVPSlepkHDL-IPDCEGLTNSFAYCSQSAWLLNDTVKNNIIFDNFYNEDRynKVIDACGLKR 788
Cdd:TIGR01846 498 TLTKLLQRLYTPQHGQVLVDG----VDLaIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFE--HVIHAAKLAG 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 789 DLEI---LPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENciTGPLMKNRTCILVT 865
Cdd:TIGR01846 572 AHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRN--MREICRGRTVIIIA 649
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6321752 866 HNVSlTLRNAHFAIVLENGKVKNQGTITEL-QSKGLFKEKYVQLS 909
Cdd:TIGR01846 650 HRLS-TVRACDRIIVLEKGQIAESGRHEELlALQGLYARLWQQQS 693
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1323-1562 |
2.63e-22 |
|
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: 99.74 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPV--IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEP---ITGCIKIDGQDISKIDLVTLR 1397
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1398 ----RSITIIPQDPI-----------LFAGTIKS-NVDPYDEYDEkKIFKALSQVNLisshefeevLNSEERFNST-Hnk 1460
Cdd:COG0444 82 kirgREIQMIFQDPMtslnpvmtvgdQIAEPLRIhGGLSKAEARE-RAIELLERVGL---------PDPERRLDRYpH-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1461 flnlhteiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYdsdhLIQGII-------RSEFNKSTILtIAHRL 1533
Cdd:COG0444 150 -------------ELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQIlnllkdlQRELGLAILF-ITHDL 211
|
250 260 270
....*....|....*....|....*....|.
gi 6321752 1534 rSVIDY--DRIIVMDAGEVKEYDRPSELLKD 1562
Cdd:COG0444 212 -GVVAEiaDRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
663-891 |
2.79e-22 |
|
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: 97.18 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 663 KIEFKNATLTWNENDSDmnafKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLE----PKHDLi 738
Cdd:cd03244 2 DIEFKNVSLRYRPNLPP----VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiGLHDL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 739 pdceglTNSFAYCSQSAWLLNDTVKNNIIFDNFYNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISL 818
Cdd:cd03244 77 ------RSRISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 819 ARAVYSSAKHVLLDDCLSAVDSHTAVWI----YENcitgplMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGT 891
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIqktiREA------FKDCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1323-1562 |
3.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.58 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLP---PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDIS--KIDLVTLR 1397
Cdd:PRK13637 3 IKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1398 RSITIIPQDP--ILFAGTIK-------SNVDPYDEYDEKKIFKALSQVNLisshEFEEVLNSEErfnsthnkflnlhtei 1468
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEkdiafgpINLGLSEEEIENRVKRAMNIVGL----DYEDYKDKSP---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1469 aeggLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS--EFNKSTILTIAHRLRSVIDY-DRIIVM 1545
Cdd:PRK13637 143 ----FELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKLaDRIIVM 218
|
250
....*....|....*..
gi 6321752 1546 DAGEVKEYDRPSELLKD 1562
Cdd:PRK13637 219 NKGKCELQGTPREVFKE 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1323-1566 |
3.97e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.90 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPI-LFAGTI---------KSNVDPYDEYDEKkIFKALSQVNLISSHEFEEvlnseerfNSthnkflnlhteiaegg 1472
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvafglENHAVPYDEMHRR-VSEALKQVDMLERADYEP--------NA---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1473 lnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIR--SEFNKSTILTIAHRLRSVIDYDRIIVMDAGEV 1550
Cdd:PRK13648 143 --LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
250
....*....|....*.
gi 6321752 1551 KEYDRPSELLKDERGI 1566
Cdd:PRK13648 221 YKEGTPTEIFDHAEEL 236
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
334-898 |
6.13e-22 |
|
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: 102.04 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 334 FKTYLLIGMLWVLVNSIVNLLPTILMkrfLEIVDNPNRSSSCMNLAWLYIIGMFICrLTLAICNSQGQFVSDKICLRIRA 413
Cdd:TIGR01842 4 VKRTFIIVGLFSFVINILMLAPPLYM---LQVYDRVLTSGSVPTLLMLTVLALGLY-LFLGLLDALRSFVLVRIGEKLDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 414 ILIGEIYAKGLRRRLFTSPKTSSDsdsisanlgTIINLISIDSFKVSELANYLYvTVQAVIMIIVVVGLLFNFLGVSAFA 493
Cdd:TIGR01842 80 ALNQPIFAASFSATLRRGSGDGLQ---------ALRDLDQLRQFLTGPGLFAFF-DAPWMPIYLLVCFLLHPWIGILALG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 494 GIsiiLVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSLLKKS----L 569
Cdd:TIGR01842 150 GA---VVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASdragM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 570 VWSVTSFLWFVTPTLVTGVTfAICTFVQHEDLNAPLAFTTLSLFTLlkTPLDQLSNMLSFINQSKVSLKRISDFLRmDDT 649
Cdd:TIGR01842 227 LSNLSKYFRIVLQSLVLGLG-AYLAIDGEITPGMMIAGSILVGRAL--APIDGAIGGWKQFSGARQAYKRLNELLA-NYP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 650 EKYNQLTISPDKNKIEFKNATLTWNENdsdmNAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVP 729
Cdd:TIGR01842 303 SRDPAMPLPEPEGHLSVENVTIVPPGG----KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 730 SLEPKHdliPDCEGLTNSFAYCSQSAWLLNDTVKNNI--IFDNFYNEdrynKVIDACGLKRDLEI---LPAGDLTEIGEK 804
Cdd:TIGR01842 379 GADLKQ---WDRETFGKHIGYLPQDVELFPGTVAENIarFGENADPE----KIIEAAKLAGVHELilrLPDGYDTVIGPG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 805 GITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYeNCITGPLMKNRTCILVTHNVSLtLRNAHFAIVLENG 884
Cdd:TIGR01842 452 GATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALA-NAIKALKARGITVVVITHRPSL-LGCVDKILVLQDG 529
|
570
....*....|....
gi 6321752 885 KVKNQGTITELQSK 898
Cdd:TIGR01842 530 RIARFGERDEVLAK 543
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1269-1548 |
8.78e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.81 E-value: 8.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1269 GAL-WLVRLYSTFEMNMNSVERLKEYS-SIEQENYLGHDEGRILLlnepswPKDGEIEIENLSLRyAPNLPPVIRNVSFK 1346
Cdd:COG4178 313 GALsWFVDNYQSLAEWRATVDRLAGFEeALEAADALPEAASRIET------SEDGALALEDLTLR-TPDGRPLLEDLSLS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1347 VDPQSKIGIVGRTGAGKSTiitaLFRLLEPI----TGCIKI-DGQDISkidlvtlrrsitIIPQDPILFAGTIKSNV--- 1418
Cdd:COG4178 386 LKPGERLLITGPSGSGKST----LLRAIAGLwpygSGRIARpAGARVL------------FLPQRPYLPLGTLREALlyp 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1419 DPYDEYDEKKIFKALSQVNLissHEFEEVLNSEERFNSThnkflnlhteiaegglnLSQGERQLLFIARSLLREPKIILL 1498
Cdd:COG4178 450 ATAEAFSDAELREALEAVGL---GHLAERLDEEADWDQV-----------------LSLGEQQRLAFARLLLHKPDWLFL 509
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1499 DEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRlRSVIDY-DRIIVMDAG 1548
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELPGTTVISVGHR-STLAAFhDRVLELTGD 559
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1054-1549 |
2.40e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 102.03 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1054 MLGGFKTMMTFLSGM---RASRKIFNNL----LDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQElIPYLEVTIFCLIQ 1126
Cdd:PTZ00265 105 LIGIFQFILSFISSFcmdVVTTKILKTLklefLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAG-IGTKFITIFTYAS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1127 CASIIFLITVITPRFLTVAVI-VFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRfILENM 1205
Cdd:PTZ00265 184 AFLGLYIWSLFKNARLTLCITcVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKT-ILKKF 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1206 NKIDQnnrafFYLSVTVK---WFSFRVDMIGAFIvLASGSF--------ILLNIANIDS-----GLAGISLTYAILFTdg 1269
Cdd:PTZ00265 263 NLSEK-----LYSKYILKanfMESLHIGMINGFI-LASYAFgfwygtriIISDLSNQQPnndfhGGSVISILLGVLIS-- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1270 ALWLVRLYSTFEMNMNSVERLKEYSSIEQENYL--GHDEGRILllnepswPKDGEIEIENLSLRYAPNLP-PVIRNVSFK 1346
Cdd:PTZ00265 335 MFMLTIILPNITEYMKSLEATNSLYEIINRKPLveNNDDGKKL-------KDIKKIQFKNVRFHYDTRKDvEIYKDLNFT 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1347 VDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKI-DGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNV------- 1418
Cdd:PTZ00265 408 LTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslysl 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1419 ---------------DPYDEYDEKKIFKALSQVNL---ISSHEFEEVLNSEERFNSTHN-------KFLNLH-------- 1465
Cdd:PTZ00265 488 kdlealsnyynedgnDSQENKNKRNSCRAKCAGDLndmSNTTDSNELIEMRKNYQTIKDsevvdvsKKVLIHdfvsalpd 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1466 ---TEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGII---RSEFNKSTILtIAHRLRSVIDY 1539
Cdd:PTZ00265 568 kyeTLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnlKGNENRITII-IAHRLSTIRYA 646
|
570
....*....|
gi 6321752 1540 DRIIVMDAGE 1549
Cdd:PTZ00265 647 NTIFVLSNRE 656
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
414-899 |
2.72e-21 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 100.16 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 414 ILIGEIYAKGLRRRLFTSPKTSSDSDSISANLGTIINLISIDSFKV-SELANYLYVTVQAVIMIIVVVGLLFnflgVSAF 492
Cdd:TIGR02204 83 TWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLqSVIGSSLSMALRNALMCIGGLIMMF----ITSP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 493 AGISIILVMFPLNFLLANLLGKfQKQTLKCTDQ-RISKLN----ECLQNIRIVKYFAWE--------RNIINEIKSIRQK 559
Cdd:TIGR02204 159 KLTSLVLLAVPLVLLPILLFGR-RVRKLSRESQdRIADAGsyagETLGAIRTVQAFGHEdaersrfgGAVEKAYEAARQR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 560 -ELRSLLkkslvwsvTSFLWFVTPTLVTGVTFAICTFVQHEDLNAplafTTLSLFTLLKT----PLDQLSNMLSFINQSK 634
Cdd:TIGR02204 238 iRTRALL--------TAIVIVLVFGAIVGVLWVGAHDVIAGKMSA----GTLGQFVFYAVmvagSIGTLSEVWGELQRAA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 635 VSLKRISDFLRMDDT--EKYNQLTIS-PDKNKIEFKNATLTWNENdsdMNAFKLCGLNIKFQIGKLNLILGSTGSGKSAL 711
Cdd:TIGR02204 306 GAAERLIELLQAEPDikAPAHPKTLPvPLRGEIEFEQVNFAYPAR---PDQPALDGLNLTVRPGETVALVGPSGAGKSTL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 712 LLGLLGELNLISGSIIVPSLePKHDLIPDceGLTNSFAYCSQSAWLLNDTVKNNIIFDNFYNEDRynKVIDACGLKRDLE 791
Cdd:TIGR02204 383 FQLLLRFYDPQSGRILLDGV-DLRQLDPA--ELRARMALVPQDPVLFAASVMENIRYGRPDATDE--EVEAAARAAHAHE 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 792 I---LPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVD--SHTAVwiyENCITGpLMKNRTCILVTH 866
Cdd:TIGR02204 458 FisaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDaeSEQLV---QQALET-LMKGRTTLIIAH 533
|
490 500 510
....*....|....*....|....*....|...
gi 6321752 867 NVSlTLRNAHFAIVLENGKVKNQGTITELQSKG 899
Cdd:TIGR02204 534 RLA-TVLKADRIVVMDQGRIVAQGTHAELIAKG 565
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1323-1559 |
3.21e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLP-PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSIT 1401
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1402 IIPQDPI-LFAG-TIKSNVD--------PYDEYDEKkIFKALsqvNLISSHEFEEvlnseerfnsthnkflnlhTEIAEg 1471
Cdd:PRK13650 85 MVFQNPDnQFVGaTVEDDVAfglenkgiPHEEMKER-VNEAL---ELVGMQDFKE-------------------REPAR- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1472 glnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSD-HLIQGI--IRSEFNKsTILTIAHRLRSVIDYDRIIVMDAG 1548
Cdd:PRK13650 141 ---LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRlELIKTIkgIRDDYQM-TVISITHDLDEVALSDRVLVMKNG 216
|
250
....*....|.
gi 6321752 1549 EVKEYDRPSEL 1559
Cdd:PRK13650 217 QVESTSTPREL 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1342-1556 |
4.03e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 96.34 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1342 NVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKI---DLVTLRRSITIIPQDP----------- 1407
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDPyaslnprmtvg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1408 -ILFAGTIKSNVDPYDEYDEkKIFKALSQVNLISS------HEFeevlnseerfnsthnkflnlhteiaegglnlSQGER 1480
Cdd:COG4608 116 dIIAEPLRIHGLASKAERRE-RVAELLELVGLRPEhadrypHEF-------------------------------SGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1481 QLLFIARSLLREPKIILLDEATSSIDYdSdhlIQ-GII------RSEFNkSTILTIAHRLrSVIDY--DRIIVMDAGEVK 1551
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDV-S---IQaQVLnlledlQDELG-LTYLFISHDL-SVVRHisDRVAVMYLGKIV 237
|
250
....*....|..
gi 6321752 1552 E-------YDRP 1556
Cdd:COG4608 238 EiaprdelYARP 249
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1323-1561 |
6.82e-21 |
|
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: 93.34 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDI---SKIDLVTLRRS 1399
Cdd:cd03261 1 IELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQDPILFAG-TIKSNV---------DPYDEYDEKKIFKaLSQVNLissHEFEEVLNSEerfnsthnkflnlhteia 1469
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVafplrehtrLSEEEIREIVLEK-LEAVGL---RGAEDLYPAE------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1470 egglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS--EFNKSTILTIAHRLRSVIDY-DRIIVMD 1546
Cdd:cd03261 137 -----LSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAIaDRIAVLY 211
|
250
....*....|....*
gi 6321752 1547 AGEVKEYDRPSELLK 1561
Cdd:cd03261 212 DGKIVAEGTPEELRA 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1323-1550 |
8.16e-21 |
|
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: 92.47 E-value: 8.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYaPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKID---LVTLRRS 1399
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQD-PILFAGTIKSNV--------DPYDEYdEKKIFKALSQVNLisSHEfeevlnseerfnsthnkflnlHTEIAE 1470
Cdd:cd03292 80 IGVVFQDfRLLPDRNVYENVafalevtgVPPREI-RKRVPAALELVGL--SHK---------------------HRALPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1471 GglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSeFNK--STILTIAHRLRSVIDYD-RIIVMDA 1547
Cdd:cd03292 136 E---LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKK-INKagTTVVVATHAKELVDTTRhRVIALER 211
|
...
gi 6321752 1548 GEV 1550
Cdd:cd03292 212 GKL 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1324-1564 |
8.32e-21 |
|
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: 93.12 E-value: 8.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1324 EIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKI---DLVtlRRSI 1400
Cdd:COG0410 5 EVENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpphRIA--RLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDpilfagtiksnvdpydeydeKKIFKALSqV--NLI-----------SSHEFEEVLNS----EERFNSthnkfln 1463
Cdd:COG0410 81 GYVPEG--------------------RRIFPSLT-VeeNLLlgayarrdraeVRADLERVYELfprlKERRRQ------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1464 lhteiaEGGlNLSQGERQLLFIARSLLREPKIILLDEATSSIdydSDHLIQGIIR--SEFNKS--TILTIAHRLRSVIDY 1539
Cdd:COG0410 133 ------RAG-TLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL---APLIVEEIFEiiRRLNREgvTILLVEQNARFALEI 202
|
250 260
....*....|....*....|....*.
gi 6321752 1540 -DRIIVMDAGEVKEYDRPSELLKDER 1564
Cdd:COG0410 203 aDRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1323-1559 |
9.40e-21 |
|
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: 92.57 E-value: 9.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKiDLVTLRRSITI 1402
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAG-TIKSNVdpydeydekKIFKALSQVNLisSHEFEEVLNSEERFNSTHNKflnlHTEIAegglNLSQGERQ 1481
Cdd:cd03263 80 CPQFDALFDElTVREHL---------RFYARLKGLPK--SEIKEEVELLLRVLGLTDKA----NKRAR----TLSGGMKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1482 LLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEF-NKSTILTiAHRLRsVIDY--DRIIVMDAGEVKEYDRPSE 1558
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRkGRSIILT-THSMD-EAEAlcDRIAIMSDGKLRCIGSPQE 218
|
.
gi 6321752 1559 L 1559
Cdd:cd03263 219 L 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1323-1558 |
2.31e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 94.48 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPVI--RNVSFKVdPQSKI-GIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKID---LVTL 1396
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHalNNVSLHI-PAGEIfGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1397 RRSITIIPQD---------------PILFAGTIKSNVdpydeydEKKIFKALSQVNLISSHefeevlnseERFNSthnkf 1461
Cdd:PRK11153 81 RRQIGMIFQHfnllssrtvfdnvalPLELAGTPKAEI-------KARVTELLELVGLSDKA---------DRYPA----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1462 lnlhteiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS---TILTIAHRLrSVID 1538
Cdd:PRK11153 140 ------------QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLK-DINRElglTIVLITHEM-DVVK 205
|
250 260
....*....|....*....|..
gi 6321752 1539 Y--DRIIVMDAGEVKEYDRPSE 1558
Cdd:PRK11153 206 RicDRVAVIDAGRLVEQGTVSE 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1323-1567 |
4.16e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 91.68 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVdPQSKI-GIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSIT 1401
Cdd:COG4604 2 IEIKNVSKRYGGK--VVLDDVSLTI-PKGGItALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1402 IIPQDPILfagTIKSNVD--------PY-----DEYDEKKIFKALSQVNLissHEFEevlnseerfnsthNKFLNlhtei 1468
Cdd:COG4604 79 ILRQENHI---NSRLTVRelvafgrfPYskgrlTAEDREIIDEAIAYLDL---EDLA-------------DRYLD----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1469 aegglNLSQGERQLLFIARSLLREPKIILLDEATSSID-YDSDHLIQgIIRS---EFNKSTILTIaHRLRSVIDY-DRII 1543
Cdd:COG4604 135 -----ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMMK-LLRRladELGKTVVIVL-HDINFASCYaDHIV 207
|
250 260
....*....|....*....|....*.
gi 6321752 1544 VMDAGEVKEYDRPSELLKDE--RGIF 1567
Cdd:COG4604 208 AMKDGRVVAQGTPEEIITPEvlSDIY 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1323-1550 |
6.87e-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: 89.90 E-value: 6.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDI--SKIDLVTLRRSI 1400
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAG-TIKSNVD---------PYDEYDEKKIfKALSQVNLisshefeevlnsEERFNSTHNKflnlhteiae 1470
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENITlapikvkgmSKAEAEERAL-ELLEKVGL------------ADKADAYPAQ---------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1471 gglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS-EFNKSTILTIAHRL---RSVIdyDRIIVMD 1546
Cdd:cd03262 136 ----LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMgfaREVA--DRVIFMD 209
|
....
gi 6321752 1547 AGEV 1550
Cdd:cd03262 210 DGRI 213
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1323-1559 |
8.81e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.61 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYapNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRL--LEP---ITGCIKIDGQDI--SKIDLVT 1395
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1396 LRRSITIIPQDPILFAGTIKSNVdPY----DEYDEKKIFKALSQVNLISSHEFEEVlnsEERfnsthnkflnLHteiaEG 1471
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENV-VYglrlKGIKDKQVLDEAVEKSLKGASIWDEV---KDR----------LH----DS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1472 GLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLR--SVIDyDRIIVMDAGE 1549
Cdd:PRK14239 146 ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQqaSRIS-DRTGFFLDGD 224
|
250
....*....|
gi 6321752 1550 VKEYDRPSEL 1559
Cdd:PRK14239 225 LIEYNDTKQM 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
965-1578 |
8.91e-20 |
|
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: 96.94 E-value: 8.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 965 PDVYKWYLKFFGGFKALTALFAL------YITAQILFIsqswwIRHWVNDTNvrinAPGFamdtlplkgmtdssknkhNA 1038
Cdd:TIGR00957 305 PSLFKVLYKTFGPYFLMSFCFKAihdlmmFIGPQILSL-----LIRFVNDPM----APDW------------------QG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1039 FYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLD--LVLHAQIRffDVTPVGRIMNRFSKDIEGVdQELIPY 1116
Cdd:TIGR00957 358 YFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRkaLVITNSAR--KSSTVGEIVNLMSVDAQRF-MDLATY 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1117 LEVTIFCLIQCA-SIIFLITVITPRFLT-VAVIVFVLYFFVGKWYLTASRELKRLDSitKSPIFQHFSETLVGVCTIRAF 1194
Cdd:TIGR00957 435 INMIWSAPLQVIlALYFLWLNLGPSVLAgVAVMVLMVPLNAVMAMKTKTYQVAHMKS--KDNRIKLMNEILNGIKVLKLY 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1195 GDERRFiLENMNKIDQNN----RAFFYLSvTVKWFSFrvdMIGAFIVLAS--GSFILLNIANI-DSGLAGISLTYAILFT 1267
Cdd:TIGR00957 513 AWELAF-LDKVEGIRQEElkvlKKSAYLH-AVGTFTW---VCTPFLVALItfAVYVTVDENNIlDAEKAFVSLALFNILR 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1268 DGALWLVRLYSTFEMNMNSVERLKEYSSIEQenyLGHD--EGRILllnepswpKDGE---IEIENLSLRYAPNLPPVIRN 1342
Cdd:TIGR00957 588 FPLNILPMVISSIVQASVSLKRLRIFLSHEE---LEPDsiERRTI--------KPGEgnsITVHNATFTWARDLPPTLNG 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1343 VSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEpitgciKIDGQdiskidlVTLRRSITIIPQDPILFAGTIKSNVDPYD 1422
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD------KVEGH-------VHMKGSVAYVPQQAWIQNDSLRENILFGK 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1423 EYDEKKIFKALSQVNLISSHefeEVLNSEERfnsthnkflnlhTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEAT 1502
Cdd:TIGR00957 724 ALNEKYYQQVLEACALLPDL---EILPSGDR------------TEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1503 SSID-YDSDHLIQGIIRSE---FNKSTILtIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELLkDERGIF------YSMCR 1572
Cdd:TIGR00957 789 SAVDaHVGKHIFEHVIGPEgvlKNKTRIL-VTHGISYLPQVDVIIVMSGGKISEMGSYQELL-QRDGAFaeflrtYAPDE 866
|
....*.
gi 6321752 1573 DSGGLE 1578
Cdd:TIGR00957 867 QQGHLE 872
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
611-903 |
1.08e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.03 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 611 SLFTLLKTPLDQLSNmlsFINQSKVSLKRISDFLRMDDT-----EKYNQLTISPDKNKIEFKNATLTWnendsDMNAFKL 685
Cdd:PRK13657 280 GFATLLIGRLDQVVA---FINQVFMAAPKLEEFFEVEDAvpdvrDPPGAIDLGRVKGAVEFDDVSFSY-----DNSRQGV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 686 CGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEpkhdlIPDC--EGLTNSFAYCSQSAWLLNDTVK 763
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD-----IRTVtrASLRRNIAVVFQDAGLFNRSIE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 764 NNIifdnfynedRYNKViDACG--LKRDLEILPAGDL---------TEIGEKGITLSGGQKQRISLARAVYSSAKHVLLD 832
Cdd:PRK13657 427 DNI---------RVGRP-DATDeeMRAAAERAQAHDFierkpdgydTVVGERGRQLSGGERQRLAIARALLKDPPILILD 496
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 833 DCLSAVDSHTavwiyENCITGPL---MKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITEL-QSKGLFKE 903
Cdd:PRK13657 497 EATSALDVET-----EAKVKAALdelMKGRTTFIIAHRLS-TVRNADRILVFDNGRVVESGSFDELvARGGRFAA 565
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1323-1559 |
1.38e-19 |
|
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: 89.35 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLppVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKiDLVTLRRSITI 1402
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPIlfagtiksnVDP-YDEYDEKKIFKALSQV-NLISSHEFEEVLnseerfnsthnKFLNLhTEIAEGGL-NLSQGE 1479
Cdd:cd03265 78 VFQDLS---------VDDeLTGWENLYIHARLYGVpGAERRERIDELL-----------DFVGL-LEAADRLVkTYSGGM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1480 RQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS---EFNkSTILTIAHRLRSVIDY-DRIIVMDAGEVKEYDR 1555
Cdd:cd03265 137 RRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKlkeEFG-MTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGT 215
|
....
gi 6321752 1556 PSEL 1559
Cdd:cd03265 216 PEEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1323-1550 |
1.49e-19 |
|
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: 87.10 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDI---SKIDlvTLRRS 1399
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsfaSPRD--ARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQdpilfagtiksnvdpydeydekkifkalsqvnlisshefeevlnseerfnsthnkflnlhteiaegglnLSQGE 1479
Cdd:cd03216 77 IAMVYQ---------------------------------------------------------------------LSVGE 87
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 1480 RQLLFIARSLLREPKIILLDEATSSI-DYDSDHLIQgIIRsEFNKS--TILTIAHRLRSVIDY-DRIIVMDAGEV 1550
Cdd:cd03216 88 RQMVEIARALARNARLLILDEPTAALtPAEVERLFK-VIR-RLRAQgvAVIFISHRLDEVFEIaDRVTVLRDGRV 160
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1323-1562 |
3.92e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.52 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPVI--RNVSFKVDPQSKIGIVGRTGAGKSTIItalfR---LLE-PITGCIKIDGQDISKID---L 1393
Cdd:COG1135 2 IELENLSKTFPTKGGPVTalDDVSLTIEKGEIFGIIGYSGAGKSTLI----RcinLLErPTSGSVLVDGVDLTALSereL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1394 VTLRRSITIIPQD---------------PILFAGTIKSNVdpydeydEKKIFKALSQVNLisshefeevlnsEERfnstH 1458
Cdd:COG1135 78 RAARRKIGMIFQHfnllssrtvaenvalPLEIAGVPKAEI-------RKRVAELLELVGL------------SDK----A 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1459 NKFLNlhteiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDH----LIQGiIRSEFNKsTILTIAHRLr 1534
Cdd:COG1135 135 DAYPS----------QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLKD-INRELGL-TIVLITHEM- 201
|
250 260 270
....*....|....*....|....*....|
gi 6321752 1535 SVIDY--DRIIVMDAGEVKEYDRPSELLKD 1562
Cdd:COG1135 202 DVVRRicDRVAVLENGRIVEQGPVLDVFAN 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1323-1550 |
6.61e-19 |
|
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: 87.04 E-value: 6.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPV--IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKiDLVTLRRSI 1400
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAG-TIKSNVdpydEYdekkiFKALSQVNLISSHEFEEVLNSEERFnsthNKFLNLHTEiaegglNLSQGE 1479
Cdd:cd03266 81 GFVSDSTGLYDRlTARENL----EY-----FAGLYGLKGDELTARLEELADRLGM----EELLDRRVG------GFSTGM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 1480 RQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS--EFNKsTILTIAHRLRSVIDY-DRIIVMDAGEV 1550
Cdd:cd03266 142 RQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQlrALGK-CILFSTHIMQEVERLcDRVVVLHRGRV 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1323-1564 |
7.33e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.50 E-value: 7.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYaPNLPpviRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKidLVTLRRSITI 1402
Cdd:COG3840 2 LRLDDLTYRY-GDFP---LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA--LPPAERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAG-TIKSNV----DP---YDEYDEKKIFKALSQVNLissHEFEEVLNSEerfnsthnkflnlhteiaeggln 1474
Cdd:COG3840 76 LFQENNLFPHlTVAQNIglglRPglkLTAEQRAQVEQALERVGL---AGLLDRLPGQ----------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1475 LSQGERQLLFIARSLLREPKIILLDEATSSID----YDSDHLIQGIIRSEfnKSTILTIAHRLRSVIDY-DRIIVMDAGE 1549
Cdd:COG3840 130 LSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARIaDRVLLVADGR 207
|
250
....*....|....*
gi 6321752 1550 VkEYDRPSELLKDER 1564
Cdd:COG3840 208 I-AADGPTAALLDGE 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1323-1589 |
9.44e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 87.84 E-value: 9.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNL--PPVIRNVSFKVDPQSKIGIVGRTGAGKSTiitaLFR----LLEPITGCIKIDGQDISKIDlvtl 1396
Cdd:COG1116 8 LELRGVSKRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKST----LLRliagLEKPTSGEVLVDGKPVTGPG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1397 rRSITIIPQDPILFA-GTIKSNVD--------PYDEYDEKkIFKALSQVNLissHEFEEVLNSEerfnsthnkflnlhte 1467
Cdd:COG1116 80 -PDRGVVFQEPALLPwLTVLDNVAlglelrgvPKAERRER-ARELLELVGL---AGFEDAYPHQ---------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1468 iaegglnLSQGERQLLFIARSLLREPKIILLDEATSSIDY----DSDHLIQGIIRSEfnKSTILTIAH------RLrSvi 1537
Cdd:COG1116 139 -------LSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRLWQET--GKTVLFVTHdvdeavFL-A-- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1538 dyDRIIVMDA--GEVKE-------YDRPSELLKDERgiFYSMCRdsgglELLKQIAKQSSK 1589
Cdd:COG1116 207 --DRVVVLSArpGRIVEeidvdlpRPRDRELRTSPE--FAALRA-----EILDLLREEAER 258
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1323-1564 |
1.18e-18 |
|
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: 86.72 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLppVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDIS--KIDLVTlRRSI 1400
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITglPPHEIA-RLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAG-TIKSNV------------------DPYDEYDEKkIFKALSQVNLisshefEEVLNseerfnsthnkf 1461
Cdd:cd03219 78 GRTFQIPRLFPElTVLENVmvaaqartgsglllararREEREARER-AEELLERVGL------ADLAD------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1462 lnlhtEIAEgglNLSQGERQLLFIARSLLREPKIILLDEATS--SIDyDSDHLIQgIIRsEFNKS--TILTIAHRLRSVI 1537
Cdd:cd03219 139 -----RPAG---ELSYGQQRRLEIARALATDPKLLLLDEPAAglNPE-ETEELAE-LIR-ELRERgiTVLLVEHDMDVVM 207
|
250 260
....*....|....*....|....*...
gi 6321752 1538 DY-DRIIVMDAGEVKEYDRPSELLKDER 1564
Cdd:cd03219 208 SLaDRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1323-1563 |
1.24e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 86.83 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKST---IITALFRllePITGCIKIDGQDISKIDLVT-LRR 1398
Cdd:cd03218 1 LRAENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTtfyMIVGLVK---PDSGKILLDGQDITKLPMHKrARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1399 SITIIPQDPILFAG-TIKSNVDPYDE--YDEKKIFKalsqvnlissHEFEEVLnseERFNSTHNKfLNLhteiaegGLNL 1475
Cdd:cd03218 76 GIGYLPQEASIFRKlTVEENILAVLEirGLSKKERE----------EKLEELL---EEFHITHLR-KSK-------ASSL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1476 SQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKST-ILTIAHRLRSVIDY-DRIIVMDAGEVKEY 1553
Cdd:cd03218 135 SGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDHNVRETLSItDRAYIIYEGKVLAE 214
|
250
....*....|
gi 6321752 1554 DRPSELLKDE 1563
Cdd:cd03218 215 GTPEEIAANE 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
476-905 |
1.24e-18 |
|
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: 92.11 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 476 IIVVVGLLFNFLGVSAFAgisIILVMFPLN----FLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIIN 551
Cdd:TIGR01193 282 ILVIVGLFLVRQNMLLFL---LSLLSIPVYaviiILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYS 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 552 EIKSirqkELRSLLKKSLVWSVTSFLW-----FVTPTLVTGVTFAICTFVQHEDLNAPLAFTTLSLFTLLKTPLDQLSNM 626
Cdd:TIGR01193 359 KIDS----EFGDYLNKSFKYQKADQGQqaikaVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 627 LSFINQSKVSLKRI-------SDFLRMDDTEKYNQLTISPDKNKIEFKNAtltwnendsdMNAFKLCGLNIKFQIGKLNL 699
Cdd:TIGR01193 435 QPKLQAARVANNRLnevylvdSEFINKKKRTELNNLNGDIVINDVSYSYG----------YGSNILSDISLTIKMNSKTT 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 700 ILGSTGSGKSALLLGLLGELNLISGSIivpSLEPKHDLIPDCEGLTNSFAYCSQSAWLLNDTVKNNIIFDNFYN--EDRY 777
Cdd:TIGR01193 505 IVGMSGSGKSTLAKLLVGFFQARSGEI---LLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENvsQDEI 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 778 NKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITgplMK 857
Cdd:TIGR01193 582 WAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN---LQ 658
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 6321752 858 NRTCILVTHNVSLTLRnAHFAIVLENGKVKNQGTITEL-QSKGLFKEKY 905
Cdd:TIGR01193 659 DKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELlDRNGFYASLI 706
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1325-1554 |
1.57e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1325 IENLSLRYAPnlPPVIRNVSFKVDPQSKIGIVGRTGAGKSTiitaLFRLlepITGCIKID-GQdiskidlVTLRRSITI- 1402
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKI---LAGELEPDsGE-------VSIPKGLRIg 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 -IPQDPILFAG-TIKSNVdpydEYDEKKIFKALSQVNLIsSHEFEEVLNSEERFNSTHNKFL-----NLHTEIAE--GGL 1473
Cdd:COG0488 65 yLPQEPPLDDDlTVLDTV----LDGDAELRALEAELEEL-EAKLAEPDEDLERLAELQEEFEalggwEAEARAEEilSGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1474 ------------NLSQGERQLLFIARSLLREPKIILLDEATSSIDYDS-----DHLIQgiirsefNKSTILTIAH-R--L 1533
Cdd:COG0488 140 gfpeedldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKN-------YPGTVLVVSHdRyfL 212
|
250 260
....*....|....*....|.
gi 6321752 1534 RSVIdyDRIIVMDAGEVKEYD 1554
Cdd:COG0488 213 DRVA--TRILELDRGKLTLYP 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1323-1562 |
1.70e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYaPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCI---KIDGQDISKidLVTLRRS 1399
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSK--LQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQDP-ILFAG-TIKSNVD--------PYDEYdEKKIFKALSQVNLisshefeevlnseERFNSTHNKflnlhteia 1469
Cdd:PRK13644 79 VGIVFQNPeTQFVGrTVEEDLAfgpenlclPPIEI-RKRVDRALAEIGL-------------EKYRHRSPK--------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1470 egglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDS-DHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAG 1548
Cdd:PRK13644 136 ----TLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRG 211
|
250
....*....|....
gi 6321752 1549 EVKEYDRPSELLKD 1562
Cdd:PRK13644 212 KIVLEGEPENVLSD 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1323-1560 |
2.17e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.07 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLP-PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSIT 1401
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1402 IIPQDP--ILFAGTIKSNVD--------PYDEYDeKKIFKALSQVNLISSHEFEEVlnseerfnsthnkflnlhteiaeg 1471
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAfgmenqgiPREEMI-KRVDEALLAVNMLDFKTREPA------------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1472 glNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKS--TILTIAHRLRSVIDYDRIIVMDAGE 1549
Cdd:PRK13642 140 --RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGE 217
|
250
....*....|.
gi 6321752 1550 VKEYDRPSELL 1560
Cdd:PRK13642 218 IIKEAAPSELF 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1339-1560 |
2.37e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.64 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1339 VIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQ------DISKIDLVTLRRSITIIPQDPILFAG 1412
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1413 -TIKSNVD-PYDEY--DEKKIFKALSQVNLISSHEFEEVlnsEERFNSTHNKflnlhteiaegglnLSQGERQLLFIARS 1488
Cdd:PRK14246 105 lSIYDNIAyPLKSHgiKEKREIKKIVEECLRKVGLWKEV---YDRLNSPASQ--------------LSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 1489 LLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPSELL 1560
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIF 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1323-1564 |
3.59e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.75 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:PRK09536 4 IDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPIL-FAGTIKSNV-----------DPYDEYDEKKIFKALSQVnliSSHEFeevlnSEERFNSthnkflnlhteiae 1470
Cdd:PRK09536 82 VPQDTSLsFEFDVRQVVemgrtphrsrfDTWTETDRAAVERAMERT---GVAQF-----ADRPVTS-------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1471 gglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYdsDHLIQGI--IRS--EFNKSTILTIaHRLRSVIDY-DRIIVM 1545
Cdd:PRK09536 140 ----LSGGERQRVLLARALAQATPVLLLDEPTASLDI--NHQVRTLelVRRlvDDGKTAVAAI-HDLDLAARYcDELVLL 212
|
250
....*....|....*....
gi 6321752 1546 DAGEVKEYDRPSELLKDER 1564
Cdd:PRK09536 213 ADGRVRAAGPPADVLTADT 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1340-1560 |
3.97e-18 |
|
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: 86.16 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1340 IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKI---DLVTLRR-SITIIPQDPILFAG-TI 1414
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1415 KSNVD--------PYDEYDEKKIfKALSQVNLissHEFEEVLNSEerfnsthnkflnlhteiaegglnLSQGERQLLFIA 1486
Cdd:cd03294 120 LENVAfglevqgvPRAEREERAA-EALELVGL---EGWEHKYPDE-----------------------LSGGMQQRVGLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1487 RSLLREPKIILLDEATSSIdydsDHLIQGIIRSEF------NKSTILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPSEL 1559
Cdd:cd03294 173 RALAVDPDILLMDEAFSAL----DPLIRREMQDELlrlqaeLQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEI 248
|
.
gi 6321752 1560 L 1560
Cdd:cd03294 249 L 249
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
338-640 |
5.68e-18 |
|
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: 86.45 E-value: 5.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 338 LLIGMLWVLVNSIVNLLPTILMKRFL-EIVDNPNrssscMNLAWLYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILI 416
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIdDVIPAGD-----LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 417 GEIYAKGLRRRL--FTSPKTssdsdsisanlGTIINLISIDSFKVSELA-NYLYVTVQAVIMIIVVVGLLFnFLGVS-AF 492
Cdd:cd07346 76 RDLFRHLQRLSLsfFDRNRT-----------GDLMSRLTSDVDAVQNLVsSGLLQLLSDVLTLIGALVILF-YLNWKlTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 493 AGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIINEIKSIRQKELRSLLKKSLVWS 572
Cdd:cd07346 144 VALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 573 VTS-FLWFVTPTLVTGVTFAICTFVQHEDLNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVSLKRI 640
Cdd:cd07346 224 LFSpLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1323-1562 |
6.85e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.91 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPN----LPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKI-DLVTLR 1397
Cdd:PRK13633 5 IKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1398 RSITIIPQDP--ILFAGTIKSNVdpydeydekkifkALSQVNL-ISSHEFEE-VLNSEERFNSTHNKFLNLHTeiaeggl 1473
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDV-------------AFGPENLgIPPEEIRErVDESLKKVGMYEYRRHAPHL------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1474 nLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS---TILTIAHRLRSVIDYDRIIVMDAGEV 1550
Cdd:PRK13633 145 -LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIK-ELNKKygiTIILITHYMEEAVEADRIIVMDSGKV 222
|
250
....*....|..
gi 6321752 1551 KEYDRPSELLKD 1562
Cdd:PRK13633 223 VMEGTPKEIFKE 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
459-867 |
7.90e-18 |
|
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: 88.96 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 459 VSELANYLYVTVQ----AVIMIIVVVGLLFNFLGVSAFAGISIILVMFPLNFLLANLLGKFQKQTLKCT----DQRISKL 530
Cdd:TIGR02868 120 VDALQDLYVRVIVpagvALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLrgelAAQLTDA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 531 NECLQNIRIvkYFAWERnIINEIkSIRQKELRSLLKKSLVW--------------SVTSFLWF----VTPTLVTGVTFAI 592
Cdd:TIGR02868 200 LDGAAELVA--SGALPA-ALAQV-EEADRELTRAERRAAAAtalgaaltllaaglAVLGALWAggpaVADGRLAPVTLAV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 593 ctfvqhedlnapLAFTTLSLFTllktPLDQLSNMLSFINQSKVSLKRISDFLR----MDDTEKYNQLTISPDKNKIEFKN 668
Cdd:TIGR02868 276 ------------LVLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVLDaagpVAEGSAPAAGAVGLGKPTLELRD 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 669 ATLTWnendsDMNAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSlEPKHDLipDCEGLTNSF 748
Cdd:TIGR02868 340 LSAGY-----PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG-VPVSSL--DQDEVRRRV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 749 AYCSQSAWLLNDTVKNNIIF--DNFYNEDRYnKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSA 826
Cdd:TIGR02868 412 SVCAQDAHLFDTTVRENLRLarPDATDEELW-AALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADA 490
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 6321752 827 KHVLLDDCLSAVDSHTAVWIYENCITGplMKNRTCILVTHN 867
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1318-1583 |
7.92e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.62 E-value: 7.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1318 PKDGEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEP---ITGCIKIDGQDISKIDLV 1394
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1395 TLRRSITIIPQDPI-LFAG-TIKSNVD--------PYDEYdEKKIFKALSQVNLIsshefeEVLNSEERfnsthnkflnl 1464
Cdd:PRK13640 81 DIREKVGIVFQNPDnQFVGaTVGDDVAfglenravPRPEM-IKIVRDVLADVGML------DYIDSEPA----------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1465 hteiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS--EFNKSTILTIAHRLRSVIDYDRI 1542
Cdd:PRK13640 143 ---------NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQV 213
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 6321752 1543 IVMDAGEVKEYDRPSELLKDErgifysmcrdsgglELLKQI 1583
Cdd:PRK13640 214 LVLDDGKLLAQGSPVEIFSKV--------------EMLKEI 240
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1321-1559 |
8.50e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.05 E-value: 8.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1321 GEIEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTiitaLFRL---LEPIT-GCIKIDGQDISkiDLVTL 1396
Cdd:COG3839 2 ASLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKST----LLRMiagLEDPTsGEILIGGRDVT--DLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1397 RRSITIIPQDPILF---------------AGTIKSNVDpydeydeKKIFKALSQVNLisshefEEVLNseeRFNSthnkf 1461
Cdd:COG3839 74 DRNIAMVFQSYALYphmtvyeniafplklRKVPKAEID-------RRVREAAELLGL------EDLLD---RKPK----- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1462 lnlhteiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYdsdHL-------IQGIIRsEFNKSTI-------- 1526
Cdd:COG3839 133 ------------QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA---KLrvemraeIKRLHR-RLGTTTIyvthdqve 196
|
250 260 270
....*....|....*....|....*....|....
gi 6321752 1527 -LTIAhrlrsvidyDRIIVMDAGEVKEYDRPSEL 1559
Cdd:COG3839 197 aMTLA---------DRIAVMNDGRIQQVGTPEEL 221
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1323-1548 |
9.99e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 83.92 E-value: 9.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPpVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCI----KIDGQDISKIDLVTLRR 1398
Cdd:cd03290 1 VQVTNGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1399 SITIIPQDPILFAGTIKSNV---DPYDEYDEKKIFKALSQVNLISSHEFEEvlnseerfnsthnkflnlHTEIAEGGLNL 1475
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENItfgSPFNKQRYKAVTDACSLQPDIDLLPFGD------------------QTEIGERGINL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 1476 SQGERQLLFIARSLLREPKIILLDEATSSID-YDSDHLIQ-GIIRS-EFNKSTILTIAHRLRSVIDYDRIIVMDAG 1548
Cdd:cd03290 142 SGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQeGILKFlQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1326-1564 |
1.17e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.17 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1326 ENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDL-VTLRRSITIIP 1404
Cdd:PRK10895 7 KNLAKAYKGR--RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1405 QdpilfagtiksnvdpydeydEKKIFKALSQV-NLISSHEFEEVLNSEERFNSTHNKFLNLHTEIAEGGL--NLSQGERQ 1481
Cdd:PRK10895 85 Q--------------------EASIFRRLSVYdNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMgqSLSGGERR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1482 LLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKST-ILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPSEL 1559
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEI 224
|
....*
gi 6321752 1560 LKDER 1564
Cdd:PRK10895 225 LQDEH 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
663-890 |
1.50e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 83.41 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 663 KIEFKNATLTWNendsDMNAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKhdLIPDCE 742
Cdd:cd03245 2 RIEFRNVSFSYP----NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIR--QLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 743 gLTNSFAYCSQSAWLLNDTVKNNIIFDNFYNED-RYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARA 821
Cdd:cd03245 76 -LRRNIGYVPQDVTLFYGTLRDNITLGAPLADDeRILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 822 VYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPlmKNRTCILVTHNVSLtLRNAHFAIVLENGKVKNQG 890
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLL--GDKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1323-1562 |
1.69e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.88 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLP---PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDI----SKIDLVT 1395
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1396 LRRSITIIPQDP--ILFAGTIKSNVD--PY-----DEYDEKKIFKALSQVNLIsshefEEVLNseerfnstHNKFlnlht 1466
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEfgPKnfgfsEDEAKEKALKWLKKVGLS-----EDLIS--------KSPF----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1467 eiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS--TILTIAHRLRSVIDY-DRII 1543
Cdd:PRK13641 145 -------ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFK-DYQKAghTVILVTHNMDDVAEYaDDVL 216
|
250
....*....|....*....
gi 6321752 1544 VMDAGEVKEYDRPSELLKD 1562
Cdd:PRK13641 217 VLEHGKLIKHASPKEIFSD 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1323-1564 |
2.03e-17 |
|
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: 83.60 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGC-IKIDGQDISKIDLVTLRRSI- 1400
Cdd:COG1119 4 LELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 --------TIIPQDPIL------FAGTIksnvDPYDEYDEKKIFKAlsqvnlisshefEEVLnseERFNSTHNKFLNLHT 1466
Cdd:COG1119 82 lvspalqlRFPRDETVLdvvlsgFFDSI----GLYREPTDEQRERA------------RELL---ELLGLAHLADRPFGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1467 eiaegglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDH----LIQGIIRSEfnKSTILTIAHRLRSVID-YDR 1541
Cdd:COG1119 143 --------LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARElllaLLDKLAAEG--APTLVLVTHHVEEIPPgITH 212
|
250 260
....*....|....*....|...
gi 6321752 1542 IIVMDAGEVKEYDRPSELLKDER 1564
Cdd:COG1119 213 VLLLKDGRVVAAGPKEEVLTSEN 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1323-1551 |
5.88e-17 |
|
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: 81.47 E-value: 5.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLppVIRNVSFKVDPqSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKiDLVTLRRSITI 1402
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPilfagTIKSNVDPYDEYDEKKIFKALSqvnliSSHEFEEVLNSEERFNSTHNKflnlHTEIAEgglnLSQGERQL 1482
Cdd:cd03264 77 LPQEF-----GVYPNFTVREFLDYIAWLKGIP-----SKEVKARVDEVLELVNLGDRA----KKKIGS----LSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1483 LFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIrSEFNKSTILTIAHRLRSVID--YDRIIVMDAGEVK 1551
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLL-SELGEDRIVILSTHIVEDVEslCNQVAVLNKGKLV 208
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1321-1564 |
9.34e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.61 E-value: 9.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1321 GEIEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKST---IITALFRllePITGCIKIDGQDISKIDLvtLR 1397
Cdd:COG1137 2 MTLEAENLVKSYGKR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTtfyMIVGLVK---PDSGRIFLDGEDITHLPM--HK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1398 RS---ITIIPQDPILFAG-TIKSNvdpydeydekkIFKALSQVNLiSSHEFEEVLNS--EErFNSTH---NKflnlhtei 1468
Cdd:COG1137 75 RArlgIGYLPQEASIFRKlTVEDN-----------ILAVLELRKL-SKKEREERLEEllEE-FGITHlrkSK-------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1469 aegGLNLSQGERQLLFIARSLLREPKIILLDEATSSID----YDsdhlIQGIIRS--EFNKSTILTiAHRLR---SVIdy 1539
Cdd:COG1137 134 ---AYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiavAD----IQKIIRHlkERGIGVLIT-DHNVRetlGIC-- 203
|
250 260
....*....|....*....|....*
gi 6321752 1540 DRIIVMDAGEVKEYDRPSELLKDER 1564
Cdd:COG1137 204 DRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1322-1563 |
9.83e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.60 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1322 EIEIENLSLRYAPNlpPVIRNVSFKVdPQSKI-GIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSI 1400
Cdd:PRK11231 2 TLRTENLTVGYGTK--RILNDLSLSL-PTGKItALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAG-TIKSNV----DPYDEY-------DEKKIFKALSQVNLisshefeevlnseerfnsthnkflnlhTEI 1468
Cdd:PRK11231 79 ALLPQHHLTPEGiTVRELVaygrSPWLSLwgrlsaeDNARVNQAMEQTRI---------------------------NHL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1469 AEGGL-NLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS--TILTIAHRLRSVIDY-DRIIV 1544
Cdd:PRK11231 132 ADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR-ELNTQgkTVVTVLHDLNQASRYcDHLVV 210
|
250
....*....|....*....
gi 6321752 1545 MDAGEVKEYDRPSELLKDE 1563
Cdd:PRK11231 211 LANGHVMAQGTPEEVMTPG 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
656-886 |
1.10e-16 |
|
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: 80.98 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 656 TISPD--KNKIEFKNATLTWnENDSDMNAFKlcGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIV---PS 730
Cdd:cd03248 2 SLAPDhlKGIVKFQNVTFAY-PTRPDTLVLQ--DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdgkPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 731 LEPKHdlipdcEGLTNSFAYCSQSAWLLNDTVKNNIIFD-NFYNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLS 809
Cdd:cd03248 79 SQYEH------KYLHSKVSLVGQEPVLFARSLQDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 810 GGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPlmKNRTCILVTHNVSlTLRNAHFAIVLENGKV 886
Cdd:cd03248 153 GGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWP--ERRTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1323-1555 |
1.80e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.30 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKID-LVTLRRSIT 1401
Cdd:COG1129 5 LEMRGISKSFGGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1402 IIPQDPILF-----------------AGTIksnvdpydeyDEKKIFKalsqvnlisshEFEEVLnseERFNSThnkfLNL 1464
Cdd:COG1129 83 IIHQELNLVpnlsvaeniflgreprrGGLI----------DWRAMRR-----------RARELL---ARLGLD----IDP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1465 HTEIAEgglnLSQGERQLLFIARSLLREPKIILLDEATSSI-DYDSDHLIqGIIRsEFNKS--TILTIAHRLRSVIDY-D 1540
Cdd:COG1129 135 DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLtEREVERLF-RIIR-RLKAQgvAIIYISHRLDEVFEIaD 208
|
250 260
....*....|....*....|.
gi 6321752 1541 RIIVM------DAGEVKEYDR 1555
Cdd:COG1129 209 RVTVLrdgrlvGTGPVAELTE 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1323-1566 |
2.23e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.28 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYaPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDI--SKIDLVTLRRSI 1400
Cdd:PRK13639 2 LETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDP--ILFAGTIKSNVD--------PYDEYdEKKIFKALSQVNLissHEFEEvlnseerfNSTHnkflnlhteiae 1470
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVAfgplnlglSKEEV-EKRVKEALKAVGM---EGFEN--------KPPH------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1471 gglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIrSEFNKS--TILTIAHRLRSVIDY-DRIIVMDA 1547
Cdd:PRK13639 137 ---HLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLL-YDLNKEgiTIIISTHDVDLVPVYaDKVYVMSD 212
|
250
....*....|....*....
gi 6321752 1548 GEVKEYDRPSELLKDERGI 1566
Cdd:PRK13639 213 GKIIKEGTPKEVFSDIETI 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1323-1550 |
2.28e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.90 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLP---PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKidLVTLRRS 1399
Cdd:COG1101 2 LELKNLSKTFNPGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK--LPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITI--IPQDPilFAGT-----IKSN----------------VDPydeyDEKKIFKA-LSQVNlisshefeevLNSEERfn 1455
Cdd:COG1101 80 KYIgrVFQDP--MMGTapsmtIEENlalayrrgkrrglrrgLTK----KRRELFRElLATLG----------LGLENR-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1456 sthnkflnLHTEIaegGLnLSQGERQLLfiarSLL----REPKIILLDEATSSIDYDSDHLI----QGIIRSefNKSTIL 1527
Cdd:COG1101 142 --------LDTKV---GL-LSGGQRQAL----SLLmatlTKPKLLLLDEHTAALDPKTAALVleltEKIVEE--NNLTTL 203
|
250 260
....*....|....*....|....
gi 6321752 1528 TIAHRLRSVIDY-DRIIVMDAGEV 1550
Cdd:COG1101 204 MVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1033-1290 |
2.81e-16 |
|
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: 81.06 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1033 KNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVdQE 1112
Cdd:cd07346 33 GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAV-QN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1113 LIPYLEVTIF-CLIQCASIIFLITVITPRFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTI 1191
Cdd:cd07346 112 LVSSGLLQLLsDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1192 RAFGDERRFILENMNKIDQNNRAFFYLSVTVKWFSFRVDMIG----AFIVLASGSFILLNIANIDSGLAgiSLTYAILFT 1267
Cdd:cd07346 192 KAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTalgtALVLLYGGYLVLQGSLTIGELVA--FLAYLGMLF 269
|
250 260
....*....|....*....|...
gi 6321752 1268 DGALWLVRLYSTFEMNMNSVERL 1290
Cdd:cd07346 270 GPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1323-1552 |
2.86e-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: 79.44 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPP--VIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIdlvtlRRSI 1400
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFA-GTIKSNVdpydeydekkIFkALSQVNLISSHEFEEVLNSEERFNSTHnkFLNLHteIAEgglnLSQGE 1479
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNV----------AL-GLELQGVPKAEARERAEELLELVGLSG--FENAY--PHQ----LSGGM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1480 RQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQ----GIIRSEfnKSTILTIAHRLRSVIdY--DRIIVMDA--GEVK 1551
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQeellDIWRET--GKTVLLVTHDIDEAV-FlaDRVVVLSArpGRIV 213
|
.
gi 6321752 1552 E 1552
Cdd:cd03293 214 A 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1323-1518 |
5.36e-16 |
|
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: 78.29 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTiitaLFR----LLEPITGCIKIDGQDISKiDLVTLRR 1398
Cdd:COG4133 3 LEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTT----LLRilagLLPPSAGEVLWNGEPIRD-AREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1399 SITIIPQDPILFAG-TIKSNVDPY-----DEYDEKKIFKALSQVNLisshefeevlnseERFnsthnkflnLHTEIAegg 1472
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRFWaalygLRADREAIDEALEAVGL-------------AGL---------ADLPVR--- 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6321752 1473 lNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIR 1518
Cdd:COG4133 131 -QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1323-1565 |
5.52e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.42 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDI-SKIDLVtlRRSIT 1401
Cdd:PRK13536 42 IDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1402 IIPQ-DPILFAGTIKSNVDPYDEYdekkiFKalsqvnlISSHEFEEVLNSEERFNSTHNKflnLHTEIAEgglnLSQGER 1480
Cdd:PRK13536 118 VVPQfDNLDLEFTVRENLLVFGRY-----FG-------MSTREIEAVIPSLLEFARLESK---ADARVSD----LSGGMK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1481 QLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEF--NKSTILTI-----AHRLrsvidYDRIIVMDAGEVKEY 1553
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLarGKTILLTThfmeeAERL-----CDRLCVLEAGRKIAE 253
|
250
....*....|..
gi 6321752 1554 DRPSELLKDERG 1565
Cdd:PRK13536 254 GRPHALIDEHIG 265
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1323-1536 |
5.91e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.70 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYapNLPPVIRNVSFKVdPQSKI-GIVGRTGAGKSTIITALFRLLE-----PITGCIKIDGQDI--SKIDLV 1394
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEI-YQSKVtAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1395 TLRRSITIIPQDPILFAGTIKSNVdpydEYDEKKI-FKALSQVNLIssheFEEVLNSEERFNSTHNKflnlhteIAEGGL 1473
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVgWRPKLEIDDI----VESALKDADLWDEIKHK-------IHKSAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321752 1474 NLSQGERQLLFIARSLLREPKIILLDEATSSID----YDSDHLIQGI-IRSEFnksTILTIAHRLRSV 1536
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLrLRSEL---TMVIVSHNLHQV 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1323-1532 |
6.25e-16 |
|
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: 76.81 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLrYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIdgqdiskidlvTLRRSITI 1402
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAGTIKSnvdpydeydekKIFKALSQVnlisshefeevlnseerfnsthnkflnlhteiaegglnLSQGERQL 1482
Cdd:cd03223 69 LPQRPYLPLGTLRE-----------QLIYPWDDV--------------------------------------LSGGEQQR 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6321752 1483 LFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFnkSTILTIAHR 1532
Cdd:cd03223 100 LAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1338-1517 |
8.66e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.22 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1338 PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSN 1417
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1418 VD-PY----DEYDEKKIFKALSQVNLIsshefEEVLNSeerfnsthnkflnlhtEIAEgglnLSQGERQLLFIARSLLRE 1492
Cdd:PRK10247 101 LIfPWqirnQQPDPAIFLDDLERFALP-----DTILTK----------------NIAE----LSGGEKQRISLIRNLQFM 155
|
170 180
....*....|....*....|....*
gi 6321752 1493 PKIILLDEATSSIDYDSDHLIQGII 1517
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEII 180
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1322-1534 |
9.75e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.06 E-value: 9.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1322 EIEIENLSLRYAPNLppVIRNVSFKVdPQSKI-GIVGRTGAGKSTIITALFRLLEPITGC-----IKIDGQDI--SKIDL 1393
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDI-PKNQItAFIGPSGCGKSTILRCFNRLNDLIPGFrvegkVTFHGKNLyaPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1394 VTLRRSITIIPQDPILFAGTIKSN------VDPY----DEYDEkkifKALSQVNLissheFEEVLNseerfnsthnkfln 1463
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPKSIYDNiaygarINGYkgdmDELVE----RSLRQAAL-----WDEVKD-------------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1464 lhtEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLR 1534
Cdd:PRK14243 144 ---KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1322-1562 |
1.14e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 79.29 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1322 EIEIENLSLRYAPNLPPVIR-----NVSFKvdPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDIS----KID 1392
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFERRalydvNVSIP--SGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1393 LVTLRRSITIIPQDP--ILFAGTIK-------SNVDPYDEYDEKKIFKALSQVNLIsshefEEVLnseerfnsTHNKFln 1463
Cdd:PRK13634 80 LKPLRKKVGIVFQFPehQLFEETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLP-----EELL--------ARSPF-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1464 lhteiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGI---IRSEFNKSTILtIAHRLRSVIDY- 1539
Cdd:PRK13634 145 ----------ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMfykLHKEKGLTTVL-VTHSMEDAARYa 213
|
250 260
....*....|....*....|...
gi 6321752 1540 DRIIVMDAGEVKEYDRPSELLKD 1562
Cdd:PRK13634 214 DQIVVMHKGTVFLQGTPREIFAD 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1342-1552 |
1.16e-15 |
|
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: 82.04 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1342 NVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLePITGCIKIDGQDISKID---LVTLRRSITIIPQDPilFA------- 1411
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGslsprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1412 -GTIKS------NVDPYDEYDEKKIFKALSQVNLISS------HEFeevlnseerfnsthnkflnlhteiaegglnlSQG 1478
Cdd:COG4172 381 vGQIIAeglrvhGPGLSAAERRARVAEALEEVGLDPAarhrypHEF-------------------------------SGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1479 ERQLLFIARSLLREPKIILLDEATSSIdydsDHLIQGII-------RSEFNKSTILtIAHRLRsVIDY--DRIIVMDAGE 1549
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSAL----DVSVQAQIldllrdlQREHGLAYLF-ISHDLA-VVRAlaHRVMVMKDGK 503
|
...
gi 6321752 1550 VKE 1552
Cdd:COG4172 504 VVE 506
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1338-1550 |
1.26e-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: 76.82 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1338 PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITAL--FRLLEPITGCIKIDGQDISKIdlvTLRRSITIIPQDPILFAG-TI 1414
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKR---SFRKIIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1415 KSNVDpydeydekkiFKALSQvnlisshefeevlnseerfnsthnkflnlhteiaegglNLSQGERQLLFIARSLLREPK 1494
Cdd:cd03213 100 RETLM----------FAAKLR--------------------------------------GLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1495 IILLDEATSSIDYDSDHLIQGIIR--SEFNKSTILTIaHRLRSVI--DYDRIIVMDAGEV 1550
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRrlADTGRTIICSI-HQPSSEIfeLFDKLLLLSQGRV 190
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1323-1531 |
1.41e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.35 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLppVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLE-----PITGCIKIDGQDI--SKIDLVT 1395
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1396 LRRSITIIPQDPILFAG-TIKSNV----------DPYDEYDEKkIFKALSQVNLissheFEEVLNSEERFNSthnkflnl 1464
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHlTIYDNVaigvklnglvKSKKELDER-VEWALKKAAL-----WDEVKDRLNDYPS-------- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 1465 hteiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAH 1531
Cdd:PRK14267 149 ---------NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1324-1564 |
1.56e-15 |
|
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: 78.16 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1324 EIENLSLRY----ApnlppvIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDIS--KIDLVT-- 1395
Cdd:COG0411 6 EVRGLTKRFgglvA------VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglPPHRIArl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1396 -LRRSITIIpqdpilfagtiksnvdpydeydekKIFKALSqV--NLI---SSHEFEEVLNSEERFNSTHNKFLNLHTEIA 1469
Cdd:COG0411 80 gIARTFQNP------------------------RLFPELT-VleNVLvaaHARLGRGLLAALLRLPRARREEREARERAE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1470 EG----GL---------NLSQGERQLLFIARSLLREPKIILLDEATSSIDY-DSDHLIQGI--IRSEFNKsTILTIAHRL 1533
Cdd:COG0411 135 ELlervGLadradepagNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPeETEELAELIrrLRDERGI-TILLIEHDM 213
|
250 260 270
....*....|....*....|....*....|..
gi 6321752 1534 RSVIDY-DRIIVMDAGEVKEYDRPSELLKDER 1564
Cdd:COG0411 214 DLVMGLaDRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1323-1531 |
1.67e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPnlPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLE-----PITGCIKIDGQDISKIDLVTLR 1397
Cdd:PRK14247 4 IEIRDLKVSFGQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1398 RSITIIPQ--DPI----LF---AGTIKSN--VDPYDEYDEkKIFKALSQVNLissheFEEVLNseeRFNSTHNKflnlht 1466
Cdd:PRK14247 82 RRVQMVFQipNPIpnlsIFenvALGLKLNrlVKSKKELQE-RVRWALEKAQL-----WDEVKD---RLDAPAGK------ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 1467 eiaegglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAH 1531
Cdd:PRK14247 147 --------LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1323-1559 |
2.03e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 79.76 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTiitaLFRL---LEPIT-GCIKIDGQDISkiDLVTLRR 1398
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTT----LLRMiagFETPDsGRILLDGRDVT--GLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1399 SITIIPQDPILFAG-TIKSNV--------DPYDEYDEKkIFKALSQVNLisshefEEVlnsEERFnsthnkflnlhteIA 1469
Cdd:COG3842 78 NVGMVFQDYALFPHlTVAENVafglrmrgVPKAEIRAR-VAELLELVGL------EGL---ADRY-------------PH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1470 EgglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDS-DHLIQGI--IRSEFNKSTI---------LTIAhrlrsvi 1537
Cdd:COG3842 135 Q----LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLrEEMREELrrLQRELGITFIyvthdqeeaLALA------- 203
|
250 260
....*....|....*....|..
gi 6321752 1538 dyDRIIVMDAGEVKEYDRPSEL 1559
Cdd:COG3842 204 --DRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1323-1548 |
2.83e-15 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 76.49 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKiDLVTLRRSITI 1402
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IpQDPILfagtiksnvdpYDEYDEKKIFKALSQVNLISSHEFEEVLNSEERFNSTHNKFlnlhteiaeGGLNLsqGERQL 1482
Cdd:cd03268 78 I-EAPGF-----------YPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKV---------KGFSL--GMKQR 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321752 1483 LFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKS-TILTIAHRLRSV-IDYDRIIVMDAG 1548
Cdd:cd03268 135 LGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGiTVLISSHLLSEIqKVADRIGIINKG 202
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1342-1562 |
3.46e-15 |
|
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: 78.99 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1342 NVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDG---QDISK-IDLVTLRRSITIIPQDPILFAG-TIKS 1416
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgIFLPPHRRRIGYVFQEARLFPHlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1417 NVdpydEYDEKKIFKALSQVnlisshEFEEVLnseerfnsthnKFLNLhteiaeGGL------NLSQGERQLLFIARSLL 1490
Cdd:COG4148 97 NL----LYGRKRAPRAERRI------SFDEVV-----------ELLGI------GHLldrrpaTLSGGERQRVAIGRALL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 1491 REPKIILLDEATSSIDYDSDHLIQGII---RSEFNKStILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPSELLKD 1562
Cdd:COG4148 150 SSPRLLLMDEPLAALDLARKAEILPYLerlRDELDIP-ILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
753-903 |
6.03e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.89 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 753 QSAW------LLNDTVKNNIIFDNF-YNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSS 825
Cdd:PRK11174 424 HLSWvgqnpqLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQP 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 826 AKHVLLDDCLSAVDSHTavwiyENCITGPL---MKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITEL-QSKGLF 901
Cdd:PRK11174 504 CQLLLLDEPTASLDAHS-----EQLVMQALnaaSRRQTTLMVTHQLE-DLAQWDQIWVMQDGQIVQQGDYAELsQAGGLF 577
|
..
gi 6321752 902 KE 903
Cdd:PRK11174 578 AT 579
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1324-1566 |
6.34e-15 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 76.02 E-value: 6.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1324 EIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKI---DLVtlRRSI 1400
Cdd:TIGR03410 2 EVSNLNVYYGQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLpphERA--RAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAG-TIKSNVD-------------PYDEYDekkIFKALsqvnlisshefEEVLNseeRfnsthnkflnlht 1466
Cdd:TIGR03410 78 AYVPQGREIFPRlTVEENLLtglaalprrsrkiPDEIYE---LFPVL-----------KEMLG---R------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1467 eiaEGGlNLSQGERQLLFIARSLLREPKIILLDEATS----SIDYDsdhlIQGIIRsEFNKS---TILTIAHRLRSVIDY 1539
Cdd:TIGR03410 128 ---RGG-DLSGGQQQQLAIARALVTRPKLLLLDEPTEgiqpSIIKD----IGRVIR-RLRAEggmAILLVEQYLDFAREL 198
|
250 260
....*....|....*....|....*...
gi 6321752 1540 -DRIIVMDAGEVKEYDRPSELlkDERGI 1566
Cdd:TIGR03410 199 aDRYYVMERGRVVASGAGDEL--DEDKV 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1327-1554 |
6.65e-15 |
|
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: 75.41 E-value: 6.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1327 NLSLRYAPNLPPVIRNVSFKVdPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQ---DISK-IDLVTLRRSITI 1402
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAG-TIKSNVD---PYDEYDEKKIFkalsqvnlissheFEEVLnseERFNSTHNKFLNLHTeiaegglnLSQG 1478
Cdd:cd03297 80 VFQQYALFPHlNVRENLAfglKRKRNREDRIS-------------VDELL---DLLGLDHLLNRYPAQ--------LSGG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1479 ERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIR---SEFNKSTILtIAHRLrSVIDY--DRIIVMDAGEVKEY 1553
Cdd:cd03297 136 EKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKqikKNLNIPVIF-VTHDL-SEAEYlaDRIVVMEDGRLQYI 213
|
.
gi 6321752 1554 D 1554
Cdd:cd03297 214 G 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1320-1569 |
7.11e-15 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 76.82 E-value: 7.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1320 DGEIEIENLSLRYAPnlppVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQdiskidlvtlrrs 1399
Cdd:cd03291 37 DNNLFFSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQDPILFAGTIKSNV---DPYDEYDEKKIFKAlSQVNlisshefEEVLNSEERFNsthnkflnlhTEIAEGGLNLS 1476
Cdd:cd03291 100 ISFSSQFSWIMPGTIKENIifgVSYDEYRYKSVVKA-CQLE-------EDITKFPEKDN----------TVLGEGGITLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1477 QGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLI--QGIIRSEFNKSTILtIAHRLRSVIDYDRIIVMDAGEVKEYD 1554
Cdd:cd03291 162 GGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfeSCVCKLMANKTRIL-VTSKMEHLKKADKILILHEGSSYFYG 240
|
250
....*....|....*
gi 6321752 1555 RPSElLKDERGIFYS 1569
Cdd:cd03291 241 TFSE-LQSLRPDFSS 254
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
757-901 |
8.04e-15 |
|
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: 79.48 E-value: 8.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 757 LLNDTVKNNIIfdnfY-----NEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLL 831
Cdd:COG5265 443 LFNDTIAYNIA----YgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIF 518
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 832 DDCLSAVDSHTavwiyENCITGPLM---KNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITEL-QSKGLF 901
Cdd:COG5265 519 DEATSALDSRT-----ERAIQAALRevaRGRTTLVIAHRLS-TIVDADEILVLEAGRIVERGTHAELlAQGGLY 586
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1339-1552 |
2.11e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.21 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1339 VIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLePITGCIKIDGQDISKID---LVTLRRSITIIPQDPilfagtiK 1415
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP-------N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1416 SNVDPydeydekkifkALSQVNLIsshefEEVLNSEERFNSTHNKFLNLHTEIAEGGLN----------LSQGERQLLFI 1485
Cdd:PRK15134 373 SSLNP-----------RLNVLQII-----EEGLRVHQPTLSAAQREQQVIAVMEEVGLDpetrhrypaeFSGGQRQRIAI 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1486 ARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTI--LTIAHRLRSVIDY-DRIIVMDAGEVKE 1552
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALcHQVIVLRQGEVVE 506
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1323-1553 |
4.96e-14 |
|
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: 72.70 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDlvtlRRSITI 1402
Cdd:cd03269 1 LEVENVTKRFGRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILfagtiksnvdpYDEYDEKKIFKALSQVNLISSHEF-EEVLNSEERFNSTHNKFLNLHTeiaegglnLSQGERQ 1481
Cdd:cd03269 75 LPEERGL-----------YPKMKVIDQLVYLAQLKGLKKEEArRRIDEWLERLELSEYANKRVEE--------LSKGNQQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 1482 LLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS-EFNKSTILTIAHRLRSVIDY-DRIIVMDAGEVKEY 1553
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEELcDRVLLLNKGRAVLY 209
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1355-1550 |
5.59e-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: 72.53 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1355 IVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVtlRRSITIIPQDPILFAG-TIKSNVD----P---YDEYDE 1426
Cdd:cd03298 29 IVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGlglsPglkLTAEDR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1427 KKIFKALSQVNLissHEFEEVLNSEerfnsthnkflnlhteiaegglnLSQGERQLLFIARSLLREPKIILLDEATSSID 1506
Cdd:cd03298 107 QAIEVALARVGL---AGLEKRLPGE-----------------------LSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6321752 1507 ----YDSDHLIQGIIRSEfnKSTILTIAHRLRSVID-YDRIIVMDAGEV 1550
Cdd:cd03298 161 palrAEMLDLVLDLHAET--KMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1339-1556 |
6.69e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.57 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1339 VIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKID---LVTLRRSITIIPQDPIlfagtik 1415
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSI------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1416 SNVDPydeydEKKIFKALSQV--NLISSHEFEEVLNSEERFNSthnkfLNLHTEIAEG-GLNLSQGERQLLFIARSLLRE 1492
Cdd:PRK10419 100 SAVNP-----RKTVREIIREPlrHLLSLDKAERLARASEMLRA-----VDLDDSVLDKrPPQLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1493 PKIILLDEATSSIDYdsdHLIQGII------RSEFNkSTILTIAHRLRSVIDY-DRIIVMDAGEVKEyDRP 1556
Cdd:PRK10419 170 PKLLILDEAVSNLDL---VLQAGVIrllkklQQQFG-TACLFITHDLRLVERFcQRVMVMDNGQIVE-TQP 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1323-1560 |
1.25e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.90 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLS--LRYAPNL-----PPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVT 1395
Cdd:PRK15112 5 LEVRNLSktFRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1396 LRRSITIIPQDPI-----------LFAGTIKSNVDPYDEYDEKKIFKALSQVNLISSHefeevlnseerfnsthnkfLNL 1464
Cdd:PRK15112 85 RSQRIRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDH-------------------ASY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1465 HTEIaegglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYD-SDHLI---------QGIirsefnkSTILTIAHRLR 1534
Cdd:PRK15112 146 YPHM------LAPGQKQRLGLARALILRPKVIIADEALASLDMSmRSQLInlmlelqekQGI-------SYIYVTQHLGM 212
|
250 260
....*....|....*....|....*.
gi 6321752 1535 SVIDYDRIIVMDAGEVKEYDRPSELL 1560
Cdd:PRK15112 213 MKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
665-886 |
1.55e-13 |
|
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: 71.41 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 665 EFKNATLTWNENdsdmNAFKlcGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKHDLipdcegl 744
Cdd:cd03235 1 EVEDLTVSYGGH----PVLE--DVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 745 tNSFAYCSQSA---WLLNDTVKN--------NIIFDNFYNEDRYNKVIDAcgLKRdleilpaGDLTEIGEKGI-TLSGGQ 812
Cdd:cd03235 68 -KRIGYVPQRRsidRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEA--LER-------VGLSELADRQIgELSGGQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 813 KQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENcITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKV 886
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYEL-LRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1323-1581 |
1.79e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.57 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYaPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQ--DISKIDLVTLRRSI 1400
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDP--ILFAGTIKSNVDpydeydekkiFKALSqVNLISSHEFEEVLNSEERFNSTHNKFLNLHTeiaegglnLSQG 1478
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVS----------FGAVN-LKLPEDEVRKRVDNALKRTGIEHLKDKPTHC--------LSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1479 ERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKS--TILTIAHRLRSVIDY-DRIIVMDAGEVKEYDR 1555
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYcDNVFVMKEGRVILQGN 225
|
250 260
....*....|....*....|....*....
gi 6321752 1556 PSELLKDE---RGIFYSMCRDSGGLELLK 1581
Cdd:PRK13636 226 PKEVFAEKemlRKVNLRLPRIGHLMEILK 254
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1323-1563 |
1.99e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.46 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYaPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:PRK13647 5 IEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDP--ILFAGTIKSNVdpydeydekkifkALSQVNLISSHefEEVlnsEERFNSTHnKFLNLHTEIAEGGLNLSQGER 1480
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDV-------------AFGPVNMGLDK--DEV---ERRVEEAL-KAVRMWDFRDKPPYHLSYGQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1481 QLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIrSEFNK--STILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPS 1557
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEIL-DRLHNqgKTVIVATHDVDLAAEWaDQVIVLKEGRVLAEGDKS 223
|
....*.
gi 6321752 1558 eLLKDE 1563
Cdd:PRK13647 224 -LLTDE 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1340-1562 |
3.10e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.53 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1340 IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLR-----------RSITIIPQDPI 1408
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1409 LFAGTIKSNVD--PYDEYDEKKIfKALSQVNLIS-SHEFEEvlnseerfnsthnkflnlhteiaegglNLSQGERQLLFI 1485
Cdd:PRK10070 124 LDNTAFGMELAgiNAEERREKAL-DALRQVGLENyAHSYPD---------------------------ELSGGMRQRVGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1486 ARSLLREPKIILLDEATSSIdydsDHLIQGIIRSEF------NKSTILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPSE 1558
Cdd:PRK10070 176 ARALAINPDILLMDEAFSAL----DPLIRTEMQDELvklqakHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDE 251
|
....
gi 6321752 1559 LLKD 1562
Cdd:PRK10070 252 ILNN 255
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
664-890 |
4.05e-13 |
|
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: 69.26 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDSDMnafkLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSlEPKHDLIpdcEG 743
Cdd:cd03247 1 LSINNVSFSYPEQEQQV----LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG-VPVSDLE---KA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 744 LTNSFAYCSQSAWLLNDTVKNNIifdnfynedrynkvidacglkrdleilpagdlteigekGITLSGGQKQRISLARAVY 823
Cdd:cd03247 73 LSSLISVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 824 SSAKHVLLDDCLSAVDSHTAVWIYENCITgpLMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQG 890
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
750-887 |
4.13e-13 |
|
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: 74.01 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 750 YCSQSAWLLNDTVKNNIIfdNFYNEDRyNKVIDACglKR----DLeI--LPAGDLTEIGEKGITLSGGQKQRISLARAVY 823
Cdd:COG4618 410 YLPQDVELFDGTIAENIA--RFGDADP-EKVVAAA--KLagvhEM-IlrLPDGYDTRIGEGGARLSGGQRQRIGLARALY 483
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321752 824 SSAKHVLLDDCLSAVDS--HTAVwiyENCITGplMKNR--TCILVTHNVSLtLRNAHFAIVLENGKVK 887
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDegEAAL---AAAIRA--LKARgaTVVVITHRPSL-LAAVDKLLVLRDGRVQ 545
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1323-1559 |
4.93e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.37 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPpVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDP--ILFAGTIKSNVdpydeydekkifkALSQVNL-----ISSHEFEEVLN----SEERFNSTHnkflnlhteiaeg 1471
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDI-------------AFGPINLgldeeTVAHRVSSALHmlglEELRDRVPH------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1472 glNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDS-DHLIQGIIR-SEFNKSTILTIAHRLRSVIDY-DRIIVMDAG 1548
Cdd:PRK13652 137 --HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGvKELIDFLNDlPETYGMTVIFSTHQLDLVPEMaDYIYVMDKG 214
|
250
....*....|.
gi 6321752 1549 EVKEYDRPSEL 1559
Cdd:PRK13652 215 RIVAYGTVEEI 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1323-1552 |
5.57e-13 |
|
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: 73.57 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYA--PNLPPVIRNVSFKVDPQSKIGIVGRTGAGKStiITAL--FRLLEP----ITGCIKIDGQDISKIDLV 1394
Cdd:COG4172 7 LSVEDLSVAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKS--VTALsiLRLLPDpaahPSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1395 TLRR----SITIIPQDPI-----LFagTIksnvdpydeydEKKIFKALSQVNLISSHE--------FEEV--LNSEERFN 1455
Cdd:COG4172 85 ELRRirgnRIAMIFQEPMtslnpLH--TI-----------GKQIAEVLRLHRGLSGAAararalelLERVgiPDPERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1456 S-THnkflnlhteiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYdsdhLIQGII-------RSEFNKStIL 1527
Cdd:COG4172 152 AyPH---------------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQAQIldllkdlQRELGMA-LL 211
|
250 260
....*....|....*....|....*.
gi 6321752 1528 TIAHRLRSVIDY-DRIIVMDAGEVKE 1552
Cdd:COG4172 212 LITHDLGVVRRFaDRVAVMRQGEIVE 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1323-1560 |
5.73e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSL--RYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKStiITAL--FRLLE--PI---TGCIKIDGQDISKIDL 1393
Cdd:PRK15134 6 LAIENLSVafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKS--VTALsiLRLLPspPVvypSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1394 VTLRR----SITIIPQDPILfagtiksNVDPYDEYdEKKIFKALSqvnLISSHEFE----EVLNSEERFNSTHnkflnlh 1465
Cdd:PRK15134 84 QTLRGvrgnKIAMIFQEPMV-------SLNPLHTL-EKQLYEVLS---LHRGMRREaargEILNCLDRVGIRQ------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1466 teiAEGGLN-----LSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIR---SEFNKStILTIAHRLRSVI 1537
Cdd:PRK15134 146 ---AAKRLTdyphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelqQELNMG-LLFITHNLSIVR 221
|
250 260
....*....|....*....|....
gi 6321752 1538 DY-DRIIVMDAGEVKEYDRPSELL 1560
Cdd:PRK15134 222 KLaDRVAVMQNGRCVEQNRAATLF 245
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1323-1565 |
5.90e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.37 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLppVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTlRRSITI 1402
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQdpilFagtikSNVDPydEYDEKKIFKALSQVNLISSHEFEEVLNSEERFNSTHNKflnlhteiAEGGL-NLSQGERQ 1481
Cdd:PRK13537 85 VPQ----F-----DNLDP--DFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENK--------ADAKVgELSGGMKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1482 LLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNK-STILTIAH------RLrsvidYDRIIVMDAGEVKEYD 1554
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEG 220
|
250
....*....|.
gi 6321752 1555 RPSELLKDERG 1565
Cdd:PRK13537 221 APHALIESEIG 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1323-1549 |
5.91e-13 |
|
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: 67.86 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGcikidgqdiskidlvtlrrSITI 1402
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-------------------IVTW 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFagtiksnvdpydeydekkifkaLSQvnlisshefeevlnseerfnsthnkflnlhteiaegglnLSQGERQL 1482
Cdd:cd03221 60 GSTVKIGY----------------------FEQ---------------------------------------LSGGEKMR 78
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1483 LFIARSLLREPKIILLDEATSSIDYDS-DHLIQGIirSEFnKSTILTIAH-R--LRSVIdyDRIIVMDAGE 1549
Cdd:cd03221 79 LALAKLLLENPNLLLLDEPTNHLDLESiEALEEAL--KEY-PGTVILVSHdRyfLDQVA--TKIIELEDGK 144
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
689-836 |
6.09e-13 |
|
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: 68.06 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 689 NIKFQI--GKLNLILGSTGSGKSALLLGLLGELNLISGSIivpSLEPKHDLIPDCEGLTNSFAYCSQSAWLLND-TVKNN 765
Cdd:pfam00005 3 NVSLTLnpGEILALVGPNGAGKSTLLKLIAGLLSPTEGTI---LLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 766 IIFdNFYNEDRYNKVIDAcGLKRDLEILPAGDL--TEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLS 836
Cdd:pfam00005 80 LRL-GLLLKGLSKREKDA-RAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1323-1554 |
6.87e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.18 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTiitaLFRLL----EPITGCIKIdGQdiskidlvTLRr 1398
Cdd:COG0488 316 LELEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLLagelEPDSGTVKL-GE--------TVK- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1399 sITIIPQDPILFagtiksnvDPydeydEKKIFKALSQVNlisshefEEVLNSE-----ERFNSTHNKflnLHTEIAeggl 1473
Cdd:COG0488 380 -IGYFDQHQEEL--------DP-----DKTVLDELRDGA-------PGGTEQEvrgylGRFLFSGDD---AFKPVG---- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1474 NLSQGERQLLFIARSLLREPKIILLDEATSSIDYDS-DHLIQGIIrsEFnKSTILTIAH-R--LRSVIdyDRIIVMDAGE 1549
Cdd:COG0488 432 VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETlEALEEALD--DF-PGTVLLVSHdRyfLDRVA--TRILEFEDGG 506
|
....*
gi 6321752 1550 VKEYD 1554
Cdd:COG0488 507 VREYP 511
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1323-1564 |
6.88e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.57 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:PRK13548 3 LEARNLSVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPIL-FAGTIKSNV----DPYDEY---DEKKIFKALSQVnlisshefeEVLNSEERFNSThnkflnlhteiaeggln 1474
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVamgrAPHGLSraeDDALVAAALAQV---------DLAHLAGRDYPQ----------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1475 LSQGERQLLFIARSLLR------EPKIILLDEATSSIDydsdhliqgiIRsefNKSTILTIAHRL-----RSVI----D- 1538
Cdd:PRK13548 135 LSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD----------LA---HQHHVLRLARQLahergLAVIvvlhDl 201
|
250 260 270
....*....|....*....|....*....|..
gi 6321752 1539 -----Y-DRIIVMDAGEVKEYDRPSELLKDER 1564
Cdd:PRK13548 202 nlaarYaDRIVLLHQGRLVADGTPAEVLTPET 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1323-1550 |
8.64e-13 |
|
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: 69.21 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISkiDLVTLRRSITI 1402
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILF---------AGTIKSNVDPYDEYDEKkifkalsqvnlisSHEFEEVLNSEErfnsthnkFLNLHTEiaeggl 1473
Cdd:cd03301 77 VFQNYALYphmtvydniAFGLKLRKVPKDEIDER-------------VREVAELLQIEH--------LLDRKPK------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1474 NLSQGERQLLFIARSLLREPKIILLDEATSSIdydsDHLIQGIIRSEFNK------STILTIAHrlrsviDY-------D 1540
Cdd:cd03301 130 QLSGGQRQRVALGRAIVREPKVFLMDEPLSNL----DAKLRVQMRAELKRlqqrlgTTTIYVTH------DQveamtmaD 199
|
250
....*....|
gi 6321752 1541 RIIVMDAGEV 1550
Cdd:cd03301 200 RIAVMNDGQI 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1318-1550 |
9.81e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.45 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1318 PKDGEIEIENLSLRYAPNlppvIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKID----- 1392
Cdd:PRK10982 246 PGEVILEVRNLTSLRQPS----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneai 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1393 -----LVTL-RRSITIIPQDPILFAGTIkSNVDPYdeydeKKIFKALSQVNLISSHEFeeVLNSEERFNSTHnkflnlHT 1466
Cdd:PRK10982 322 nhgfaLVTEeRRSTGIYAYLDIGFNSLI-SNIRNY-----KNKVGLLDNSRMKSDTQW--VIDSMRVKTPGH------RT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1467 EIAegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKST-ILTIAHRLRSVIDY-DRIIV 1544
Cdd:PRK10982 388 QIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKgIIIISSEMPELLGItDRILV 463
|
....*.
gi 6321752 1545 MDAGEV 1550
Cdd:PRK10982 464 MSNGLV 469
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
744-909 |
1.15e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.52 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 744 LTNSFAYCSQSAWLLNDTVKNNIIF--DNFYNEDrYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARA 821
Cdd:PTZ00265 1294 LRNLFSIVSQEPMLFNMSIYENIKFgkEDATRED-VKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARA 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 822 VYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSlTLRNAHFAIVLENGK-----VKNQGTITELQ 896
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVVFNNPDrtgsfVQAHGTHEELL 1451
|
170
....*....|....*
gi 6321752 897 S--KGLFKeKYVQLS 909
Cdd:PTZ00265 1452 SvqDGVYK-KYVKLA 1465
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
659-891 |
1.47e-12 |
|
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: 68.21 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 659 PDKNKIEFKNATLTWNENDSDMnafkLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKHdlI 738
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPV----LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIST--I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 739 PdCEGLTNSFAYCSQSAWLLNDTVKNNIifdnfyneDRYNKVIDAcglkrdlEILPAgdlTEIGEKGITLSGGQKQRISL 818
Cdd:cd03369 76 P-LEDLRSSLTIIPQDPTLFSGTIRSNL--------DPFDEYSDE-------EIYGA---LRVSEGGLNLSQGQRQLLCL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 819 ARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncITGPLMKNRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGT 891
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDALIQK--TIREEFTNSTILTIAHRLR-TIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
797-890 |
1.62e-12 |
|
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: 67.46 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 797 DLTEIGEKGI-TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNA 875
Cdd:cd03214 86 GLAHLADRPFnELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYA 165
|
90
....*....|....*
gi 6321752 876 HFAIVLENGKVKNQG 890
Cdd:cd03214 166 DRVILLKDGRIVAQG 180
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
689-886 |
2.10e-12 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 67.92 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 689 NIKFQI--GKLNLILGSTGSGKS------AlllgllgelnlisgsiivpslepkhDLIPDCEG--------LTNS----- 747
Cdd:COG4619 18 PVSLTLeaGECVAITGPSGSGKStllralA-------------------------DLDPPTSGeiyldgkpLSAMpppew 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 748 ---FAYCSQSAWLLNDTVKNNIIFDNFYNEDRYNKVIdacgLKRDLEI--LPAGDL-TEIGEkgitLSGGQKQRISLARA 821
Cdd:COG4619 73 rrqVAYVPQEPALWGGTVRDNLPFPFQLRERKFDRER----ALELLERlgLPPDILdKPVER----LSGGERQRLALIRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 822 ------VYssakhvLLDDCLSAVDSHTA----VWIYENCitgpLMKNRTCILVTHNVSLTLRNAHFAIVLENGKV 886
Cdd:COG4619 145 lllqpdVL------LLDEPTSALDPENTrrveELLREYL----AEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
616-912 |
2.18e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.67 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 616 LKTPLDQLSNMLSFINQSKVSLKRIsdFLRMDDT-EKYNQLTISPDKNKIEFKNATLTWNENdsdmnafKLCGLNIKFQI 694
Cdd:PRK10790 294 LNEPLIELTTQQSMLQQAVVAGERV--FELMDGPrQQYGNDDRPLQSGRIDIDNVSFAYRDD-------NLVLQNINLSV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 695 GKLNLI--LGSTGSGKSALLLGLLGELNLISGSIIV---PSLEPKHDLipdcegLTNSFAYCSQSAWLLNDTVKNNIIFD 769
Cdd:PRK10790 365 PSRGFValVGHTGSGKSTLASLLMGYYPLTEGEIRLdgrPLSSLSHSV------LRQGVAMVQQDPVVLADTFLANVTLG 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 770 NFYNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTavwiyEN 849
Cdd:PRK10790 439 RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT-----EQ 513
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321752 850 CITGPLMKNR---TCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITEL-QSKGLFKEKY-VQLSSRD 912
Cdd:PRK10790 514 AIQQALAAVRehtTLVVIAHRLS-TIVEADTILVLHRGQAVEQGTHQQLlAAQGRYWQMYqLQLAGEE 580
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1327-1533 |
2.90e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.97 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1327 NLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGC-----IKIDGQDISKI-DLVTLRRSI 1400
Cdd:PRK14271 26 NLTLGFAGK--TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQDPILFAGTIKSNVdpydeydekkiFKALSQVNLISSHEFEEVlnSEERFNSThNKFLNLHTEIAEGGLNLSQGER 1480
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNV-----------LAGVRAHKLVPRKEFRGV--AQARLTEV-GLWDAVKDRLSDSPFRLSGGQQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6321752 1481 QLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRL 1533
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1323-1550 |
4.24e-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: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLppVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVT------- 1395
Cdd:COG4152 2 LELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1396 --LRRSITIIPQdpILFAGTIKSnvdpydeYDEKKIFKALsqvnlisshefEEVLnseERFNSTHNKFLNLHTeiaeggl 1473
Cdd:COG4152 80 rgLYPKMKVGEQ--LVYLARLKG-------LSKAEAKRRA-----------DEWL---ERLGLGDRANKKVEE------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1474 nLSQGERQLL-FIArSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS--TILTIAHRLRSVIDY-DRIIVMDAGE 1549
Cdd:COG4152 130 -LSKGNQQKVqLIA-ALLHDPELLILDEPFSGLDPVNVELLKDVIR-ELAAKgtTVIFSSHQMELVEELcDRIVIINKGR 206
|
.
gi 6321752 1550 V 1550
Cdd:COG4152 207 K 207
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1345-1568 |
5.36e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.98 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1345 FKVDPQSKIGIVGRTGAGKSTIITALFRLLEP---ITGCIKIDGQDI---SKIDLVTLR-RSITIIPQDPIlfagtikSN 1417
Cdd:PRK09473 37 FSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlPEKELNKLRaEQISMIFQDPM-------TS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1418 VDPYdeydeKKIFKALSQV-----NLISSHEFEE-------VLNSEERfnsthnKFLNLHTEIAEGGLnlsqgeRQLLFI 1485
Cdd:PRK09473 110 LNPY-----MRVGEQLMEVlmlhkGMSKAEAFEEsvrmldaVKMPEAR------KRMKMYPHEFSGGM------RQRVMI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1486 ARSLLREPKIILLDEATSSIDYDSDHLIQGI---IRSEFNkSTILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPsellk 1561
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLlneLKREFN-TAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNA----- 246
|
....*..
gi 6321752 1562 deRGIFY 1568
Cdd:PRK09473 247 --RDVFY 251
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1323-1566 |
6.09e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.71 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLppVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDIS-----KIDL---- 1393
Cdd:PRK11300 6 LSVSGLMMRFGGLL--AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpghQIARmgvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1394 -----VTLRRSITIIPQDPI---------LFAGTIKSnvdP-YDEYDEKKIFKA---LSQVNLisshefeevlnseerfn 1455
Cdd:PRK11300 84 rtfqhVRLFREMTVIENLLVaqhqqlktgLFSGLLKT---PaFRRAESEALDRAatwLERVGL----------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1456 sthnkflnlhTEIA--EGGlNLSQGERQLLFIARSLLREPKIILLDEATSSID----YDSDHLIqGIIRSEFNKStILTI 1529
Cdd:PRK11300 144 ----------LEHAnrQAG-NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNpketKELDELI-AELRNEHNVT-VLLI 210
|
250 260 270
....*....|....*....|....*....|....*...
gi 6321752 1530 AHRLRSVIDY-DRIIVMDAGEVKEYDRPSELLKDERGI 1566
Cdd:PRK11300 211 EHDMKLVMGIsDRIYVVNQGTPLANGTPEEIRNNPDVI 248
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1323-1564 |
6.15e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 67.45 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITI 1402
Cdd:COG4559 2 LEAENLSVRLGGR--TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQD-PILFAGTIKSNV----DPYDEY---DEKKIFKALSQVnlisshefeEVLNSEERFNSThnkflnlhteiaeggln 1474
Cdd:COG4559 80 LPQHsSLAFPFTVEEVValgrAPHGSSaaqDRQIVREALALV---------GLAHLAGRSYQT----------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1475 LSQGERQLLFIARSLL-------REPKIILLDEATSSIDydsdhliqgiIRsefNKSTILTIAHRLRS----VI----D- 1538
Cdd:COG4559 134 LSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD----------LA---HQHAVLRLARQLARrgggVVavlhDl 200
|
250 260 270
....*....|....*....|....*....|..
gi 6321752 1539 -----Y-DRIIVMDAGEVKEYDRPSELLKDER 1564
Cdd:COG4559 201 nlaaqYaDRILLLHQGRLVAQGTPEEVLTDEL 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
465-911 |
7.05e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 70.24 E-value: 7.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 465 YLYV---TVQAVIMIIVVVGLL--FNF-LGVSAFAGISIILVMFPLNFLLanlLGKFQKQTLkcTDQRI---SKLNECLQ 535
Cdd:PRK11160 134 YLRLispLVAALVVILVLTIGLsfFDLtLALTLGGILLLLLLLLPLLFYR---LGKKPGQDL--THLRAqyrVQLTEWLQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 536 NIRIVKYFAWERNIINEIKSIRQKELRS-------------LLKKSLVWSVTSFLWFVtptlVTGVTFAictfVQHEDLN 602
Cdd:PRK11160 209 GQAELTLFGAEDRYRQQLEQTEQQWLAAqrrqanltglsqaLMILANGLTVVLMLWLA----AGGVGGN----AQPGALI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 603 APLAFTTLSLFTLLkTPLdqlsnMLSF--INQSKVSLKRISDFLRMDDTEKYN-QLTISPDKNKIEFKNATLTWNenDSD 679
Cdd:PRK11160 281 ALFVFAALAAFEAL-MPV-----AGAFqhLGQVIASARRINEITEQKPEVTFPtTSTAAADQVSLTLNNVSFTYP--DQP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 680 MNAFKlcGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVpSLEPKHDLipDCEGLTNSFAYCSQSAWLLN 759
Cdd:PRK11160 353 QPVLK--GLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL-NGQPIADY--SEAALRQAISVVSQRVHLFS 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 760 DTVKNNIIF-DNFYNEDRYNKVIDACGLKRDLEILPAGDLTeIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAV 838
Cdd:PRK11160 428 ATLRDNLLLaAPNASDEALIEVLQQVGLEKLLEDDKGLNAW-LGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 839 DSHTAVWIYENCITgpLMKNRTCILVTHNvsltLRN-AHF--AIVLENGKVKNQGTITELQSKglfKEKYVQLSSR 911
Cdd:PRK11160 507 DAETERQILELLAE--HAQNKTVLMITHR----LTGlEQFdrICVMDNGQIIEQGTHQELLAQ---QGRYYQLKQR 573
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1323-1562 |
9.61e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.84 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPVIR---NVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKI----DLVT 1395
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1396 LRRSITIIPQDP--ILFAGTIKSNVdpydeydekkifkALSQVNLISSHEFEEVLNSEERfnsthnKFLNLHTEIAEGG- 1472
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDV-------------AFGPQNFGIPKEKAEKIAAEKL------EMVGLADEFWEKSp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1473 LNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS-EFNKSTILTIAHRLRSVIDY-DRIIVMDAGEV 1550
Cdd:PRK13643 143 FELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYaDYVYLLEKGHI 222
|
250
....*....|..
gi 6321752 1551 KEYDRPSELLKD 1562
Cdd:PRK13643 223 ISCGTPSDVFQE 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1340-1562 |
9.87e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.50 E-value: 9.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1340 IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDI-SKID---LVTLRRSITIIPQDP--ILFAGT 1413
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKdkyIRPVRKRIGMVFQFPesQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1414 IksnvdpydeydEKKIfkalsqvnLISSHEFEevLNSEERFNSTHNKFLNLHTE---IAEGGLNLSQGERQLLFIARSLL 1490
Cdd:PRK13646 103 V-----------EREI--------IFGPKNFK--MNLDEVKNYAHRLLMDLGFSrdvMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 1491 REPKIILLDEATSSIDYDSDHLIQGIIRS---EFNKsTILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPSELLKD 1562
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqtDENK-TIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKELFKD 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1261-1562 |
1.04e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.45 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1261 TYAILFTDGALWLVRLYSTF-EMNMNSVERLKEYSSIEQENYLghdegrilllnepswpkdgeIEIENLSLRYAPNLPPV 1339
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVvAVFMEGVSEVEKECEVEVGEPI--------------------IKVRNVSKRYISVDRGV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1340 IR---NVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITG--CIKI------------DGQDISKIDLVTLRRSITI 1402
Cdd:TIGR03269 297 VKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVgdewvdmtkpgpDGRGRAKRYIGILHQEYDL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAGTIKSNVDPYDEYDEKKIFKALSQVNLiSSHEFEEVLNseeRFNSThnkflnlhteiaegglnLSQGERQL 1482
Cdd:TIGR03269 377 YPHRTVLDNLTEAIGLELPDELARMKAVITLKMVGF-DEEKAEEILD---KYPDE-----------------LSEGERHR 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1483 LFIARSLLREPKIILLDEATSSIDYDSDHLIQGII---RSEFNKsTILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPSE 1558
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDPEE 514
|
....
gi 6321752 1559 LLKD 1562
Cdd:TIGR03269 515 IVEE 518
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1323-1548 |
1.14e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYapnlPPV--IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKID-LVTLRRS 1399
Cdd:PRK09700 6 ISMAGIGKSF----GPVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQD-PILFAGTIKSNVdpydeYDEKKIFKALSQVNLISSHEFEEVlnseerfNSTHNKFLNLHTEIAEGGLNLSQG 1478
Cdd:PRK09700 82 IGIIYQElSVIDELTVLENL-----YIGRHLTKKVCGVNIIDWREMRVR-------AAMMLLRVGLKVDLDEKVANLSIS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321752 1479 ERQLLFIARSLLREPKIILLDEATSSI-DYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDY-DRIIVMDAG 1548
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
688-890 |
1.37e-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: 65.78 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 688 LNIKFQI-GKLNLILGSTGSGKS------ALLLGLLGELNLISGSIIVPSlEPKHDLIPDCEGLtnsfAYCSQSAWLL-N 759
Cdd:cd03297 15 LKIDFDLnEEVTGIFGASGAGKStllrciAGLEKPDGGTIVLNGTVLFDS-RKKINLPPQQRKI----GLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 760 DTVKNNIIFDNFYNEDRYNKVidacglkRDLEILPAGDLTEIGEKGI-TLSGGQKQRISLARAVYSSAKHVLLDDCLSAV 838
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRI-------SVDELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6321752 839 DSHTAvwiyENCItgPLMK------NRTCILVTHNVSLTLRNAHFAIVLENGKVKNQG 890
Cdd:cd03297 163 DRALR----LQLL--PELKqikknlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1339-1550 |
1.41e-11 |
|
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: 65.76 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1339 VIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEP---ITGCIKIDGQDISKidlVTLRRSITIIPQDPILFagtik 1415
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP---DQFQKCVAYVRQDDILL----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1416 snvdPYDEYDEKKIFKALSQVNLISSHEFEEVLNSEERFNSTHNKFLNlHTEIAegglNLSQGERQLLFIARSLLREPKI 1495
Cdd:cd03234 94 ----PGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIG-GNLVK----GISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 1496 ILLDEATSSIDYDSDHLIQGIIR--SEFNKSTILTIaHRLRSVI--DYDRIIVMDAGEV 1550
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSqlARRNRIVILTI-HQPRSDLfrLFDRILLLSSGEI 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1338-1550 |
1.64e-11 |
|
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: 65.82 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1338 PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGqdiskidLVTLRRSITIIPQDPILFA--GTIK 1415
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-------LVPWKRRKKFLRRIGVVFGqkTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1416 SNVDPYDEYdekKIFKALSQVnlisshefeevlnSEERFNSTHNKF---LNLHTEIAEGGLNLSQGERQLLFIARSLLRE 1492
Cdd:cd03267 108 WDLPVIDSF---YLLAAIYDL-------------PPARFKKRLDELselLDLEELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321752 1493 PKIILLDEATSSIDYDSDHLIQGIIRsEFNK---STILTIAHRLRSVIDY-DRIIVMDAGEV 1550
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLK-EYNRergTTVLLTSHYMKDIEALaRRVLVIDKGRL 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1319-1563 |
1.66e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.18 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1319 KDGEI-EIENLSLRY---APNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKID----GQDISK 1390
Cdd:PRK13631 17 SDDIIlRVKNLYCVFdekQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1391 IDLVT------------LRRSITIIPQDP--ILFAGTIksnvdpydeydEKKIFkaLSQVNLISSHEfeevlNSEERFNS 1456
Cdd:PRK13631 97 HELITnpyskkiknfkeLRRRVSMVFQFPeyQLFKDTI-----------EKDIM--FGPVALGVKKS-----EAKKLAKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1457 THNKFLNLHTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDH-LIQGIIRSEFNKSTILTIAHRLRS 1535
Cdd:PRK13631 159 YLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEH 238
|
250 260
....*....|....*....|....*....
gi 6321752 1536 VIDY-DRIIVMDAGEVKEYDRPSELLKDE 1563
Cdd:PRK13631 239 VLEVaDEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1306-1551 |
1.88e-11 |
|
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: 68.31 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1306 EGRILLLNEPSWPKDGEIEIENLSLrYAPNLPPVIR--NVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLE-PITGCIK 1382
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTC-WDVINPHRKRvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVF 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1383 IDGQDIS-KIDLVTLRRSITIIPQD-------PILFAG-----------TIKSNVDpyDEYDEKKIFKALSQVNLISSHE 1443
Cdd:TIGR02633 320 INGKPVDiRNPAQAIRAGIAMVPEDrkrhgivPILGVGknitlsvlksfCFKMRID--AAAELQIIGSAIQRLKVKTASP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1444 FeevlnseerfnsthnkflnlhteIAEGGLnlSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNK 1523
Cdd:TIGR02633 398 F-----------------------LPIGRL--SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE 452
|
250 260 270
....*....|....*....|....*....|
gi 6321752 1524 S-TILTIAHRLRSVIDY-DRIIVMDAGEVK 1551
Cdd:TIGR02633 453 GvAIIVVSSELAEVLGLsDRVLVIGEGKLK 482
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1338-1550 |
1.90e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.54 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1338 PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRR-SITIIPQDPILFAG-TIK 1415
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1416 SNVD---PYDEYDEKKIFKALSQVNlisSHefeevlnseerfnsthnkfLNLHteIAEGGLNLSqgERQLLFIARSLLRE 1492
Cdd:PRK15439 105 ENILfglPKRQASMQKMKQLLAALG---CQ-------------------LDLD--SSAGSLEVA--DRQIVEILRGLMRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1493 PKIILLDEATSSIDYDSDHLIQGIIRSEFNKST-ILTIAHRLRSVIDY-DRIIVMDAGEV 1550
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQGVgIVFISHKLPEIRQLaDRISVMRDGTI 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
808-885 |
2.33e-11 |
|
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: 63.42 E-value: 2.33e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEnCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGK 885
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE-LLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1340-1531 |
2.43e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 65.28 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1340 IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKI---DLVTLRRSITIIPQDP-ILFAGTIK 1415
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1416 SNV-------DPYDEYDEKKIFKALSQVNLisshefeevLNSEERFNsthnkflnlhteiaeggLNLSQGERQLLFIARS 1488
Cdd:PRK10908 98 DNVaipliiaGASGDDIRRRVSAALDKVGL---------LDKAKNFP-----------------IQLSGGEQQRVGIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6321752 1489 LLREPKIILLDEATSSIDydsDHLIQGIIR--SEFNK--STILTIAH 1531
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLD---DALSEGILRlfEEFNRvgVTVLMATH 195
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
338-640 |
3.05e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 66.38 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 338 LLIGMLWVLVNSIVNLLPTILMKRFLEIVDNPNRSSSCMNLAWLYIIGMFICRLTLAICNSQGQFVSDKICLRIrailig 417
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 418 eiyAKGLRRRLFTSPKTSSDS--DSISAnlGTIINLISIDSFKVSE-LANYLYVTVQAVIMIIVVVGLLF--NF-LGVsa 491
Cdd:cd18563 75 ---TADLRRDLYEHLQRLSLSffDKRQT--GSLMSRVTSDTDRLQDfLSDGLPDFLTNILMIIGIGVVLFslNWkLAL-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 492 fagisIILVMFPLNFLLANLLGK-----FQKQtlkctDQRISK----LNECLQNIRIVKYFAWERNIINEIKSIRQKELR 562
Cdd:cd18563 148 -----LVLIPVPLVVWGSYFFWKkirrlFHRQ-----WRRWSRlnsvLNDTLPGIRVVKAFGQEKREIKRFDEANQELLD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 563 SLLKKSLVWS-VTSFLWFVTPTLVTGVTFAICTFVQHEDLNAP--LAFTtlSLFTLLKTPLDQLSNMLSFINQSKVSLKR 639
Cdd:cd18563 218 ANIRAEKLWAtFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGtlVAFL--SYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
.
gi 6321752 640 I 640
Cdd:cd18563 296 I 296
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1032-1247 |
3.28e-11 |
|
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: 66.03 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1032 SKNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQ 1111
Cdd:cd18572 29 DGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1112 ELIPYLEVTIFCLIQCASIIFLITVITPRFLTVAVIVFVLYFFVGKWYLTASRELKRL--DSITKSPifQHFSETLVGVC 1189
Cdd:cd18572 109 PLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEiqDALAEAN--QVAEEALSNIR 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321752 1190 TIRAFGDE----RRFiLENMNKIDQNNRAFFYLSVTVKWFSFRVDMIGAFIVLASGSFILLN 1247
Cdd:cd18572 187 TVRSFATEereaRRY-ERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLS 247
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1340-1506 |
3.37e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1340 IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDI---SKIDLVTLRRSITIIPQDPIlfagtikS 1416
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY-------A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1417 NVDPYDEYDEkKIFKALSQVNLISSHE--------FEEV-LNSEERFNSTHnkflnlhteiaegglNLSQGERQLLFIAR 1487
Cdd:PRK10261 413 SLDPRQTVGD-SIMEPLRVHGLLPGKAaaarvawlLERVgLLPEHAWRYPH---------------EFSGGQRQRICIAR 476
|
170
....*....|....*....
gi 6321752 1488 SLLREPKIILLDEATSSID 1506
Cdd:PRK10261 477 ALALNPKVIIADEAVSALD 495
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
748-916 |
3.58e-11 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 66.67 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 748 FAYCSQSAWLLND-TVKNNIIF-----DNFYNEDRYNKVIDACGLKRDLEILPAgdlteigekgiTLSGGQKQRISLARA 821
Cdd:TIGR02142 77 IGYVFQEARLFPHlSVRGNLRYgmkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 822 VYSSAKHVLLDDCLSAVDSHTAVWIYencitgPLMKNRT------CILVTHNVSLTLRNAHFAIVLENGKVKNQGTITEL 895
Cdd:TIGR02142 146 LLSSPRLLLMDEPLAALDDPRKYEIL------PYLERLHaefgipILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
170 180
....*....|....*....|.
gi 6321752 896 QSKGLFkeKYVQLSSRDSINE 916
Cdd:TIGR02142 220 WASPDL--PWLAREDQGSLIE 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1323-1559 |
3.62e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.52 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRL--LEPITG-----------CIKID----- 1384
Cdd:TIGR03269 1 IEVKNLTKKFDGK--EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGriiyhvalcekCGYVErpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1385 GQDISK---------IDLVTLRRSIT--IIPQDPILFAGTiksnvdpYDEYDEKK----IFKALSQVNLISSHEFEEVLN 1449
Cdd:TIGR03269 79 GEPCPVcggtlepeeVDFWNLSDKLRrrIRKRIAIMLQRT-------FALYGDDTvldnVLEALEEIGYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1450 SEERFNSTHNKflnlhTEIAEgglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS---EFNKSTI 1526
Cdd:TIGR03269 152 LIEMVQLSHRI-----THIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavkASGISMV 223
|
250 260 270
....*....|....*....|....*....|....
gi 6321752 1527 LTiAHRLRSVIDY-DRIIVMDAGEVKEYDRPSEL 1559
Cdd:TIGR03269 224 LT-SHWPEVIEDLsDKAIWLENGEIKEEGTPDEV 256
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1323-1548 |
3.67e-11 |
|
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: 64.76 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLS------LRYAPNLPpVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDiSKIDLVT- 1395
Cdd:COG4778 5 LEVENLSktftlhLQGGKRLP-VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG-GWVDLAQa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1396 -------LRRSiTI---------IPQ--------DPILFAGtiksnVDPYDEYDEKKifKALSQVNLisshefeevlnSE 1451
Cdd:COG4778 83 spreilaLRRR-TIgyvsqflrvIPRvsaldvvaEPLLERG-----VDREEARARAR--ELLARLNL-----------PE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1452 ERFNSTHNKFlnlhteiaegglnlSQGERQLLFIARSLLREPKIILLDEATSSIDYDS-DHLIQGIIRSEFNKSTILTIA 1530
Cdd:COG4778 144 RLWDLPPATF--------------SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANrAVVVELIEEAKARGTAIIGIF 209
|
250 260
....*....|....*....|
gi 6321752 1531 HRlRSVIDY--DRIIVMDAG 1548
Cdd:COG4778 210 HD-EEVREAvaDRVVDVTPF 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
665-885 |
6.56e-11 |
|
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: 63.64 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 665 EFKNATLTWNendsDMNAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKHDLI------ 738
Cdd:cd03225 1 ELKNLSFSYP----DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkelrrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 739 -------PDcegltnsfaycSQsawLLNDTVKNNIIFdNFYNEDRYNKVIDacglKRDLEILPAGDLTEIGEKGI-TLSG 810
Cdd:cd03225 77 vglvfqnPD-----------DQ---FFGPTVEEEVAF-GLENLGLPEEEIE----ERVEEALELVGLEGLRDRSPfTLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 811 GQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK-----NRTCILVTHNVSLTLRNAHFAIVLENGK 885
Cdd:cd03225 138 GQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE------LLKklkaeGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1323-1562 |
7.18e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.77 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLP---PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDI---SK-IDLVT 1395
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKnKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1396 LRRSITIIPQDP--ILFAGTIKSNVdpydeydekkifkALSQVNL-ISSHEFE----EVLN----SEERFNSthNKFlnl 1464
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVLKDV-------------AFGPQNFgVSQEEAEalarEKLAlvgiSESLFEK--NPF--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1465 hteiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS--TILTIAHRLRSVIDY-DR 1541
Cdd:PRK13649 145 ---------ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFK-KLHQSgmTIVLVTHLMDDVANYaDF 214
|
250 260
....*....|....*....|.
gi 6321752 1542 IIVMDAGEVKEYDRPSELLKD 1562
Cdd:PRK13649 215 VYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
808-886 |
7.96e-11 |
|
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: 62.62 E-value: 7.96e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENcITGPLMKNRTCILVTHNVSlTLRNAHFAIVLENGKV 886
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA-IAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
689-841 |
1.21e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 689 NIKFQI--GKLNLILGSTGSGKSALLLGLLGELNLISGSII-----VPSLEPkhdlipdcEGLTNSFAYCSQSAWLLNDT 761
Cdd:PRK10247 25 NISFSLraGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLfegedISTLKP--------EIYRQQVSYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 762 VKNNIIFDNfynEDRyNKVIDACGLKRDLEI--LPagdlTEIGEKGIT-LSGGQKQRISLARAVYSSAKHVLLDDCLSAV 838
Cdd:PRK10247 97 VYDNLIFPW---QIR-NQQPDPAIFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
...
gi 6321752 839 DSH 841
Cdd:PRK10247 169 DES 171
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1044-1290 |
1.50e-10 |
|
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: 64.12 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1044 VYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFC 1123
Cdd:cd18557 41 ILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1124 LIQCASIIFLITVITPRfLTVAVIVFV-LYFFVGKWYLTASRELKR--LDSITKSPifQHFSETLVGVCTIRAFGDERRF 1200
Cdd:cd18557 121 ILQVIGGLIILFILSWK-LTLVLLLVIpLLLIASKIYGRYIRKLSKevQDALAKAG--QVAEESLSNIRTVRSFSAEEKE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1201 IL---ENMNKIDQNNRAF-----FYLSVTvkWFSFrvdMIGAFIVLASGSFILLNiANIDSG-LAGISLtYAILFTDGAL 1271
Cdd:cd18557 198 IRrysEALDRSYRLARKKalanaLFQGIT--SLLI---YLSLLLVLWYGGYLVLS-GQLTVGeLTSFIL-YTIMVASSVG 270
|
250
....*....|....*....
gi 6321752 1272 WLVRLYSTFEMNMNSVERL 1290
Cdd:cd18557 271 GLSSLLADIMKALGASERV 289
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1320-1560 |
1.53e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1320 DGEIEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDIS---------- 1389
Cdd:PRK10619 3 ENKLNVIDLHKRYGEH--EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1390 ---KIDLVTLRRSITIIPQDPILFAG-TIKSNVdpydeydekkiFKALSQVNLISSHEfeevlnSEERfnstHNKFLNLH 1465
Cdd:PRK10619 81 vadKNQLRLLRTRLTMVFQHFNLWSHmTVLENV-----------MEAPIQVLGLSKQE------ARER----AVKYLAKV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1466 --TEIAEGG--LNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDsdhLIQGIIR-----SEFNKsTILTIAHRL--- 1533
Cdd:PRK10619 140 giDERAQGKypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRimqqlAEEGK-TMVVVTHEMgfa 215
|
250 260
....*....|....*....|....*..
gi 6321752 1534 RSVIDYdrIIVMDAGEVKEYDRPSELL 1560
Cdd:PRK10619 216 RHVSSH--VIFLHQGKIEEEGAPEQLF 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1323-1550 |
1.88e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.43 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYapnlPPVI--RNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDiskidlVTLRRS- 1399
Cdd:COG3845 6 LELRGITKRF----GGVVanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP------VRIRSPr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ------ITIIPQDPILFAG-TIKSNV----DPYdeydeKKIFKALSQVNlissHEFEEVLnseERFNsthnkF-LNLHTE 1467
Cdd:COG3845 76 daialgIGMVHQHFMLVPNlTVAENIvlglEPT-----KGGRLDRKAAR----ARIRELS---ERYG-----LdVDPDAK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1468 IAEgglnLSQGERQLLFIARSLLREPKIILLDEATSSI-DYDSDHLIQgIIRsEFNKS--TILTIAHRLRSVIDY-DRII 1543
Cdd:COG3845 139 VED----LSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE-ILR-RLAAEgkSIIFITHKLREVMAIaDRVT 212
|
....*..
gi 6321752 1544 VMDAGEV 1550
Cdd:COG3845 213 VLRRGKV 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1326-1563 |
1.92e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.47 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1326 ENLSLRYAPNLppVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQ 1405
Cdd:PRK10253 11 EQLTLGYGKYT--VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1406 DPILFAGTIKSNVDPYDEYDEKKIFKALSQvnlisshEFEEVLNSEERFNSThnkflnlhTEIAEGGLN-LSQGERQLLF 1484
Cdd:PRK10253 89 NATTPGDITVQELVARGRYPHQPLFTRWRK-------EDEEAVTKAMQATGI--------THLADQSVDtLSGGQRQRAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1485 IARSLLREPKIILLDEATSSIDYdsDHLIQGI-IRSEFNKS---TILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPSEL 1559
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDI--SHQIDLLeLLSELNREkgyTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEI 231
|
....
gi 6321752 1560 LKDE 1563
Cdd:PRK10253 232 VTAE 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1343-1556 |
2.03e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.22 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1343 VSFKVDPQSKIGIVGRTGAGKSTiitaLFRLL----EPITGCIKIDGQDISKIDLVT---LRRSITIIPQDPIlfagtik 1415
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKST----LARLLtmieTPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNPY------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1416 SNVDPydeydEKKIFKALSQVNLISSHefeevLNSEERfnstHNKFLNLhteIAEGGLN----------LSQGERQLLFI 1485
Cdd:PRK11308 103 GSLNP-----RKKVGQILEEPLLINTS-----LSAAER----REKALAM---MAKVGLRpehydryphmFSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1486 ARSLLREPKIILLDEATSSIDYDsdhlIQGII-------RSEFNKSTILtIAHRLrSVIDY--DRIIVMDAGEVKE---- 1552
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVS----VQAQVlnlmmdlQQELGLSYVF-ISHDL-SVVEHiaDEVMVMYLGRCVEkgtk 239
|
....*..
gi 6321752 1553 ---YDRP 1556
Cdd:PRK11308 240 eqiFNNP 246
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1322-1559 |
2.07e-10 |
|
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: 62.74 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1322 EIEIENLSLRYaPNLPpVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLvtLRRSIT 1401
Cdd:cd03296 2 SIEVRNVSKRF-GDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV--QERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1402 IIPQDPILFAG-TIKSNV------------DPYDEYDEkKIFKALSQVNLisshefeEVLnsEERFNSthnkflnlhtei 1468
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVafglrvkprserPPEAEIRA-KVHELLKLVQL-------DWL--ADRYPA------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1469 aegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIR---SEFNKSTILtIAHRLRSVIDY-DRIIV 1544
Cdd:cd03296 136 -----QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRrlhDELHVTTVF-VTHDQEEALEVaDRVVV 209
|
250
....*....|....*
gi 6321752 1545 MDAGEVKEYDRPSEL 1559
Cdd:cd03296 210 MNKGRIEQVGTPDEV 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
679-898 |
2.90e-10 |
|
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: 62.35 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 679 DMNAFKLcgLNIKFQIGKLN--LILGSTGSGKSALLLGLLGELNLISGSIIvpsLEPKH--DLIPDCEGltnsFAYCSQS 754
Cdd:cd03299 9 DWKEFKL--KNVSLEVERGDyfVILGPTGSGKSVLLETIAGFIKPDSGKIL---LNGKDitNLPPEKRD----ISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 755 AWLL-NDTVKNNIIFdNFYNEDRYNKVIDacglKRDLEIlpAGDLtEIGE----KGITLSGGQKQRISLARAVYSSAKHV 829
Cdd:cd03299 80 YALFpHMTVYKNIAY-GLKKRKVDKKEIE----RKVLEI--AEML-GIDHllnrKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 830 LLDDCLSAVDSHT--------AVWIYENcitgplmkNRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITELQSK 898
Cdd:cd03299 152 LLDEPFSALDVRTkeklreelKKIRKEF--------GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1323-1562 |
3.84e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.03 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALfRLLEPIT-GCIKIDGQDI--SKIDLVTLRRS 1399
Cdd:PRK09493 2 IEFKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITsGDLIVDGLKVndPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQDPILFA----------GTIKsnVDPYDEYDEKKIFKAL-SQVNLisshefeevlnsEERFNSTHNKflnlhtei 1468
Cdd:PRK09493 79 AGMVFQQFYLFPhltalenvmfGPLR--VRGASKEEAEKQARELlAKVGL------------AERAHHYPSE-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1469 aegglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKS-TILTIAHRL---RSVIdyDRIIV 1544
Cdd:PRK09493 137 ------LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGmTMVIVTHEIgfaEKVA--SRLIF 208
|
250
....*....|....*...
gi 6321752 1545 MDAGEVKEYDRPSELLKD 1562
Cdd:PRK09493 209 IDKGRIAEDGDPQVLIKN 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1323-1558 |
4.63e-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: 61.68 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPV--IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKID---LVTLR 1397
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedaRARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1398 -RSITIIPQD---------------PILFAGtiksNVDPYDEYDEkkifkALSQVNLisshefeevlnsEERFNSTHNKf 1461
Cdd:COG4181 89 aRHVGFVFQSfqllptltalenvmlPLELAG----RRDARARARA-----LLERVGL------------GHRLDHYPAQ- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1462 lnlhteiaegglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNK---STILTIAH--RL--R 1534
Cdd:COG4181 147 -------------LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLF-ELNRergTTLVLVTHdpALaaR 212
|
250 260
....*....|....*....|....
gi 6321752 1535 SvidyDRIIVMDAGEVKEYDRPSE 1558
Cdd:COG4181 213 C----DRVLRLRAGRLVEDTAATA 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1325-1552 |
4.79e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.87 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1325 IENLSLRYAPNLPpvIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTL----RRSI 1400
Cdd:PRK11701 9 VRGLTKLYGPRKG--CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 T-----IIPQDPI----------------LFA------GTIKSnvdpydeydekkifkalsqvnlISSHEFEEVLNSEER 1453
Cdd:PRK11701 87 LrtewgFVHQHPRdglrmqvsaggnigerLMAvgarhyGDIRA----------------------TAGDWLERVEIDAAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1454 FNSTHNKFlnlhteiaegglnlSQGERQLLFIARSLLREPKIILLDEATSSID-------YDsdhLIQGIIRsEFNKSTI 1526
Cdd:PRK11701 145 IDDLPTTF--------------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqarlLD---LLRGLVR-ELGLAVV 206
|
250 260 270
....*....|....*....|....*....|.
gi 6321752 1527 LtIAH-----RLRSvidyDRIIVMDAGEVKE 1552
Cdd:PRK11701 207 I-VTHdlavaRLLA----HRLLVMKQGRVVE 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1325-1550 |
5.18e-10 |
|
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: 64.65 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1325 IENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDIsKIDLVTLRRSITIIP 1404
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1405 QDPILFAGTIKSnvdpydeydEKKIFKAlsqvNLISSHEFEEVLNSEERFNSThnkflNLHTEIAEGGLNLSQGERQLLF 1484
Cdd:TIGR01257 1010 QHNILFHHLTVA---------EHILFYA----QLKGRSWEEAQLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLS 1071
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 1485 IARSLLREPKIILLDEATSSID-YDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEV 1550
Cdd:TIGR01257 1072 VAIAFVGDAKVVVLDEPTSGVDpYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
687-896 |
7.05e-10 |
|
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: 60.98 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 687 GLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIV-----PSLEPKhDLIPdcegLTNSFAYCSQSAWLLND- 760
Cdd:cd03261 18 GVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgediSGLSEA-ELYR----LRRRMGMLFQSGALFDSl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 761 TVKNNIIFDNFYN--------EDRYNKVIDACGLKRDLEILPAgdlteigekgiTLSGGQKQRISLARAVYSSAKHVLLD 832
Cdd:cd03261 93 TVFENVAFPLREHtrlseeeiREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 833 DCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITELQ 896
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1327-1552 |
8.64e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.98 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1327 NLSLRYAPN--LPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVT---LR-RSI 1400
Cdd:PRK11629 10 NLCKRYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1401 TIIPQ------D---------PILFAGTIKSNVdpydeydEKKIFKALSQVNLisshefeevlnsEERfnSTHNKflnlh 1465
Cdd:PRK11629 90 GFIYQfhhllpDftalenvamPLLIGKKKPAEI-------NSRALEMLAAVGL------------EHR--ANHRP----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1466 teiAEgglnLSQGERQLLFIARSLLREPKIILLDEATSSID-YDSDHLIQgiIRSEFNK---STILTIAHRLRSVIDYDR 1541
Cdd:PRK11629 144 ---SE----LSGGERQRVAIARALVNNPRLVLADEPTGNLDaRNADSIFQ--LLGELNRlqgTAFLVVTHDLQLAKRMSR 214
|
250
....*....|.
gi 6321752 1542 IIVMDAGEVKE 1552
Cdd:PRK11629 215 QLEMRDGRLTA 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
749-913 |
9.62e-10 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 60.85 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 749 AYCSQSAWLLND-TVKNNIIF-------DNFYNEDRYNKVIDACGLKRDLEILPAgdlteigekgiTLSGGQKQRISLAR 820
Cdd:COG1131 76 GYVPQEPALYPDlTVRENLRFfarlyglPRKEARERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 821 AVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK-----NRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITEL 895
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWE------LLRelaaeGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
170
....*....|....*...
gi 6321752 896 QSKGLfKEKYVQLSSRDS 913
Cdd:COG1131 219 KARLL-EDVFLELTGEEA 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1323-1500 |
1.06e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.66 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPnlPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLV-TLRRSIT 1401
Cdd:PRK11614 6 LSFDKVSAHYGK--IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1402 IIPQDpilfagtiksnvdpydeydeKKIFKALS-QVNLISSHEFEEVLNSEERFNSTHNKFLNLHTEIAEGGLNLSQGER 1480
Cdd:PRK11614 84 IVPEG--------------------RRVFSRMTvEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQ 143
|
170 180
....*....|....*....|
gi 6321752 1481 QLLFIARSLLREPKIILLDE 1500
Cdd:PRK11614 144 QMLAIGRALMSQPRLLLLDE 163
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1327-1560 |
1.10e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.18 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1327 NLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQ--DISKIDLVTLRRSITIIP 1404
Cdd:PRK13638 6 DLWFRYQDE--PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1405 QDP--ILFAGTIKSNVdpydeydekkifkALSQVNL-ISSHEF-EEVLNSEERFNSTHNKflnlHTEIAegglNLSQGER 1480
Cdd:PRK13638 84 QDPeqQIFYTDIDSDI-------------AFSLRNLgVPEAEItRRVDEALTLVDAQHFR----HQPIQ----CLSHGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1481 QLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTI-AHRLRSVIDY-DRIIVMDAGEVKEYDRPSE 1558
Cdd:PRK13638 143 KRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEIsDAVYVLRQGQILTHGAPGE 222
|
..
gi 6321752 1559 LL 1560
Cdd:PRK13638 223 VF 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1323-1587 |
1.17e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.85 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITAL--FRLLEPITGCIKIDGQDIskIDLVTLRRS- 1399
Cdd:cd03217 1 LEIKDLHVSVGGK--EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDI--TDLPPEERAr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 --ITIIPQDPIlfagtiksnvdpydeydekkifkalsqvnlisshEFEEVLNSEerfnsthnkFLNlhtEIAEGglnLSQ 1477
Cdd:cd03217 77 lgIFLAFQYPP----------------------------------EIPGVKNAD---------FLR---YVNEG---FSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1478 GERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFN-KSTILTIAHRLRsVIDY---DRIIVMDAGEVKEy 1553
Cdd:cd03217 108 GEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVK- 185
|
250 260 270
....*....|....*....|....*....|....
gi 6321752 1554 drpsellkdergifysmcrdSGGLELLKQIAKQS 1587
Cdd:cd03217 186 --------------------SGDKELALEIEKKG 199
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1323-1506 |
1.25e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.37 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYApNLPpvIRnVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIdlVTLRRSITI 1402
Cdd:PRK10771 2 LKLTDITWLYH-HLP--MR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT--PPSRRPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAG-TIKSNV----DP---YDEYDEKKIFKALSQVNLisshefEEVLnseERFNSthnkflnlhteiaegglN 1474
Cdd:PRK10771 76 LFQENNLFSHlTVAQNIglglNPglkLNAAQREKLHAIARQMGI------EDLL---ARLPG-----------------Q 129
|
170 180 190
....*....|....*....|....*....|..
gi 6321752 1475 LSQGERQLLFIARSLLREPKIILLDEATSSID 1506
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1323-1561 |
1.35e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.48 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPP--------------------VIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIK 1382
Cdd:COG1134 5 IEVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1383 IDGQDISKIDL-------VTLRrsitiipqDPILFAGTIksnvdpY----DEYDEKkifkalsqvnlissheFEEVLN-S 1450
Cdd:COG1134 85 VNGRVSALLELgagfhpeLTGR--------ENIYLNGRL------LglsrKEIDEK----------------FDEIVEfA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1451 E-ERFnsthnkflnLHTEIAegglNLSQGER-QLLF-IARSLlrEPKIILLDEATSSIDYD----SDHLIQGIIRSEfnk 1523
Cdd:COG1134 135 ElGDF---------IDQPVK----TYSSGMRaRLAFaVATAV--DPDILLVDEVLAVGDAAfqkkCLARIRELRESG--- 196
|
250 260 270
....*....|....*....|....*....|....*....
gi 6321752 1524 STILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPSELLK 1561
Cdd:COG1134 197 RTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1343-1554 |
1.35e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 61.65 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1343 VSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLR--RS-ITIIPQDPI------LFAGT 1413
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavRSdIQMIFQDPLaslnprMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1414 IKSnvDPYDEY-------DEKKIFKA-LSQV----NLISS--HEFeevlnseerfnsthnkflnlhteiaegglnlSQGE 1479
Cdd:PRK15079 120 IIA--EPLRTYhpklsrqEVKDRVKAmMLKVgllpNLINRypHEF-------------------------------SGGQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1480 RQLLFIARSLLREPKIILLDEATS----SIDYDSDHLIQGIIRsEFNKSTILtIAHRLrSVIDY--DRIIVM---DAGEV 1550
Cdd:PRK15079 167 CQRIGIARALILEPKLIICDEPVSaldvSIQAQVVNLLQQLQR-EMGLSLIF-IAHDL-AVVKHisDRVLVMylgHAVEL 243
|
....
gi 6321752 1551 KEYD 1554
Cdd:PRK15079 244 GTYD 247
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
664-886 |
1.81e-09 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 59.34 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDSDMNafklcGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKH---DLIPD 740
Cdd:cd03292 1 IEFINVTKTYPNGTAALD-----GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 741 cegLTNSFAYCSQSAWLLND-TVKNNIIFDNFYNE-------DRYNKVIDACGLKRDLEILPAGdlteigekgitLSGGQ 812
Cdd:cd03292 76 ---LRRKIGVVFQDFRLLPDrNVYENVAFALEVTGvppreirKRVPAALELVGLSHKHRALPAE-----------LSGGE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 813 KQRISLARAVYSSAKHVLLDDCLSAVDSHTAvWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKV 886
Cdd:cd03292 142 QQRVAIARAIVNSPTILIADEPTGNLDPDTT-WEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1028-1239 |
1.90e-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: 60.86 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1028 MTDSSKNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIE 1107
Cdd:cd18544 30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1108 GVdQELIPYLEVTIFcliqcASIIFLITVIT------PRFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHF 1181
Cdd:cd18544 110 AL-NELFTSGLVTLI-----GDLLLLIGILIamfllnWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321752 1182 SETLVGVCTIRAFGDERRFilenMNKIDQNNRAFFYLSV-TVKWFS-FR--VDMIGAFIVLA 1239
Cdd:cd18544 184 QESISGMSVIQLFNREKRE----FEEFDEINQEYRKANLkSIKLFAlFRplVELLSSLALAL 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1318-1555 |
2.10e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.96 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1318 PKDGEI--EIENLSLRyapnlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDIS------ 1389
Cdd:COG1129 250 AAPGEVvlEVEGLSVG------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprd 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1390 ----KIDLVTL-RRSITIIPQDPILFAGTIKSnvdpydeydekkiFKALSQVNLISSH-EFEEVLNSEERFNSthnKFLN 1463
Cdd:COG1129 324 airaGIAYVPEdRKGEGLVLDLSIRENITLAS-------------LDRLSRGGLLDRRrERALAEEYIKRLRI---KTPS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1464 LHTEIAegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIR-------------SEFnkSTILTIA 1530
Cdd:COG1129 388 PEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRelaaegkavivisSEL--PELLGLS 461
|
250 260
....*....|....*....|....*.
gi 6321752 1531 hrlrsvidyDRIIVMDAGE-VKEYDR 1555
Cdd:COG1129 462 ---------DRILVMREGRiVGELDR 478
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
779-886 |
3.13e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 59.69 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 779 KVIDACGL-------KRDLEILPAGDLTE-IGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENC 850
Cdd:PRK11247 97 KVIDNVGLglkgqwrDAALQALAAVGLADrANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLI 176
|
90 100 110
....*....|....*....|....*....|....*.
gi 6321752 851 ITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKV 886
Cdd:PRK11247 177 ESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
664-898 |
4.25e-09 |
|
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: 58.73 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDsdmNAFKlcGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIV-----PSLEPK---- 734
Cdd:cd03256 1 IEVENLSKTYPNGK---KALK--DVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdiNKLKGKalrq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 735 -----------HDLIPDCEGLTN----SFAYcsQSAWllndtvknNIIFDNFYNEDRynkvidacglKRDLEILPAGDLT 799
Cdd:cd03256 76 lrrqigmifqqFNLIERLSVLENvlsgRLGR--RSTW--------RSLFGLFPKEEK----------QRALAALERVGLL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 800 EIGEKGI-TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIY----ENCITgplmKNRTCILVTHNVSLTLRN 874
Cdd:cd03256 136 DKAYQRAdQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMdllkRINRE----EGITVIVSLHQVDLAREY 211
|
250 260
....*....|....*....|....
gi 6321752 875 AHFAIVLENGKVKNQGTITELQSK 898
Cdd:cd03256 212 ADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
664-885 |
4.29e-09 |
|
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: 57.58 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDSdmnafkLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSlEPKHDLIPDCEG 743
Cdd:cd03229 1 LELKNVSKRYGQKTV------LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG-EDLTDLEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 744 LTNSFAYCSQSAWLL-NDTVKNNIIFdnfynedrynkvidacglkrdleilpagdlteigekgiTLSGGQKQRISLARAV 822
Cdd:cd03229 74 LRRRIGMVFQDFALFpHLTVLENIAL--------------------------------------GLSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 823 YSSAKHVLLDDCLSAVDSHTAVWIyencitGPLMK------NRTCILVTHNVSLTLRNAHFAIVLENGK 885
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREV------RALLKslqaqlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
664-886 |
4.38e-09 |
|
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: 58.73 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDsdmnAFKlcGLNIKFQIGKLNLILGSTGSGKSAL-----LLGLLGELNLISGSIIVpSLEPKHDLI 738
Cdd:cd03260 1 IELRDLNVYYGDKH----ALK--DISLDIPKGEITALIGPSGCGKSTLlrllnRLNDLIPGAPDEGEVLL-DGKDIYDLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 739 PDCEGLTNSFAYCSQSAWLLNDTVKNNIifdnfynedRYNKVIDACGLKRDLEILPAGDLTEIG--------EKGITLSG 810
Cdd:cd03260 74 VDVLELRRRVGMVFQKPNPFPGSIYDNV---------AYGLRLHGIKLKEELDERVEEALRKAAlwdevkdrLHALGLSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 811 GQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIyENCITGpLMKNRTCILVTHNVSLTLRNAHFAIVLENGKV 886
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKI-EELIAE-LKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
801-905 |
4.39e-09 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 58.95 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 801 IGEkgitLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK-----NRTCILVTHNVSLTLRNA 875
Cdd:COG1121 137 IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYE------LLRelrreGKTILVVTHDLGAVREYF 206
|
90 100 110
....*....|....*....|....*....|
gi 6321752 876 HFAIVLeNGKVKNQGTITELQSKGLFKEKY 905
Cdd:COG1121 207 DRVLLL-NRGLVAHGPPEEVLTPENLSRAY 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
808-895 |
5.42e-09 |
|
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: 58.36 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYE-----NCITGPlmknrTCILVTHNVSLTLRNAHFAIVLE 882
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILAllrdiNRELGL-----TIVLITHEMEVVKRICDRVAVME 215
|
90
....*....|...
gi 6321752 883 NGKVKNQGTITEL 895
Cdd:cd03258 216 KGEVVEEGTVEEV 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
807-905 |
6.76e-09 |
|
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: 58.52 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK------NRTCILVTHNVSLTLRNAHFAIV 880
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLE------LLRrlarerGRTVVMVLHDLNLAARYADRLVL 210
|
90 100
....*....|....*....|....*
gi 6321752 881 LENGKVKNQGTITELQSKGLFKEKY 905
Cdd:COG1120 211 LKDGRIVAQGPPEEVLTPELLEEVY 235
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
664-886 |
9.02e-09 |
|
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: 57.50 E-value: 9.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDSDMNAFKlcGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKHdliPDCEG 743
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALK--GVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISK---LSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 744 LT----NSFAYCSQSAWLLND-TVKNNIIF-------DNFYNEDRYNKVIDACGLKRDLEILPAgdlteigekgiTLSGG 811
Cdd:cd03255 76 LAafrrRHIGFVFQSFNLLPDlTALENVELplllagvPKKERRERAEELLERVGLGDRLNHYPS-----------ELSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 812 QKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK------NRTCILVTHNVSLTLRnAHFAIVLENGK 885
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVME------LLRelnkeaGTTIVVVTHDPELAEY-ADRIIELRDGK 217
|
.
gi 6321752 886 V 886
Cdd:cd03255 218 I 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1323-1554 |
1.04e-08 |
|
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: 57.54 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPP--------------------VIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIK 1382
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1383 IDGQDISKIDL-VTLRRSITIIpqDPILFAGTIKsNVDPyDEYDEKKIFkalsqvnlIssHEFEEVlnseerfnsthNKF 1461
Cdd:cd03220 81 VRGRVSSLLGLgGGFNPELTGR--ENIYLNGRLL-GLSR-KEIDEKIDE--------I--IEFSEL-----------GDF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1462 LNLHTeiaeggLNLSQGER-QLLF-IARSLlrEPKIILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIA-HRLRSVID 1538
Cdd:cd03220 136 IDLPV------KTYSSGMKaRLAFaIATAL--EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKR 207
|
250
....*....|....*..
gi 6321752 1539 Y-DRIIVMDAGEVKEYD 1554
Cdd:cd03220 208 LcDRALVLEKGKIRFDG 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1342-1558 |
1.08e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.12 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1342 NVSFKVD---PQSKI-GIVGRTGAGKSTIITALFRLLEPITGCIKIDGQ---DI-SKIDLVTLRRSITIIPQDPILFAG- 1412
Cdd:PRK11144 12 DLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARLFPHy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1413 TIKSNVdpydEYDEKKIFKAL--SQVNLISsheFEEVLNseeRFNSThnkflnlhteiaegglnLSQGERQLLFIARSLL 1490
Cdd:PRK11144 92 KVRGNL----RYGMAKSMVAQfdKIVALLG---IEPLLD---RYPGS-----------------LSGGEKQRVAIGRALL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1491 REPKIILLDEATSSIDYDSDH-LIQGIIR-SEFNKSTILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPSE 1558
Cdd:PRK11144 145 TAPELLLMDEPLASLDLPRKReLLPYLERlAREINIPILYVSHSLDEILRLaDRVVVLEQGKVKAFGPLEE 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1340-1550 |
1.61e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1340 IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKidlvTLRRS-ITIIPQD-------PILFA 1411
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNlVAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1412 GTIKSN-------VDPYDEYDEKKIFKALSQVNLIsshEFEevlnseerfnsthnkflnlHTEIAEgglnLSQGERQLLF 1484
Cdd:PRK15056 99 DVVMMGryghmgwLRRAKKRDRQIVTAALARVDMV---EFR-------------------HRQIGE----LSGGQKKRVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 1485 IARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKS-TILTIAHRLRSVIDYDRIIVMDAGEV 1550
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGkTMLVSTHNLGSVTEFCDYTVMVKGTV 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1353-1553 |
1.64e-08 |
|
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: 57.03 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1353 IGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDIS-KIDLVTLRRSITIipqDPILFAGTIKSNVDPYDEYDekkIFK 1431
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPQYIKADYEGTV---RDLLSSITKDFYTHPYFKTE---IAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1432 ALsqvnlisshEFEEVLNSEERfnsthnkflnlhteiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDH 1511
Cdd:cd03237 102 PL---------QIEQILDREVP--------------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6321752 1512 LIQGIIR--SEFNKSTILTIAHRLrSVIDY--DRIIVMDaGEVKEY 1553
Cdd:cd03237 153 MASKVIRrfAENNEKTAFVVEHDI-IMIDYlaDRLIVFE-GEPSVN 196
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1323-1553 |
1.82e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTiitalfrLLEPITGCIKID-GQDISKIDLVTLRrsit 1401
Cdd:PRK11147 4 ISIHGAWLSFSDA--PLLDNAELHIEDNERVCLVGRNGAGKST-------LMKILNGEVLLDdGRIIYEQDLIVAR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1402 iIPQDPIL-FAGTIksnvdpYD-------EYDEK-KIFKALSQvnLISSHEFEEVLNSEERFNST--HNKFLNLHTEIAE 1470
Cdd:PRK11147 71 -LQQDPPRnVEGTV------YDfvaegieEQAEYlKRYHDISH--LVETDPSEKNLNELAKLQEQldHHNLWQLENRINE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1471 G----GLN-------LSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSeFNKStILTIAHRlRSVID- 1538
Cdd:PRK11147 142 VlaqlGLDpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT-FQGS-IIFISHD-RSFIRn 218
|
250
....*....|....*.
gi 6321752 1539 -YDRIIVMDAGEVKEY 1553
Cdd:PRK11147 219 mATRIVDLDRGKLVSY 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1340-1554 |
1.92e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.79 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1340 IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKiDLVTLRRSITII------------PQDP 1407
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVfgqrsqlwwdlpAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1408 ILFAGTIksnvdpydeYD-EKKIFKAlsqvNLissHEFEEVLNSEErfnsthnkFLNLHTEiaegglNLSQGERQLLFIA 1486
Cdd:COG4586 117 FRLLKAI---------YRiPDAEYKK----RL---DELVELLDLGE--------LLDTPVR------QLSLGQRMRCELA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321752 1487 RSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS---TILTIAHRLRSVIDY-DRIIVMDAGEVKeYD 1554
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLDVVSKEAIREFLK-EYNRErgtTILLTSHDMDDIEALcDRVIVIDHGRII-YD 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1321-1592 |
2.09e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.33 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1321 GEIEIENLSLRYAPNLP---PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLL-----EPITGCIKIDGqDISKID 1392
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgQTIVGDYAIPA-NLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1393 LVT-LRRSITIIPQDP--ILFAGTIKSNVdpydeydekkifkALSQVNLISshefeevlNSEERFNSTHN--KFLNLHTE 1467
Cdd:PRK13645 84 EVKrLRKEIGLVFQFPeyQLFQETIEKDI-------------AFGPVNLGE--------NKQEAYKKVPEllKLVQLPED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1468 IAE-GGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDH-LIQGIIRSEFN-KSTILTIAHRLRSVIDY-DRII 1543
Cdd:PRK13645 143 YVKrSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdFINLFERLNKEyKKRIIMVTHNMDQVLRIaDEVI 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6321752 1544 VMDAGEVKEYDRPSELLKDErgifysmcrdsgglELLKQIAKQSSKMMK 1592
Cdd:PRK13645 223 VMHEGKVISIGSPFEIFSNQ--------------ELLTKIEIDPPKLYQ 257
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
808-891 |
2.68e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 57.85 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAV----WiyencitgpLMK-----NRTCILVTHNVSLTLRNAHFA 878
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKelrrW---------LRRlhdelGGTTVFVTHDQEEALELADRV 204
|
90
....*....|...
gi 6321752 879 IVLENGKVKNQGT 891
Cdd:COG1118 205 VVMNQGRIEQVGT 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
687-908 |
2.94e-08 |
|
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: 56.40 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 687 GLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKHD---------LIPDCEGLTNSFaycsqsawl 757
Cdd:COG4555 19 DVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEprearrqigVLPDERGLYDRL--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 758 lndTVKNNI-IFDNFY--NEDRYNKVIDacglkrdlEILPAGDLTEIGEKGI-TLSGGQKQRISLARAVYSSAKHVLLDD 833
Cdd:COG4555 90 ---TVRENIrYFAELYglFDEELKKRIE--------ELIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 834 CLSAVDSHTAVWIYENCITgpLMKNRTCILV-THNVSLTLRNAHFAIVLENGKVKNQGTITELQSKGL---FKEKYVQL 908
Cdd:COG4555 159 PTNGLDVMARRLLREILRA--LKKEGKTVLFsSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGeenLEDAFVAL 235
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1078-1559 |
3.10e-08 |
|
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: 58.27 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1078 LLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQ------ELIPYLEVTIFCLIQCASI---IFLITVItprFLTVAVIV 1148
Cdd:COG4615 87 LSRRILAAPLERLERIGAARLLAALTEDVRTISQafvrlpELLQSVALVLGCLAYLAWLsppLFLLTLV---LLGLGVAG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1149 FVLYFFVGKWYLTASRELK-RLdsitkspiFQHFSETLVGVCTIR-------AFGDERrfILENMNKI-DQNNRAFFYLS 1219
Cdd:COG4615 164 YRLLVRRARRHLRRAREAEdRL--------FKHFRALLEGFKELKlnrrrrrAFFDED--LQPTAERYrDLRIRADTIFA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1220 VTVKWFSFrvdMIgaFIVLASGSFILLNIANIDSG-LAGISLTyaILFTDGALW-LVR---LYSTFEMNMNSVERLKEys 1294
Cdd:COG4615 234 LANNWGNL---LF--FALIGLILFLLPALGWADPAvLSGFVLV--LLFLRGPLSqLVGalpTLSRANVALRKIEELEL-- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1295 SIEQEnylghdEGRILLLNEPSWPKD-GEIEIENLSLRYAPNLPP---VIRNVSFKVDPQSKIGIVGRTGAGKST---II 1367
Cdd:COG4615 305 ALAAA------EPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTlakLL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1368 TALFRllePITGCIKIDGQDISKIDLVTLRRSITIIPQDPILFagtiKSNVDPYDEYDEKKIFKALSQVNLisshefeev 1447
Cdd:COG4615 379 TGLYR---PESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLERLEL--------- 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1448 lnseerfnstHNKflnlhTEIAEGGL---NLSQGERQLLFIARSLLREPKIILLDEATSsidyDSD---------HLI-- 1513
Cdd:COG4615 443 ----------DHK-----VSVEDGRFsttDLSQGQRKRLALLVALLEDRPILVFDEWAA----DQDpefrrvfytELLpe 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 1514 ---QGIirsefnksTILTIAHrlrsviD--Y----DRIIVMDAGEVKEYDRPSEL 1559
Cdd:COG4615 504 lkaRGK--------TVIAISH------DdrYfdlaDRVLKMDYGKLVELTGPAAL 544
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
664-895 |
3.69e-08 |
|
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: 56.15 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENdsdmnAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSlEPKHDLipDCEG 743
Cdd:cd03295 1 IEFENVTKRYGGG-----KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG-EDIREQ--DPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 744 LTNSFAYCSQSAWLL-NDTVKNNIIFD---NFYNEDRYNKvidacglkRDLEILPAGDLTEIGEKG---ITLSGGQKQRI 816
Cdd:cd03295 73 LRRKIGYVIQQIGLFpHMTVEENIALVpklLKWPKEKIRE--------RADELLALVGLDPAEFADrypHELSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 817 SLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITEL 895
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1327-1531 |
4.00e-08 |
|
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: 58.02 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1327 NLSLRYAPNlPPVIRNVSFKVDPQSKIGIVGRTGAGKSTiitalfrLLEPITGcikIDgQDISKIDLVTLRRSITIIPQD 1406
Cdd:TIGR03719 9 RVSKVVPPK-KEILKDISLSFFPGAKIGVLGLNGAGKST-------LLRIMAG---VD-KDFNGEARPQPGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1407 PILFAG-TIKSNV--------DPYDEYDEkkIFKALSQVNLISSHEFEEVLNSEERFNSTHNKFLNLHTEIAEGGL---- 1473
Cdd:TIGR03719 77 PQLDPTkTVRENVeegvaeikDALDRFNE--ISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALrcpp 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 1474 ------NLSQGERQLLFIARSLLREPKIILLDEATSSIDYDS-----DHLIqgiirsEFnKSTILTIAH 1531
Cdd:TIGR03719 155 wdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawleRHLQ------EY-PGTVVAVTH 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
685-843 |
4.05e-08 |
|
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: 55.74 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 685 LCGLNIKFQIGKLNLILGSTGSGKSA---LLLGLLGELNLISGSIIVPSLEPKHDLIPDCegltnsFAYCSQS-AWLLND 760
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPRKPDQFQKC------VAYVRQDdILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 761 TVKNNIIFDNFY-----NEDRYNKVIDACGLKRDLEILPAGdlteiGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCL 835
Cdd:cd03234 97 TVRETLTYTAILrlprkSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
....*...
gi 6321752 836 SAVDSHTA 843
Cdd:cd03234 172 SGLDSFTA 179
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
687-895 |
4.25e-08 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 55.59 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 687 GLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPslepKHDLIPDCEGLTNSFAYCSQSawllndtvknNI 766
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN----GYSIRTDRKAARQSLGYCPQF----------DA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 767 IFDNF--------------YNEDRYNKVIDAcgLKRDLEILPAGDlTEIGekgiTLSGGQKQRISLARAVYSSAKHVLLD 832
Cdd:cd03263 86 LFDELtvrehlrfyarlkgLPKSEIKEEVEL--LLRVLGLTDKAN-KRAR----TLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 833 DCLSAVDSHT--AVWiyeNCITGpLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITEL 895
Cdd:cd03263 159 EPTSGLDPASrrAIW---DLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1322-1564 |
4.27e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.63 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1322 EIEIENLSLRYAPNLP---PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCI-----------KIDGQD 1387
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1388 ISKIDLVT-------------LRRSITIIPQ--DPILFAGTIKSNVdpydeydekkIFKALSQVnlISSHEFEEVLnsee 1452
Cdd:PRK13651 82 KVLEKLVIqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDI----------IFGPVSMG--VSKEEAKKRA---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1453 rfnSTHNKFLNLHTEIAEGG-LNLSQGERQLLFIARSLLREPKIILLDEATSSIDydsdhlIQGI-----IRSEFNKS-- 1524
Cdd:PRK13651 146 ---AKYIELVGLDESYLQRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD------PQGVkeileIFDNLNKQgk 216
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 6321752 1525 TILTIAHRLRSVIDY-DRIIVMDAGEVKEYDRPSELLKDER 1564
Cdd:PRK13651 217 TIILVTHDLDNVLEWtKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
689-897 |
4.99e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.17 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 689 NIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKHDL--IPDCEGLTNSFAYCSQ--SAWLLNDTVKN 764
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLkkIKEVKRLRKEIGLVFQfpEYQLFQETIEK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 765 NIIFDNFY----NEDRYNKV---IDACGLKRDLeilpagdlteIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSA 837
Cdd:PRK13645 111 DIAFGPVNlgenKQEAYKKVpelLKLVQLPEDY----------VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 838 VD---SHTAVWIYENcitgpLMKN--RTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITELQS 897
Cdd:PRK13645 181 LDpkgEEDFINLFER-----LNKEykKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1338-1530 |
5.42e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.88 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1338 PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDiskIDLVTLRRSITII-PQDPILFAGTIKS 1416
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLgHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1417 NVDpydeydekkiFKAlsqvnlisshefeEVLNSEERFNSTHNKFLNLH--TEIAEGglNLSQGERQLLFIARSLLREPK 1494
Cdd:PRK13539 93 NLE----------FWA-------------AFLGGEELDIAAALEAVGLAplAHLPFG--YLSAGQKRRVALARLLVSNRP 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 6321752 1495 IILLDEATSSIDYDSDHLIQGIIRSEFNKSTILTIA 1530
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1353-1549 |
6.03e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1353 IGIVGRTGAGKSTIITALFRLLEPITGCIKIDgQDIS-KidlvtlrrsitiiPQdpilfagTIKSNVD-PYDEYdekkif 1430
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISyK-------------PQ-------YIKPDYDgTVEDL------ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1431 kaLSQV--NLISSHEFEEVLNSeerfnsthnkfLNLHtEIAEGGLN-LSQGERQLLFIARSLLREPKIILLDEATSSIDY 1507
Cdd:PRK13409 421 --LRSItdDLGSSYYKSEIIKP-----------LQLE-RLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6321752 1508 DSDHLIQGIIR--SEFNKSTILTIAHRLrSVIDY--DRIIVMDaGE 1549
Cdd:PRK13409 487 EQRLAVAKAIRriAEEREATALVVDHDI-YMIDYisDRLMVFE-GE 530
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
807-895 |
7.53e-08 |
|
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: 55.03 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK-----NRTCILVTHNVSLTLRNAHFAIVL 881
Cdd:COG1122 134 ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLE------LLKrlnkeGKTVIIVTHDLDLVAELADRVIVL 207
|
90
....*....|....
gi 6321752 882 ENGKVKNQGTITEL 895
Cdd:COG1122 208 DDGRIVADGTPREV 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1340-1561 |
8.85e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.98 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1340 IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEP---ITGCIKIDGQdisKIDLVTLRRSITIIPQDPiLFAGTIKS 1416
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM---PIDAKEMRAISAYVQQDD-LFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1417 nvdpydeyDEKKIFKA-LSQVNLISSHE----FEEVLNSeerfnsthnkfLNL----HTEIAEGGL--NLSQGERQLLFI 1485
Cdd:TIGR00955 117 --------REHLMFQAhLRMPRRVTKKEkrerVDEVLQA-----------LGLrkcaNTRIGVPGRvkGLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 1486 ARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNK-STILTIAHRLRSVI--DYDRIIVMDAGEVKEYDRPSELLK 1561
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQPSSELfeLFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1323-1562 |
9.31e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.14 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLppVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDgqDISkID---------- 1392
Cdd:PRK11264 4 IEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DIT-IDtarslsqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1393 -LVTLRRSITIIPQDPILFAG-TIKSNV---------DPYDEYdEKKIFKALSQVNLiSSHEfeevlNSEERfnsthnkf 1461
Cdd:PRK11264 79 lIRQLRQHVGFVFQNFNLFPHrTVLENIiegpvivkgEPKEEA-TARARELLAKVGL-AGKE-----TSYPR-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1462 lnlhteiaegglNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS-EFNKSTILTIAHRLRSVIDY- 1539
Cdd:PRK11264 144 ------------RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDVa 211
|
250 260
....*....|....*....|...
gi 6321752 1540 DRIIVMDAGEVKEYDRPSELLKD 1562
Cdd:PRK11264 212 DRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1315-1564 |
1.11e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1315 PSWPKdgeIEIENLSLRYAPNlppvirnvSFKVDPQS-------KIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQD 1387
Cdd:PRK10522 318 PDWQT---LELRNVTFAYQDN--------GFSVGPINltikrgeLLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1388 ISKIDLVTLRRSITIIPQDPILFAGTIKsnvDPYDEYDEKKIFKALSQVNLISSHEFEEvlnseerfnsthNKFLNlhte 1467
Cdd:PRK10522 387 VTAEQPEDYRKLFSAVFTDFHLFDQLLG---PEGKPANPALVEKWLERLKMAHKLELED------------GRISN---- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1468 iaeggLNLSQGERQLLFIARSLLREPKIILLDEATSsidyDSD-HLiqgiiRSEFNK----------STILTIAHRLRSV 1536
Cdd:PRK10522 448 -----LKLSKGQKKRLALLLALAEERDILLLDEWAA----DQDpHF-----RREFYQvllpllqemgKTIFAISHDDHYF 513
|
250 260
....*....|....*....|....*...
gi 6321752 1537 IDYDRIIVMDAGEVkeydrpSELLKDER 1564
Cdd:PRK10522 514 IHADRLLEMRNGQL------SELTGEER 535
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
774-895 |
1.24e-07 |
|
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: 56.06 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 774 EDRYNKVIDACGLKRD-LEILPAgdlteigekgiTLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncit 852
Cdd:COG1123 381 RERVAELLERVGLPPDlADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILN---- 445
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 6321752 853 gpLMK------NRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITEL 895
Cdd:COG1123 446 --LLRdlqrelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1323-1537 |
1.25e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQdiskidlvtLRrsITI 1402
Cdd:PRK09544 5 VSLENVSVSFGQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQ----DPIL------FAgTIKSNVDPYDeydekkIFKALSQVNliSSHEFEEVLNseerfnsthnkflnlhteiaegg 1472
Cdd:PRK09544 72 VPQklylDTTLpltvnrFL-RLRPGTKKED------ILPALKRVQ--AGHLIDAPMQ----------------------- 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321752 1473 lNLSQGERQLLFIARSLLREPKIILLDEATSSID-------YDsdhLIQGiIRSEFNkSTILTIAHRLRSVI 1537
Cdd:PRK09544 120 -KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvngqvalYD---LIDQ-LRRELD-CAVLMVSHDLHLVM 185
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1323-1567 |
1.38e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 55.72 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISkiDLVTLRRSITI 1402
Cdd:PRK09452 15 VELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAG-TIKSNVD--------PYDEYdEKKIFKALSQVNLisshefEEVLNSEERfnsthnkflnlhteiaeggl 1473
Cdd:PRK09452 91 VFQSYALFPHmTVFENVAfglrmqktPAAEI-TPRVMEALRMVQL------EEFAQRKPH-------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1474 NLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQ----------GIirsefnksTILTIAH-RLRSVIDYDRI 1542
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQnelkalqrklGI--------TFVFVTHdQEEALTMSDRI 215
|
250 260
....*....|....*....|....*
gi 6321752 1543 IVMDAGEVKEYDRPSELLKDERGIF 1567
Cdd:PRK09452 216 VVMRDGRIEQDGTPREIYEEPKNLF 240
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
808-886 |
1.50e-07 |
|
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: 54.05 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK------NRTCILVTHNVSLTLRNAHFAIVL 881
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILD------LLKklqeelGLTLLFITHDLGVVAKIADRVAVM 219
|
....*
gi 6321752 882 ENGKV 886
Cdd:cd03257 220 YAGKI 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
658-868 |
1.60e-07 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 54.33 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 658 SPDKNKIEFKNATLTWNENDSDMNAFKlcglNIKFQI--GKLNLILGSTGSGKS-----------ALllgllgelnliSG 724
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVTALD----DVSLTVaaGEFVALVGPSGCGKStllrliaglekPT-----------SG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 725 SIIVPSlEPKHDLIPDCegltnsfAYCSQSA----WLlndTVKNNIIF-------DNFYNEDRYNKVIDACGLKRDLEIL 793
Cdd:COG1116 67 EVLVDG-KPVTGPGPDR-------GVVFQEPallpWL---TVLDNVALglelrgvPKAERRERARELLELVGLAGFEDAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 794 PAgdlteigekgiTLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTA---------VWiyencitgpLMKNRTCILV 864
Cdd:COG1116 136 PH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRerlqdellrLW---------QETGKTVLFV 195
|
....
gi 6321752 865 THNV 868
Cdd:COG1116 196 THDV 199
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
807-897 |
1.62e-07 |
|
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: 55.49 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDS-------------HTAVWIyencitgPLmknrtcILVTHNVSLTLR 873
Cdd:COG4148 133 TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkaeilpylerlRDELDI-------PI------LYVSHSLDEVAR 199
|
90 100
....*....|....*....|....
gi 6321752 874 NAHFAIVLENGKVKNQGTITELQS 897
Cdd:COG4148 200 LADHVVLLEQGRVVASGPLAEVLS 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1325-1552 |
1.91e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1325 IENLSLRYAPNLPPV--IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISK-----IDLVTLR 1397
Cdd:PRK10261 15 VENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrsrqvIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1398 RS---------ITIIPQDPIlfagtikSNVDPydeydekkIFKALSQVnlISSHEFEEVLNSEERFNSThNKFLNL---- 1464
Cdd:PRK10261 95 AAqmrhvrgadMAMIFQEPM-------TSLNP--------VFTVGEQI--AESIRLHQGASREEAMVEA-KRMLDQvrip 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1465 --HTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIR---SEFNKSTILtIAHRLRSVIDY 1539
Cdd:PRK10261 157 eaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqKEMSMGVIF-ITHDMGVVAEI 235
|
250
....*....|....
gi 6321752 1540 -DRIIVMDAGEVKE 1552
Cdd:PRK10261 236 aDRVLVMYQGEAVE 249
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
685-895 |
1.98e-07 |
|
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: 53.62 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 685 LCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIvpsLEPKHDLIPDCEGLTnSFAYCSQSAWLlndTVKN 764
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVI---LEGKQITEPGPDRMV-VFQNYSLLPWL---TVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 765 NIifdnfynedrynkvidACGLKRDLEILPAGD-------------LTEIGEKGIT-LSGGQKQRISLARAVYSSAKHVL 830
Cdd:TIGR01184 74 NI----------------ALAVDRVLPDLSKSErraiveehialvgLTEAADKRPGqLSGGMKQRVAIARALSIRPKVLL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 831 LDDCLSAVDSHTAVWIYENcitgpLMK-----NRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITEL 895
Cdd:TIGR01184 138 LDEPFGALDALTRGNLQEE-----LMQiweehRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
808-897 |
2.03e-07 |
|
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: 54.04 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK------NRTCILVTHNVSLTlrnAHFA--- 878
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILN------LLKdlreerGLTYLFVSHDLAVV---AHLCdrv 209
|
90
....*....|....*....
gi 6321752 879 IVLENGKVKNQGTITELQS 897
Cdd:COG1124 210 AVMQNGRIVEELTVADLLA 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
807-886 |
2.26e-07 |
|
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: 53.29 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMKN------RTCILVTHNVSLTLRNAHFAIV 880
Cdd:cd03259 130 ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELRE------ELKElqrelgITTIYVTHDQEEALALADRIAV 203
|
....*.
gi 6321752 881 LENGKV 886
Cdd:cd03259 204 MNEGRI 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
788-897 |
2.63e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.92 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 788 RDLEILPAGDLT-EIGEK-GITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK------NR 859
Cdd:PRK10419 130 RASEMLRAVDLDdSVLDKrPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR------LLKklqqqfGT 203
|
90 100 110
....*....|....*....|....*....|....*...
gi 6321752 860 TCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITELQS 897
Cdd:PRK10419 204 ACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
808-886 |
2.77e-07 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 53.12 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK------NRTCILVTHNVSLtlrnAHFA--- 878
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLE------LLRelnrelGTTIVMVTHDPEL----AARAdrv 214
|
....*...
gi 6321752 879 IVLENGKV 886
Cdd:COG1136 215 IRLRDGRI 222
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
685-897 |
2.80e-07 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 53.66 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 685 LCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSII-----VPSLEPKHD---------LIPDCEGLTNSFay 750
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdLYQLDRKQRrafrrdvqlVFQDSPSAVNPR-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 751 cSQSAWLLNDTVKNNIIFDNFYNEDRYNKVIDACGLK-RDLEILPAgdlteigekgiTLSGGQKQRISLARAVYSSAKHV 829
Cdd:TIGR02769 105 -MTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPR-----------QLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321752 830 LLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITELQS 897
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1313-1551 |
2.87e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1313 NEPSWPKDGEIEIENLSLrYAPNLP--PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLE-PITGCIKIDGQdis 1389
Cdd:PRK13549 250 REPHTIGEVILEVRNLTA-WDPVNPhiKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGK--- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1390 KIDLVT----LRRSITIIPQD-------PILFAGtiksnvdpydeydeKKI-FKALSQVNLISshefeeVLNSEERFNST 1457
Cdd:PRK13549 326 PVKIRNpqqaIAQGIAMVPEDrkrdgivPVMGVG--------------KNItLAALDRFTGGS------RIDDAAELKTI 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1458 HNKFLNLHTEIAEGGL---NLSQGERQLLFIARSLLREPKIILLDEATSSID----YDSDHLI-----QGI----IRSEF 1521
Cdd:PRK13549 386 LESIQRLKVKTASPELaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakYEIYKLInqlvqQGVaiivISSEL 465
|
250 260 270
....*....|....*....|....*....|
gi 6321752 1522 NKstILTIAhrlrsvidyDRIIVMDAGEVK 1551
Cdd:PRK13549 466 PE--VLGLS---------DRVLVMHEGKLK 484
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1339-1566 |
3.19e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.12 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1339 VIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKID---LVTLRRS-ITIIPQDPILFAG-T 1413
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLRREhFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1414 IKSNVDPYDEYD--EKKIFKALSQVNLISshefeevLNSEERFNSTHNKflnlhteiaegglnLSQGERQLLFIARSLLR 1491
Cdd:PRK10535 103 AAQNVEVPAVYAglERKQRLLRAQELLQR-------LGLEDRVEYQPSQ--------------LSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 1492 EPKIILLDEATSSIDYDSDHLIQGIIRSEFNKS-TILTIAHRLRSVIDYDRIIVMDAGEVKEyDRPSELLKDERGI 1566
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGhTVIIVTHDPQVAAQAERVIEIRDGEIVR-NPPAQEKVNVAGG 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
808-933 |
3.46e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 54.04 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKhVLL-DDCLSAVDSHTAVWIYEncitgpLMK--NR----TCILVTHNVSLTLRNAHFAIV 880
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPK-VLLcDEATSALDPATTRSILE------LLKdiNRelglTIVLITHEMDVVKRICDRVAV 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 881 LENGKVKNQGTITE--LQSKGLFKEKYVQLSSRDSINEKNANRLKAPRKNDSQKI 933
Cdd:PRK11153 214 IDAGRLVEQGTVSEvfSHPKHPLTREFIQSTLHLDLPEDYLARLQAEPTTGSGPL 268
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
804-905 |
3.63e-07 |
|
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: 52.93 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 804 KGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncITGPLMKNRTCILVT-HNVSLTLRNAHFAIVLE 882
Cdd:cd03218 130 KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQK--IIKILKDRGIGVLITdHNVRETLSITDRAYIIY 207
|
90 100
....*....|....*....|...
gi 6321752 883 NGKVKNQGTITELQSKGLFKEKY 905
Cdd:cd03218 208 EGKVLAEGTPEEIAANELVRKVY 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
689-903 |
3.78e-07 |
|
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: 53.32 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 689 NIKFQI--GKLNLILGSTGSGKSALLLGLLGELNlISGSIIVPSLEpkHDLIPdCEGLTNSFAYCSQSAWLLNDTVKNNI 766
Cdd:cd03289 22 NISFSIspGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVS--WNSVP-LQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 767 IFDNFYNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWI 846
Cdd:cd03289 98 DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 847 -------YENCitgplmknrTCILVTHNVSLTLRNAHFaIVLENGKVKNQGTITELQS-KGLFKE 903
Cdd:cd03289 178 rktlkqaFADC---------TVILSEHRIEAMLECQRF-LVIEENKVRQYDSIQKLLNeKSHFKQ 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1340-1563 |
3.86e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1340 IRNVSFKVD------------PQSKI-GIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRSITIIPQD 1406
Cdd:PRK10575 14 LRNVSFRVPgrtllhplsltfPAGKVtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1407 -PILFAGTIKSNVD----P-------YDEYDEKKIFKALSQVNLisshefeevlnseerfNSTHNKFLNlhteiaegglN 1474
Cdd:PRK10575 94 lPAAEGMTVRELVAigryPwhgalgrFGAADREKVEEAISLVGL----------------KPLAHRLVD----------S 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1475 LSQGERQLLFIARSLLREPKIILLDEATSSID----YDSDHLIQGIirSEFNKSTILTIAHRLRSVIDY-DRIIVMDAGE 1549
Cdd:PRK10575 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRL--SQERGLTVIAVLHDINMAARYcDYLVALRGGE 225
|
250
....*....|....
gi 6321752 1550 VKEYDRPSELLKDE 1563
Cdd:PRK10575 226 MIAQGTPAELMRGE 239
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
656-870 |
4.15e-07 |
|
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: 54.75 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 656 TISPDKNKIEFKNATLTWNENDSDMNAfklcgLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSlepkh 735
Cdd:TIGR00954 444 IVEYQDNGIKFENIPLVTPNGDVLIES-----LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA----- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 736 dlipdceglTNSFAYCSQSAWLLNDTVKNNIIFDNfYNEDRYNKVIDACGLKRDLEILpagDLTEIGEKGI--------- 806
Cdd:TIGR00954 514 ---------KGKLFYVPQRPYMTLGTLRDQIIYPD-SSEDMKRRGLSDKDLEQILDNV---QLTHILEREGgwsavqdwm 580
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 807 -TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITgplmKNRTCILVTHNVSL 870
Cdd:TIGR00954 581 dVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE----FGITLFSVSHRKSL 641
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
689-895 |
4.18e-07 |
|
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: 54.52 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 689 NIKFQI--GKLNLILGSTGSGKSALLLGL---LGELNLISGSIivpSLEPKHDLIPDCEGLTNSFAYCSQSAW--LLNDT 761
Cdd:COG1123 24 GVSLTIapGETVALVGESGSGKSTLALALmglLPHGGRISGEV---LLDGRDLLELSEALRGRRIGMVFQDPMtqLNPVT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 762 VKNNIIFdnfynedrynkVIDACGLKRD------LEILPAGDLTEIGEKGI-TLSGGQKQRISLARAVYSSAKHVLLDDC 834
Cdd:COG1123 101 VGDQIAE-----------ALENLGLSRAeararvLELLEAVGLERRLDRYPhQLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 835 LSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITEL 895
Cdd:COG1123 170 TTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
664-898 |
5.45e-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: 54.04 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNendsDMNAFKlcglNIKFQI--GKLNLILGSTGSGKSALLLGL--LGELNLISGSII-----VPS---L 731
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLK----NISFTIeeGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalCEKcgyV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 732 EPKHDLIPDCEGLTNSFAYCSQSAWLLNDTVKNN------IIFDN---FYNEDR-YNKVIDA---CGLKRDLEILPAGDL 798
Cdd:TIGR03269 73 ERPSKVGEPCPVCGGTLEPEEVDFWNLSDKLRRRirkriaIMLQRtfaLYGDDTvLDNVLEAleeIGYEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 799 TEIGEKG--IT-----LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLT 871
Cdd:TIGR03269 153 IEMVQLShrIThiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|....*..
gi 6321752 872 LRNAHFAIVLENGKVKNQGTITELQSK 898
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1340-1552 |
6.14e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1340 IRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDIS-KIDLVTLRRSITIIPQ---DPILFAG-TI 1414
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNfSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1415 KSNVdpydeydekKIFKALSQ------VNLISSHEfeevlnsEERFNSTHNKFLNLHTEIAEGGLN-LSQGERQLLFIAR 1487
Cdd:PRK09700 359 AQNM---------AISRSLKDggykgaMGLFHEVD-------EQRTAENQRELLALKCHSVNQNITeLSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 1488 SLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKS-TILTIAHRLRSVIDY-DRIIVMDAGEVKE 1552
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGkVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
700-901 |
6.64e-07 |
|
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: 52.60 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 700 ILGSTGSGKSALLLGLLGELNLISGSIIVPSLE----PKHDLipdceglTNSFAYCSQSAWLLNDTVKNNIIFDNFYNED 775
Cdd:cd03288 52 ICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDisklPLHTL-------RSRLSIILQDPILFSGSIRFNLDPECKCTDD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 776 RYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTavwiyENCITGPL 855
Cdd:cd03288 125 RLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-----ENILQKVV 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6321752 856 MK---NRTCILVTHNVSlTLRNAHFAIVLENGKVKNQGTITEL--QSKGLF 901
Cdd:cd03288 200 MTafaDRTVVTIAHRVS-TILDADLVLVLSRGILVECDTPENLlaQEDGVF 249
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1324-1550 |
7.67e-07 |
|
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: 50.89 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1324 EIENLSLryapnlPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLVTLRRS-ITI 1402
Cdd:cd03215 6 EVRGLSV------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPI---LFAG-TIKSNVdpydeydekkifkalsqvnLISSHefeevlnseerfnsthnkflnlhteiaegglnLSQG 1478
Cdd:cd03215 80 VPEDRKregLVLDlSVAENI-------------------ALSSL--------------------------------LSGG 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 1479 ERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNK-STILTIAHRLRSVIDY-DRIIVMDAGEV 1550
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
808-895 |
7.87e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.06 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTaVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVK 887
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPEL-VGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
....*...
gi 6321752 888 NQGTITEL 895
Cdd:PRK11264 224 EQGPAKAL 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
807-870 |
8.01e-07 |
|
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: 50.62 E-value: 8.01e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCiTGPLMknrTCILVTHNVSL 870
Cdd:cd03223 91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL-KELGI---TVISVGHRPSL 150
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1033-1289 |
9.62e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 52.48 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1033 KNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKI----FNNLLDLVLhaqiRFFDVTPVGRIMNRFSKDIEG 1108
Cdd:cd18540 36 GTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLrkkaFEHLQTLSF----SYFDKTPVGWIMARVTSDTQR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1109 VdQELIPY--LEVtIFCLIQCASIIFLITVITPR-----FLTVAVIVFVLYFFVGKwYLTASRELKRLDS-ITKSpifqh 1180
Cdd:cd18540 112 L-GEIISWglVDL-VWGITYMIGILIVMLILNWKlalivLAVVPVLAVVSIYFQKK-ILKAYRKVRKINSrITGA----- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1181 FSETLVGVCTIRAFGDErrfilenmnkiDQNNRAFFYLSVTVKWFSFR-----------VDMIG----AFIVLASGSFIL 1245
Cdd:cd18540 184 FNEGITGAKTTKTLVRE-----------EKNLREFKELTEEMRRASVRaarlsalflpiVLFLGsiatALVLWYGGILVL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 6321752 1246 LNIANIDSGLAGISltYAILFTDGALWLVRLYSTFEMNMNSVER 1289
Cdd:cd18540 253 AGAITIGTLVAFIS--YATQFFEPIQQLARVLAELQSAQASAER 294
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1323-1550 |
1.10e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.95 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTI--ITALFRLLEPITGCIKIDGQDISKIDlVTLR--R 1398
Cdd:CHL00131 8 LEIKNLHASVNEN--EILKGLNLSINKGEIHAIMGPNGSGKSTLskVIAGHPAYKILEGDILFKGESILDLE-PEERahL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1399 SITIIPQDPILFAGTikSNVDPYD-EYDEKKIFKALSQVNLIsshEFEEVLNSEERFNSTHNKFlnLHTEIAEGglnLSQ 1477
Cdd:CHL00131 85 GIFLAFQYPIEIPGV--SNADFLRlAYNSKRKFQGLPELDPL---EFLEIINEKLKLVGMDPSF--LSRNVNEG---FSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 1478 GERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRSEFNKST-ILTIAH--RLRSVIDYDRIIVMDAGEV 1550
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENsIILITHyqRLLDYIKPDYVHVMQNGKI 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1323-1506 |
1.17e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.02 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLppVIRNVSFKVDPQSKIGIVGRTGAGKSTiitaLFRLL----EPITGCIKI-DGQDISKIDlvtlr 1397
Cdd:TIGR03719 323 IEAENLTKAFGDKL--LIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMItgqeQPDSGTIEIgETVKLAYVD----- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1398 rsitiipqdpilfagTIKSNVDPydeydEKKIFKALSQVN---LISSHEFeevlNSEE---RFN---STHNKFLNlhtei 1468
Cdd:TIGR03719 392 ---------------QSRDALDP-----NKTVWEEISGGLdiiKLGKREI----PSRAyvgRFNfkgSDQQKKVG----- 442
|
170 180 190
....*....|....*....|....*....|....*...
gi 6321752 1469 aegglNLSQGERQLLFIARSLLREPKIILLDEATSSID 1506
Cdd:TIGR03719 443 -----QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
753-886 |
1.51e-06 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 50.82 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 753 QSAWLLND-TVKNNIIFdnfynedrynkVIDACGLKRD------LEILpagDLTEIGEKG----ITLSGGQKQRISLARA 821
Cdd:COG2884 86 QDFRLLPDrTVYENVAL-----------PLRVTGKSRKeirrrvREVL---DLVGLSDKAkalpHELSGGEQQRVAIARA 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 822 VYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK--NR---TCILVTHNVSLTLRNAHFAIVLENGKV 886
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIME------LLEeiNRrgtTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
808-869 |
1.68e-06 |
|
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: 50.93 E-value: 1.68e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENcitgpLMK-----NRTCILVTHNVS 869
Cdd:cd03293 132 LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEE-----LLDiwretGKTVLLVTHDID 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1353-1549 |
1.80e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.48 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1353 IGIVGRTGAGKSTIItalfRLLepiTGCIKIDGQDISKidlvTLRrsITIIPQdpilfagTIKSNVD-PYDEYDEKKIFK 1431
Cdd:COG1245 369 LGIVGPNGIGKTTFA----KIL---AGVLKPDEGEVDE----DLK--ISYKPQ-------YISPDYDgTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1432 ALSqvnliSSHEFEEVLNSeerfnsthnkfLNLHtEIAEGGL-NLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSD 1510
Cdd:COG1245 429 DFG-----SSYYKTEIIKP-----------LGLE-KLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6321752 1511 HLIQGIIR--SEFNKSTILTIAHRLrSVIDY--DRIIVMDaGE 1549
Cdd:COG1245 492 LAVAKAIRrfAENRGKTAMVVDHDI-YLIDYisDRLMVFE-GE 532
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1323-1564 |
2.22e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.17 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTiitalfrLLEPITGCIKIDGQDISKIDLvtLRRSIti 1402
Cdd:PRK09984 5 IRVEKLAKTFNQH--QALHAVDLNIHHGEMVALLGPSGSGKST-------LLRHLSGLITGDKSAGSHIEL--LGRTV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 ipQDPILFAGTIKSNvdpydEYDEKKIFKALSQVNLISSHE--FEEVLNSEERFNSTHNKFLNLHTEIAEGGLN------ 1474
Cdd:PRK09984 72 --QREGRLARDIRKS-----RANTGYIFQQFNLVNRLSVLEnvLIGALGSTPFWRTCFSWFTREQKQRALQALTrvgmvh 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1475 --------LSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKSTILTIAHRLRSViDY-----DR 1541
Cdd:PRK09984 145 fahqrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLR-DINQNDGITVVVTLHQV-DYalrycER 222
|
250 260
....*....|....*....|...
gi 6321752 1542 IIVMDAGEVKeYDRPSELLKDER 1564
Cdd:PRK09984 223 IVALRQGHVF-YDGSSQQFDNER 244
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
807-890 |
2.78e-06 |
|
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: 49.80 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDShtavwIYENCITGPLMKNR-----TCILVTHNVSLTLRNAHFAIVL 881
Cdd:cd03298 128 ELSGGERQRVALARVLVRDKPVLLLDEPFAALDP-----ALRAEMLDLVLDLHaetkmTVLMVTHQPEDAKRLAQRVVFL 202
|
....*....
gi 6321752 882 ENGKVKNQG 890
Cdd:cd03298 203 DNGRIAAQG 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
807-895 |
2.91e-06 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 51.25 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVyssAKH---VLLDDCLSAVD----SHTAVWIYEncitgpLMKNR--TCILVTHNVS--LTLrnA 875
Cdd:COG3842 135 QLSGGQQQRVALARAL---APEprvLLLDEPLSALDaklrEEMREELRR------LQRELgiTFIYVTHDQEeaLAL--A 203
|
90 100
....*....|....*....|
gi 6321752 876 HFAIVLENGKVKNQGTITEL 895
Cdd:COG3842 204 DRIAVMNDGRIEQVGTPEEI 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1338-1555 |
2.96e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.96 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1338 PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLE--PITGCIKIDGQDISkidlvtlrRSITIIpqdpilfagtik 1415
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG--------REASLI------------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1416 SNVDPYDEYDEKKifKALSQVNLisshefEEVLNSEERFNsthnkflnlhteiaegglNLSQGERQLLFIARSLLREPKI 1495
Cdd:COG2401 104 DAIGRKGDFKDAV--ELLNAVGL------SDAVLWLRRFK------------------ELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 1496 ILLDEATSSIDYDSDHLIQGIIRSEF--NKSTILTIAHR--LRSVIDYDRIIVMDAGEVKEYDR 1555
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLArrAGITLVVATHHydVIDDLQPDLLIFVGYGGVPEEKR 221
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1475-1559 |
3.03e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.18 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1475 LSQGERQLLFIARSLLREPKIILLDEATSSIdyDSDHLIQgiIRSEFNKstiltIAHRLRSVIDY------------DRI 1542
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL--DAALRVQ--MRIEISR-----LHKRLGRTMIYvthdqveamtlaDKI 204
|
90
....*....|....*..
gi 6321752 1543 IVMDAGEVKEYDRPSEL 1559
Cdd:PRK11000 205 VVLDAGRVAQVGKPLEL 221
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1323-1517 |
3.32e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYaPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCI--------------KIDGQDI 1388
Cdd:PLN03073 509 ISFSDASFGY-PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1389 SKIDLVTLRRSITIIPqdpilfagtiksnvdpydeydEKKifkalsqvnlISSHefeevLNSeerFNSTHNKFLN-LHTe 1467
Cdd:PLN03073 588 SSNPLLYMMRCFPGVP---------------------EQK----------LRAH-----LGS---FGVTGNLALQpMYT- 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1468 iaegglnLSQGERQLLFIARSLLREPKIILLDEATSSIDYDS-DHLIQGII 1517
Cdd:PLN03073 628 -------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQGLV 671
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
806-894 |
3.34e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.03 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 806 ITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDShtavwiyencitgP----LM--------KNRTCIL-VTHNVSLTL 872
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL-------------PrkreLLpylerlarEINIPILyVSHSLDEIL 193
|
90 100
....*....|....*....|..
gi 6321752 873 RNAHFAIVLENGKVKNQGTITE 894
Cdd:PRK11144 194 RLADRVVVLEQGKVKAFGPLEE 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1342-1563 |
3.52e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1342 NVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKIDLV-TLRRSITIIPQD----PILfagTIKS 1416
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQElhlvPEM---TVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1417 NvdpydeydekkIFkaLSQVnlisshefeevlnsEERFNSTHNKFLNLHT--EIAEGGLN---------LSQGERQLLFI 1485
Cdd:PRK11288 99 N-----------LY--LGQL--------------PHKGGIVNRRLLNYEAreQLEHLGVDidpdtplkyLSIGQRQMVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1486 ARSLLREPKIILLDEATSSIDY-DSDHLIQGIIRSEFNKSTILTIAHRLRSVIDY-DRIIVM-DAGEVKEYDRPSELLKD 1562
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIFALcDAITVFkDGRYVATFDDMAQVDRD 231
|
.
gi 6321752 1563 E 1563
Cdd:PRK11288 232 Q 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
808-906 |
3.65e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.43 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIyENCITgPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVK 887
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAI-EKLIT-ELKNEIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
90 100
....*....|....*....|.
gi 6321752 888 NQGTITEL--QSKGLFKEKYV 906
Cdd:PRK14246 232 EWGSSNEIftSPKNELTEKYV 252
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
807-897 |
3.71e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 49.75 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDshtavwiyencitgPLMK--------------NRTCILVTHNVSLTL 872
Cdd:COG3840 129 QLSGGQRQRVALARCLVRKRPILLLDEPFSALD--------------PALRqemldlvdelcrerGLTVLMVTHDPEDAA 194
|
90 100
....*....|....*....|....*
gi 6321752 873 RNAHFAIVLENGKVKNQGTITELQS 897
Cdd:COG3840 195 RIADRVLLVADGRIAADGPTAALLD 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
695-895 |
4.12e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.19 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 695 GKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKHdlIPDCE---GLTNSFAYCSQS-AWLLNDTVKNNIIFD- 769
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAK--ISDAElreVRRKKIAMVFQSfALMPHMTVLDNTAFGm 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 770 ---NFYNEDRYNKVIDACgLKRDLEILPAGDLTEigekgitLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWI 846
Cdd:PRK10070 132 elaGINAEERREKALDAL-RQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6321752 847 YENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITEL 895
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
338-640 |
4.31e-06 |
|
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: 50.51 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 338 LLIGMLWVLVNSIVNLLPTILMKRFLEIVDNPNRssscMNLAWLYIIGMFICRLTLAICNSQGQFVSDKICLRIrailig 417
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGL----RELLWLLALLILGVALLRGVFRYLQGYLAEKASQKV------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 418 eiyAKGLRRRLFTSPKTSSDSDSISANLGTIINLISID-----SFkvseLANYLYVTVQAVIMIIVVVGLLF--NFLgvs 490
Cdd:cd18542 71 ---AYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDvdtirRF----LAFGLVELVRAVLLFIGALIIMFsiNWK--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 491 aFAGISIILVmfPLNFLLANLLGKFQKQTLKCTDQRISKLN----ECLQNIRIVKYFAWERNIIN----EIKSIRQKELR 562
Cdd:cd18542 141 -LTLISLAII--PFIALFSYVFFKKVRPAFEEIREQEGELNtvlqENLTGVRVVKAFAREDYEIEkfdkENEEYRDLNIK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 563 SLLKKSLVWSVTSFLWFVTP--TLVTGVTFAIC------TFVqhedlnaplAFTTLSlfTLLKTPLDQLSNMLSFINQSK 634
Cdd:cd18542 218 LAKLLAKYWPLMDFLSGLQIvlVLWVGGYLVINgeitlgELV---------AFISYL--WMLIWPVRQLGRLINDMSRAS 286
|
....*.
gi 6321752 635 VSLKRI 640
Cdd:cd18542 287 ASAERI 292
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
808-839 |
4.75e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 50.72 E-value: 4.75e-06
10 20 30
....*....|....*....|....*....|..
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVD 839
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
806-886 |
5.21e-06 |
|
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: 48.55 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 806 ITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK-----NRTCILVTHNVSLTLRNAHFAIV 880
Cdd:cd03230 94 LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE------LLRelkkeGKTILLSSHILEEAERLCDRVAI 167
|
....*.
gi 6321752 881 LENGKV 886
Cdd:cd03230 168 LNNGRI 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
773-866 |
5.68e-06 |
|
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: 49.01 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 773 NEDRYNKVIDACGLkRDLEILPAGdlteigekgiTLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWiYENCIT 852
Cdd:COG4133 108 DREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVAL-LAELIA 175
|
90
....*....|....
gi 6321752 853 GPLMKNRTCILVTH 866
Cdd:COG4133 176 AHLARGGAVLLTTH 189
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
747-938 |
6.22e-06 |
|
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: 51.45 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 747 SFAYCSQSAWLLNDTVKNNIIFDNFYNEDRYNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSA 826
Cdd:TIGR01271 1293 AFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 827 KHVLLDDCLSAVDSHTAVWI-------YENCitgplmknrTCILVTHNVSLTLRNAHFaIVLENGKVKNQGTITE-LQSK 898
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIrktlkqsFSNC---------TVILSEHRVEALLECQQF-LVIEGSSVKQYDSIQKlLNET 1442
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6321752 899 GLFKEKyvqLSSRDSINEKNANRLKAPRKNDSQKIEPVTE 938
Cdd:TIGR01271 1443 SLFKQA---MSAADRLKLFPLHRRNSSKRKPQPKITALRE 1479
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
338-640 |
6.84e-06 |
|
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: 49.73 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 338 LLIGMLWVLVNSIVNLLPTILMKRFLEIVDNPNRSSSCMNLAWLyIIGMFICRltlAICNSQGQFVSDKICLRIRAILIG 417
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLA-IIGLFLLR---GLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 418 EIYAKGLRRRL--FTspKTSSdsdsisanlGTIINLISIDSFKVSE-LANYLYVTVQAVIMIIVVVGLLFNflgvsafag 494
Cdd:cd18552 77 DLFDKLLRLPLsfFD--RNSS---------GDLISRITNDVNQVQNaLTSALTVLVRDPLTVIGLLGVLFY--------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 495 IS-----IILVMFPLNFLLANLLGK----FQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIIN----EIKSIRQKEL 561
Cdd:cd18552 137 LDwkltlIALVVLPLAALPIRRIGKrlrkISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKrfrkANERLRRLSM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 562 RSLLKKSLVWSVTSFLwfvtptlvTGVTFAI-----CTFVQHEDLNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVS 636
Cdd:cd18552 217 KIARARALSSPLMELL--------GAIAIALvlwygGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAA 288
|
....
gi 6321752 637 LKRI 640
Cdd:cd18552 289 AERI 292
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
685-868 |
7.55e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.39 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 685 LCGLNIKFQIGKLNLILGSTGSGKSAlllgllgelnlisgsiIVPSLEPKHDLIPDCEgLTNSFAYCSQSAWLLN-DTV- 762
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKST----------------LLRSINRMNDLNPEVT-ITGSIVYNGHNIYSPRtDTVd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 763 -KNNI-------------IFDNFYNEDRYNKVIDACGLKRDLE--ILPAGDLTEIGEK----GITLSGGQKQRISLARAV 822
Cdd:PRK14239 84 lRKEIgmvfqqpnpfpmsIYENVVYGLRLKGIKDKQVLDEAVEksLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6321752 823 YSSAKHVLLDDCLSAVDSHTAVWIYENCITgpLMKNRTCILVTHNV 868
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLG--LKDDYTMLLVTRSM 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
808-929 |
1.17e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 49.31 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKhVLL-DDCLSAVDSHTAVWIYEncitgpLMK--NR----TCILVTHNVSLTLRNAHFAIV 880
Cdd:COG1135 141 LSGGQKQRVGIARALANNPK-VLLcDEATSALDPETTRSILD------LLKdiNRelglTIVLITHEMDVVRRICDRVAV 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 6321752 881 LENGKVKNQGTITEL--QSKGLFKEKYVQLSSRDSINEKNANRLKAPRKND 929
Cdd:COG1135 214 LENGRIVEQGPVLDVfaNPQSELTRRFLPTVLNDELPEELLARLREAAGGG 264
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
381-640 |
1.19e-05 |
|
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: 49.01 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 381 LYIIGMFICRLTLAicnsqgqFVSdKICLRIrailIGEIYAKGLRRRLFTS--PKTSSDSDSISAnlGTIINLISIDSFK 458
Cdd:cd18577 51 LYFVYLGIGSFVLS-------YIQ-TACWTI----TGERQARRIRKRYLKAllRQDIAWFDKNGA--GELTSRLTSDTNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 459 VSE-LANYLYVTVQAVIMIIV--VVGLLFNF-LgvsAFAGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECL 534
Cdd:cd18577 117 IQDgIGEKLGLLIQSLSTFIAgfIIAFIYSWkL---TLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEAL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 535 QNIRIVKYFAWERNIINEIKSIRQKELRSLLKKSLVWSV-TSFLWFVTPtlvtgVTFAIC-----TFVQHEDLNAPLAFT 608
Cdd:cd18577 194 SSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLgLGLLFFIIF-----AMYALAfwygsRLVRDGEISPGDVLT 268
|
250 260 270
....*....|....*....|....*....|..
gi 6321752 609 TLSLFTLLKTPLDQLSNMLSFINQSKVSLKRI 640
Cdd:cd18577 269 VFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
798-866 |
1.26e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 47.86 E-value: 1.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 798 LTEIGEKGI------TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTH 866
Cdd:COG4136 118 LEEAGLAGFadrdpaTLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
1028-1267 |
1.31e-05 |
|
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: 49.02 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1028 MTDSSKNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRAS--------RKIfnnlldLVLHAQIRffDVTPVGRIM 1099
Cdd:cd18579 28 SSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRsalssliyRKA------LRLSSSAR--QETSTGEIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1100 NRFSKDIEGVDqELIPYLEVTIFCLIQ-CASIIFLITVITPRFLT---VAVIVFVLYFFVGKWYLTASREL-----KRLd 1170
Cdd:cd18579 100 NLMSVDVQRIE-DFFLFLHYLWSAPLQiIVALYLLYRLLGWAALAglgVLLLLIPLQAFLAKLISKLRKKLmkatdERV- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1171 sitkspifQHFSETLVGVCTIRAFGDERRFilenMNKIDQ-------NNRAFFYLSVTVKWFSFrvdMIGAFIVLAS-GS 1242
Cdd:cd18579 178 --------KLTNEILSGIKVIKLYAWEKPF----LKRIEElrkkelkALRKFGYLRALNSFLFF---STPVLVSLATfAT 242
|
250 260
....*....|....*....|....*
gi 6321752 1243 FILLnianidsglaGISLTYAILFT 1267
Cdd:cd18579 243 YVLL----------GNPLTAAKVFT 257
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
808-895 |
1.37e-05 |
|
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: 48.10 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDS-------------HTAVWIyencitgplmknrTCILVTHNVSLTLRN 874
Cdd:cd03296 137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkelrrwlrrlHDELHV-------------TTVFVTHDQEEALEV 203
|
90 100
....*....|....*....|.
gi 6321752 875 AHFAIVLENGKVKNQGTITEL 895
Cdd:cd03296 204 ADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
767-920 |
1.52e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.55 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 767 IFDNFYNEDRYNKVIDacglKRDLEILPAGDLTEIG----------EKGITLSGGQKQRISLARAVYSSAKHVLLDDCLS 836
Cdd:PRK14271 117 IMDNVLAGVRAHKLVP----RKEFRGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 837 AVDSHTAVWIYEncITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITELQSKGLFKE--KYVQLSSRDSI 914
Cdd:PRK14271 193 ALDPTTTEKIEE--FIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAEtaRYVAGLSGDVK 270
|
....*.
gi 6321752 915 NEKNAN 920
Cdd:PRK14271 271 DAKRGN 276
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
772-882 |
1.70e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.42 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 772 YNEDRYNKVIDACGLKrDLeilpAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEnci 851
Cdd:COG4178 455 FSDAELREALEAVGLG-HL----AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ--- 526
|
90 100 110
....*....|....*....|....*....|....*
gi 6321752 852 tgpLMKNR----TCILVTHNVSLtlrNAHFAIVLE 882
Cdd:COG4178 527 ---LLREElpgtTVISVGHRSTL---AAFHDRVLE 555
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
798-903 |
1.80e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 48.09 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 798 LTEIGEKGIT-LSGGQKQRISLARAVYSSAKHVLLDDCLSAVD-SHTAvwiyencitgPLMK--------NRTCILVTHN 867
Cdd:PRK11231 128 INHLADRRLTdLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDiNHQV----------ELMRlmrelntqGKTVVTVLHD 197
|
90 100 110
....*....|....*....|....*....|....*.
gi 6321752 868 VSLTLRNAHFAIVLENGKVKNQGTITELQSKGLFKE 903
Cdd:PRK11231 198 LNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRT 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
808-886 |
1.83e-05 |
|
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: 46.65 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMKN-----RTCILVTHNVSLTLRNAHFAIVLE 882
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK------VIRRlraqgVAVIFISHRLDEVFEIADRVTVLR 156
|
....
gi 6321752 883 NGKV 886
Cdd:cd03216 157 DGRV 160
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1032-1247 |
1.88e-05 |
|
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: 48.21 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1032 SKNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSkDIEGVdQ 1111
Cdd:cd18570 35 SGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKI-R 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1112 ELIPYLEVTIF--CLIQCASIIFLITVITPRFLTVAVIVFV---LYFFVGKWYLTASRELKRLDSITKSpifqHFSETLV 1186
Cdd:cd18570 113 EAISSTTISLFldLLMVIISGIILFFYNWKLFLITLLIIPLyilIILLFNKPFKKKNREVMESNAELNS----YLIESLK 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 1187 GVCTIRAFGDERRFILENMNKIDQNNRAFFYLSVTVKWFSFRVDMIGAF---IVLASGSFILLN 1247
Cdd:cd18570 189 GIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIgslLILWIGSYLVIK 252
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1323-1560 |
1.91e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.65 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPPV--IRNVSFKVDPQSKIGIVGRTGAGKSTIITAlfrllepITGCIK------IDGQDISKIDLV 1394
Cdd:PRK15093 4 LDIRNLTIEFKTSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKA-------ICGVTKdnwrvtADRMRFDDIDLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1395 TL----RR-----SITIIPQDPilfagtiKSNVDPydeydEKKIFKALSQVnlISSHEFEEvlNSEERFNSTHNKFLNL- 1464
Cdd:PRK15093 77 RLspreRRklvghNVSMIFQEP-------QSCLDP-----SERVGRQLMQN--IPGWTYKG--RWWQRFGWRKRRAIELl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1465 -------HTEIAEG-GLNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRS--EFNKSTILTIAHRLR 1534
Cdd:PRK15093 141 hrvgikdHKDAMRSfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLISHDLQ 220
|
250 260
....*....|....*....|....*..
gi 6321752 1535 SVIDY-DRIIVMDAGEVKEYDRPSELL 1560
Cdd:PRK15093 221 MLSQWaDKINVLYCGQTVETAPSKELV 247
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
687-876 |
1.97e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 47.18 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 687 GLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIivpSLEPKHDLIPDcegltnsfaYCSQSAWL-----LND- 760
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI---KLDGGDIDDPD---------VAEACHYLghrnaMKPa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 761 -TVKNNIIF-DNFYNEDRYN--KVIDACGLkRDLEILPAGDlteigekgitLSGGQKQRISLARAVYSSAKHVLLDDCLS 836
Cdd:PRK13539 88 lTVAENLEFwAAFLGGEELDiaAALEAVGL-APLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6321752 837 AVDSHtAVWIYENCITGPLMKNRTCILVTHNvSLTLRNAH 876
Cdd:PRK13539 157 ALDAA-AVALFAELIRAHLAQGGIVIAATHI-PLGLPGAR 194
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1342-1549 |
2.01e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1342 NVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDIS-KIDLVTLRRSITIIPQD-PILFAGTIKSNVd 1419
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSVMDNM- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1420 PYDEYDEKKIFkalsqvnlisshefeevLNSEERFNSTHNKFLNLHTEI--AEGGLNLSQGERQLLFIARSLLREPKIIL 1497
Cdd:PRK10982 95 WLGRYPTKGMF-----------------VDQDKMYRDTKAIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 1498 LDEATSSI-DYDSDHLIQgIIRSEFNKST-ILTIAHRLRSVIDY-DRIIVMDAGE 1549
Cdd:PRK10982 158 MDEPTSSLtEKEVNHLFT-IIRKLKERGCgIVYISHKMEEIFQLcDEITILRDGQ 211
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1044-1243 |
2.42e-05 |
|
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: 47.87 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1044 VYFLIGIIQAmlgGFKTMMTFLSGmRASRKIfnnLLDLVL----HAQ---IRFFDVTPVGRIMNRFSKDIEGVdQELIPY 1116
Cdd:cd18546 44 AYLAVVLAGW---VAQRAQTRLTG-RTGERL---LYDLRLrvfaHLQrlsLDFHERETSGRIMTRMTSDIDAL-SELLQT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1117 -LEVTIFCLIQCASIIFLITVITPRFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFG 1195
Cdd:cd18546 116 gLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFR 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 1196 DERRfILENMNKI-----DQNNRAFFYLSVtvkWFSFrVDMIGAF---IVLASGSF 1243
Cdd:cd18546 196 RERR-NAERFAELsddyrDARLRAQRLVAI---YFPG-VELLGNLataAVLLVGAW 246
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
338-640 |
2.43e-05 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 48.20 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 338 LLIGMLWVLVNSIVNLLPTILMKRfleIVDNPNRSSSCMNLAWLyIIGMFICRLTL-AICNSQGQFVSDKICLRIRAILI 416
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKN---LIDALSAGGSSGGLLAL-LVALFLLQAVLsALSSYLLGRTGERVVLDLRRRLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 417 geiyakglrRRLFTSPKTSSDSDSIsanlGTIINLISIDSFKVSELANYLYV-TVQAVIMIIVVVGLLFnFLGVSAFAgi 495
Cdd:cd18551 77 ---------RRLLRLPVSFFDRRRS----GDLVSRVTNDTTLLRELITSGLPqLVTGVLTVVGAVVLMF-LLDWVLTL-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 496 sIILVMFPLNFLLANLLGKF-QKQTLKCTDQR---ISKLNECLQNIRIVKYFAWE----RNIINEIKSIRQKELRSLLKK 567
Cdd:cd18551 141 -VTLAVVPLAFLIILPLGRRiRKASKRAQDALgelSAALERALSAIRTVKASNAEeretKRGGEAAERLYRAGLKAAKIE 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321752 568 SLVWSVTSflwfvtpTLVTGVTFAICTF----VQHEDLNAPlAFTTLSLF-TLLKTPLDQLSNMLSFINQSKVSLKRI 640
Cdd:cd18551 220 ALIGPLMG-------LAVQLALLVVLGVggarVASGALTVG-TLVAFLLYlFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
807-886 |
2.67e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.70 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKV 886
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
683-868 |
3.23e-05 |
|
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: 48.86 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 683 FKLCG------LNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSlepkHDLIPDCEGLTNSFAYCSQSAW 756
Cdd:TIGR01257 938 FEPSGrpavdrLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG----KDIETNLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 757 LLND-TVKNNIIFdnfYNEDRyNKVIDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCL 835
Cdd:TIGR01257 1014 LFHHlTVAEHILF---YAQLK-GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190
....*....|....*....|....*....|...
gi 6321752 836 SAVDSHTAVWIYENCITgpLMKNRTCILVTHNV 868
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLK--YRSGRTIIMSTHHM 1120
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
664-903 |
3.26e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.74 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENdSDMNAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEP-----KHDLI 738
Cdd:PRK13637 3 IKIENLTHIYMEG-TPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkvKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 739 PDCEGLTnsFAYCSQSawLLNDTVKNNIIFD----NFYNEDRYNKVIDA---CGLKRDleilpagdltEIGEKG-ITLSG 810
Cdd:PRK13637 82 RKKVGLV--FQYPEYQ--LFEETIEKDIAFGpinlGLSEEEIENRVKRAmniVGLDYE----------DYKDKSpFELSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 811 GQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVKNQG 890
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
250
....*....|...
gi 6321752 891 TITElqskgLFKE 903
Cdd:PRK13637 228 TPRE-----VFKE 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1323-1563 |
3.33e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSlryAPNLP-PVirnvSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDI---SKIDLVtlRR 1398
Cdd:PRK11288 258 LRLDGLK---GPGLRePI----SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirSPRDAI--RA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1399 SITIIPQDpilfagtiksnvdpydeydeKKifkalsQVNLISSHEFEEVLN-SEERFNSTHNKFLNLHTEIAEGGL---- 1473
Cdd:PRK11288 329 GIMLCPED--------------------RK------AEGIIPVHSVADNINiSARRHHLRAGCLINNRWEAENADRfirs 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1474 -------------NLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNKS--TILTIAHRLRSVID 1538
Cdd:PRK11288 383 lniktpsreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIY-ELAAQgvAVLFVSSDLPEVLG 461
|
250 260
....*....|....*....|....*.
gi 6321752 1539 Y-DRIIVMDAGEVKeydrpSELLKDE 1563
Cdd:PRK11288 462 VaDRIVVMREGRIA-----GELAREQ 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1323-1555 |
3.34e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.46 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSlryapnlPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDI---SKIDlvTLRRS 1399
Cdd:PRK10762 258 LKVDNLS-------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrSPQD--GLANG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQDP----ILFAGTIKSNVDpydeydekkiFKALSQVnlisSHEFEEVLNSEERFNSTHN-KFLNLHTEIAEGGL- 1473
Cdd:PRK10762 329 IVYISEDRkrdgLVLGMSVKENMS----------LTALRYF----SRAGGSLKHADEQQAVSDFiRLFNIKTPSMEQAIg 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1474 NLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIrSEFNKS--TILTIAHRLRSVIDY-DRIIVMDAGEV 1550
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFKAEglSIILVSSEMPEVLGMsDRILVMHEGRI 473
|
....*.
gi 6321752 1551 K-EYDR 1555
Cdd:PRK10762 474 SgEFTR 479
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
695-924 |
3.77e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 47.91 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 695 GKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKHdlIPDCEGLTNSFAycsQSAWLL-NDTVKNNIIFdnfyn 773
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMF---QSYALFpHMTVEQNIAF----- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 774 edrynkvidacGLKRDLeiLPAGDLTEIGEKGIT--------------LSGGQKQRISLARAVYSSAKHVLLDDCLSAVD 839
Cdd:PRK11607 115 -----------GLKQDK--LPKAEIASRVNEMLGlvhmqefakrkphqLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 840 -------SHTAVWIYENCitgplmkNRTCILVTHNVSLTLRNA-HFAIVlengkvkNQGtitelqskglfkeKYVQLSSR 911
Cdd:PRK11607 182 kklrdrmQLEVVDILERV-------GVTCVMVTHDQEEAMTMAgRIAIM-------NRG-------------KFVQIGEP 234
|
250
....*....|...
gi 6321752 912 DSINEKNANRLKA 924
Cdd:PRK11607 235 EEIYEHPTTRYSA 247
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
687-886 |
3.95e-05 |
|
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: 46.48 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 687 GLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSII-----VPSLEPKHDLIpdcegltnsfAYCSQS-AWLLND 760
Cdd:cd03301 18 DLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdVTDLPPKDRDI----------AMVFQNyALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 761 TVKNNIIFdNFYNEDRYNKVIDAcGLKRDLEILPAGDLteIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDS 840
Cdd:cd03301 88 TVYDNIAF-GLKLRKVPKDEIDE-RVREVAELLQIEHL--LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6321752 841 HTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKV 886
Cdd:cd03301 164 KLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
803-877 |
4.05e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.08 E-value: 4.05e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 803 EKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncITGPLMKNRTCILVTHNVSLTLRNAHF 877
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEE--LMHELKEQYTIIIVTHNMQQAARVSDM 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
807-881 |
4.72e-05 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 46.07 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMK-----NRTCILVTHNvsLTLRNAHFAIVL 881
Cdd:NF040873 119 ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA------LLAeeharGATVVVVTHD--LELVRRADPCVL 190
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
688-906 |
4.88e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 46.81 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 688 LNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPslEPKHDLIPDCEGLTNSFAYCSQSAWLLND-TVKNNI 766
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID--DEDISLLPLHARARRGIGYLPQEASIFRRlSVYDNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 767 -----IFDNFYNEDRYNkvidacglkRDLEILPAGDLTEIGEK-GITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDS 840
Cdd:PRK10895 100 mavlqIRDDLSAEQRED---------RANELMEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 841 HTAVWIYEncITGPLMKNRTCILVT-HNVSLTLRNAHFAIVLENGKVKNQGTITELQSKGLFKEKYV 906
Cdd:PRK10895 171 ISVIDIKR--IIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL 235
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
338-640 |
4.95e-05 |
|
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: 47.00 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 338 LLIGMLWVLVNSIVNLLPTILMKRFleiVDNP-NRSSSCMNLAWLYIIGMFICRLTLAICNSQGQFVSDKICLRIraili 416
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRA---IDDYiVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRI----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 417 geIYAkgLRRRLFTSPKTSSDS--DSISAnlGTIINLISIDSFKVSEL-ANYLYVTVQAVIMIIVVVGLLFNF---LGVs 490
Cdd:cd18544 73 --IYD--LRRDLFSHIQRLPLSffDRTPV--GRLVTRVTNDTEALNELfTSGLVTLIGDLLLLIGILIAMFLLnwrLAL- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 491 afagisIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLN----ECLQNIRIVKYFAWERNIINEIKSIRQKELRSLLK 566
Cdd:cd18544 146 ------ISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNaflqESISGMSVIQLFNREKREFEEFDEINQEYRKANLK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 567 K----SLVWSVTSFLWFVTPTLVTGVtFAIctfvqhEDLNAPLAFTTLSLFTL----LKTPLDQLSNMLSFINQSKVSLK 638
Cdd:cd18544 220 SiklfALFRPLVELLSSLALALVLWY-GGG------QVLSGAVTLGVLYAFIQyiqrFFRPIRDLAEKFNILQSAMASAE 292
|
..
gi 6321752 639 RI 640
Cdd:cd18544 293 RI 294
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
416-640 |
5.52e-05 |
|
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: 47.06 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 416 IGEIYAKGLRRRLFTS-----------PKTSSdsdsisanlGTIINLISIDSFKVSEL-ANYLYVTVQAVIMIIV--VVG 481
Cdd:cd18578 79 AGERLTRRLRKLAFRAilrqdiawfddPENST---------GALTSRLSTDASDVRGLvGDRLGLILQAIVTLVAglIIA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 482 LLFNF-LgvsAFAGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIVKYFAWERNIIN----EIKSI 556
Cdd:cd18578 150 FVYGWkL---ALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEkyeeALEEP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 557 RQKELRSLLKKSLVWSVTSFLWFvtptLVTGVTFAI-CTFVQHEDLNAPLAFTTLS--LFTLLktpldQLSNMLSF---I 630
Cdd:cd18578 227 LKKGLRRALISGLGFGLSQSLTF----FAYALAFWYgGRLVANGEYTFEQFFIVFMalIFGAQ-----SAGQAFSFapdI 297
|
250
....*....|
gi 6321752 631 NQSKVSLKRI 640
Cdd:cd18578 298 AKAKAAAARI 307
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
808-897 |
5.90e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 46.11 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVD----SHTAVWIYENCITgplmKNRTCILVTHNVSLTLRNAHFAIVLEN 883
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQE----RQLTLLMVSHSLEDAARIAPRSLVVAD 205
|
90
....*....|....
gi 6321752 884 GKVKNQGTITELQS 897
Cdd:PRK10771 206 GRIAWDGPTDELLS 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
787-893 |
5.97e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 46.55 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 787 KRDLEILPAGDLTEIGEK-GITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSH-TA---VWIYENCITGPlmknrTC 861
Cdd:PRK11124 120 ARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAqivSIIRELAETGI-----TQ 194
|
90 100 110
....*....|....*....|....*....|..
gi 6321752 862 ILVTHNVSLTLRNAHFAIVLENGKVKNQGTIT 893
Cdd:PRK11124 195 VIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
808-839 |
7.48e-05 |
|
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: 46.08 E-value: 7.48e-05
10 20 30
....*....|....*....|....*....|..
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVD 839
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
807-887 |
7.89e-05 |
|
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: 45.71 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIyencitGPLMKN-----RTCILVTHNVSLTLRNAHFAIVL 881
Cdd:cd03226 126 SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV------GELIRElaaqgKAVIVITHDYEFLAKVCDRVLLL 199
|
....*.
gi 6321752 882 ENGKVK 887
Cdd:cd03226 200 ANGAIV 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1323-1506 |
8.47e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLppVIRNVSFKVDPQSKIGIVGRTGAGKSTiitaLFRLL----EPITGCIKIdGQ--DISKIDlvtl 1396
Cdd:PRK11819 325 IEAENLSKSFGDRL--LIDDLSFSLPPGGIVGIIGPNGAGKST----LFKMItgqeQPDSGTIKI-GEtvKLAYVD---- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1397 rrsitiipQDpilfagtiKSNVDPydeydEKKIFKALSQVN-LISSHEFEevLNSEE---RFN---STHNKFLNlhteia 1469
Cdd:PRK11819 394 --------QS--------RDALDP-----NKTVWEEISGGLdIIKVGNRE--IPSRAyvgRFNfkgGDQQKKVG------ 444
|
170 180 190
....*....|....*....|....*....|....*..
gi 6321752 1470 egglNLSQGERQLLFIARSLLREPKIILLDEATSSID 1506
Cdd:PRK11819 445 ----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
685-895 |
8.72e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.12 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 685 LCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKhdLIPDCEGLTNSFAycSQSAWLLNdtVKN 764
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTIN--LVRDKDGQLKVAD--KNQLRLLR--TRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 765 NIIFDNF-------YNEDRYNKVIDACGL------KRDLEILPAGDLTEI--GEKGITLSGGQKQRISLARAVYSSAKHV 829
Cdd:PRK10619 95 TMVFQHFnlwshmtVLENVMEAPIQVLGLskqearERAVKYLAKVGIDERaqGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 830 LLDDCLSAVDSHtavwiyencITGPLMK--------NRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITEL 895
Cdd:PRK10619 175 LFDEPTSALDPE---------LVGEVLRimqqlaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
659-898 |
8.77e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 46.33 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 659 PDKNKIEFKNATLTWNenDSDMNAFKlcGLNIKFQIGKLNLILGSTGSGKSALLLGllgelnlISGsIIVPSLEPKHDLI 738
Cdd:PRK13640 1 MKDNIVEFKHVSFTYP--DSKKPALN--DISFSIPRGSWTALIGHNGSGKSTISKL-------ING-LLLPDDNPNSKIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 739 PDCEGLTnsfaycSQSAWLLNDTVknNIIFDNFYNEDRYNKVID--ACGL------KRDLEILPAGDLTEIG------EK 804
Cdd:PRK13640 69 VDGITLT------AKTVWDIREKV--GIVFQNPDNQFVGATVGDdvAFGLenravpRPEMIKIVRDVLADVGmldyidSE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 805 GITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSlTLRNAHFAIVLENG 884
Cdd:PRK13640 141 PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDG 219
|
250
....*....|....
gi 6321752 885 KVKNQGTITELQSK 898
Cdd:PRK13640 220 KLLAQGSPVEIFSK 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
800-903 |
9.70e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.80 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 800 EIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIyENCITGPLMKNR-TCILVTHNVSLTLRNAHFA 878
Cdd:PRK14258 143 KIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSElTMVIVSHNLHQVSRLSDFT 221
|
90 100
....*....|....*....|....*
gi 6321752 879 IVLENgkvkNQGTITELQSKGLFKE 903
Cdd:PRK14258 222 AFFKG----NENRIGQLVEFGLTKK 242
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
774-895 |
1.71e-04 |
|
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: 45.33 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 774 EDRYNKVIDACGLKRDLEILPagdlteiGEkgitLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDshtavwiyencitg 853
Cdd:cd03294 138 EERAAEALELVGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAFSALD-------------- 192
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 854 PLMKN--------------RTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITEL 895
Cdd:cd03294 193 PLIRRemqdellrlqaelqKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
807-899 |
1.72e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 45.13 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLrNAHFAIVLENGKV 886
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM-EADHVIVMNKGTV 220
|
90
....*....|...
gi 6321752 887 KNQGTITELQSKG 899
Cdd:PRK13648 221 YKEGTPTEIFDHA 233
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1349-1549 |
1.84e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.52 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1349 PQSKIGIVGRTGAGKSTIITALFRLLEP-ITGCIKIDGQDISKIDLVTLRrsitiipqdpilfagtiksnvdpydeydek 1427
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPpGGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1428 kifkalsqvnlisshefeevlnseerfnsthnkflnlHTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSIDY 1507
Cdd:smart00382 51 -------------------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDA 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 1508 DSDHLIQGIIRSEFNKS-------TILTIAHRLRSVID------YDRIIVMDAGE 1549
Cdd:smart00382 94 EQEALLLLLEELRLLLLlkseknlTVILTTNDEKDLGPallrrrFDRRIVLLLIL 148
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1032-1289 |
1.88e-04 |
|
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: 45.15 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1032 SKNKHNAFYYLTVYFLIGIIQAMLGGFKTMMT------FLSGMRasRKIFNNLLDLvlhaQIRFFDVTPVGRIMNRFSKD 1105
Cdd:cd18545 33 NGDLSGLLIIALLFLALNLVNWVASRLRIYLMakvgqrILYDLR--QDLFSHLQKL----SFSFFDSRPVGKILSRVIND 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1106 IEGVdQELIPYLEVTIFC-LIQCASIIFLITVITPRFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSET 1184
Cdd:cd18545 107 VNSL-SDLLSNGLINLIPdLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHES 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1185 LVGVCTIRAFGDERrfilENMNKIDQNNRAFF--YLSVTVKWFSFR--VDMIGAF---IVLASGSFILLNIAnIDSGLAG 1257
Cdd:cd18545 186 ISGIRVIQSFARED----ENEEIFDELNRENRkaNMRAVRLNALFWplVELISALgtaLVYWYGGKLVLGGA-ITVGVLV 260
|
250 260 270
....*....|....*....|....*....|..
gi 6321752 1258 ISLTYAILFTDGALWLVRLYSTFEMNMNSVER 1289
Cdd:cd18545 261 AFIGYVGRFWQPIRNLSNFYNQLQSAMASAER 292
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
664-895 |
2.08e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.23 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDSdmNAFK-LCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKHDLIPDCE 742
Cdd:PRK13631 22 LRVKNLYCVFDEKQE--NELVaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 743 GLTN---------------SFAYCSQSAWLLNDTVKNNIIF-------DNFYNEDRYNKVIDACGLKRD-LEILPAGdlt 799
Cdd:PRK13631 100 ITNPyskkiknfkelrrrvSMVFQFPEYQLFKDTIEKDIMFgpvalgvKKSEAKKLAKFYLNKMGLDDSyLERSPFG--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 800 eigekgitLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEnCITGPLMKNRTCILVTHNVSLTLRNAHFAI 879
Cdd:PRK13631 177 --------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVI 247
|
250
....*....|....*.
gi 6321752 880 VLENGKVKNQGTITEL 895
Cdd:PRK13631 248 VMDKGKILKTGTPYEI 263
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
421-588 |
2.08e-04 |
|
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: 45.23 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 421 AKGLRRRLFTS-----------PKT-------SSDSDSISANLGTIINlisidsfkvselanylyVTVQAVIMIIVVVGL 482
Cdd:cd18572 68 VRRLRRDLFRSllrqdiaffdaTKTgeltsrlTSDCQKVSDPLSTNLN-----------------VFLRNLVQLVGGLAF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 483 LFN---FLGVSAFagisiilVMFPLNFLLANLLGKFQKQTLKCTDQRISKLN----ECLQNIRIVKYFAWERNIINEIKS 555
Cdd:cd18572 131 MFSlswRLTLLAF-------ITVPVIALITKVYGRYYRKLSKEIQDALAEANqvaeEALSNIRTVRSFATEEREARRYER 203
|
170 180 190
....*....|....*....|....*....|...
gi 6321752 556 IRQKELRSLLKKSLVWSVTSFLWFVTPTLVTGV 588
Cdd:cd18572 204 ALDKALKLSVRQALAYAGYVAVNTLLQNGTQVL 236
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
342-640 |
2.37e-04 |
|
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: 44.88 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 342 MLWVLVNSIVNLLPTILMkrfLEIVDN--PNRSsscMNLAWLYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILIGEI 419
Cdd:cd18566 8 LLASLFINILALATPLFI---LQVYDRviPNES---IPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 420 YakglrRRLFTSPKTSSDSDSISANLGTIINLISIDSFkvselanylyVTVQAvIMIIVVVGLLFNFLGVSAFAGISIIL 499
Cdd:cd18566 82 F-----EHLLSLPLSFFEREPSGAHLERLNSLEQIREF----------LTGQA-LLALLDLPFVLIFLGLIWYLGGKLVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 500 V---MFPLNFLLANLLGKFQKQTLKCT----DQRISKLNECLQNIRIVKYFA--------WERNIINEIKSIRQKELRSL 564
Cdd:cd18566 146 VplvLLGLFVLVAILLGPILRRALKERsradERRQNFLIETLTGIHTIKAMAmepqmlrrYERLQANAAYAGFKVAKINA 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 565 LKKSL--VWSVTSFLwfvtPTLVTGVTFAIctfvQHE-DLNAPLAFTTLSLFTLlkTPLDQLSNMLSFINQSKVSLKRI 640
Cdd:cd18566 226 VAQTLgqLFSQVSMV----AVVAFGALLVI----NGDlTVGALIACTMLSGRVL--QPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1352-1460 |
2.41e-04 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 42.22 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1352 KIGIVGRTGAGKSTIITALFRL-----------LEPITGCIKIDGQDISKIDLvtlrrsitiipqdpilfAGTIKsnvDP 1420
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAkaivsdypgttRDPNEGRLELKGKQIILVDT-----------------PGLIE---GA 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6321752 1421 YDEYDEKKIFKALSQVNLI-----SSHEFEEVLNSEERFNSTHNK 1460
Cdd:pfam01926 61 SEGEGLGRAFLAIIEADLIlfvvdSEEGITPLDEELLELLRENKK 105
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1033-1239 |
2.45e-04 |
|
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: 44.73 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1033 KNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQ- 1111
Cdd:cd18542 33 GLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRf 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1112 ------ELIPYLEVTIFCLIQCASIIFLITVITprFLTVAVIVFVLYFF---VGKWYLTASRELKRLDSITKspifqhfs 1182
Cdd:cd18542 113 lafglvELVRAVLLFIGALIIMFSINWKLTLIS--LAIIPFIALFSYVFfkkVRPAFEEIREQEGELNTVLQ-------- 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321752 1183 ETLVGVCTIRAFGDERRfileNMNKIDQNNRAFFYLSVTV-----KWFSFrVDMIGAFIVLA 1239
Cdd:cd18542 183 ENLTGVRVVKAFAREDY----EIEKFDKENEEYRDLNIKLakllaKYWPL-MDFLSGLQIVL 239
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
808-895 |
2.69e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.12 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVK 887
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
....*...
gi 6321752 888 NQGTITEL 895
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
807-911 |
2.71e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 44.59 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENcITGPLMKNRTCILVTHNVSlTLRNAHFAIVLENGKV 886
Cdd:PRK13644 136 TLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLER-IKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKI 213
|
90 100 110
....*....|....*....|....*....|.
gi 6321752 887 KNQGTI------TELQSKGLFKEKYVQLSSR 911
Cdd:PRK13644 214 VLEGEPenvlsdVSLQTLGLTPPSLIELAEN 244
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1323-1564 |
2.93e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.73 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLPP--VIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLE-P---ITGCIKIDGQDISKIDLVTL 1396
Cdd:PRK11022 4 LNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1397 RR----SITIIPQDPIlfagtikSNVDP-----YdeydekKIFKALSqvnlisSHEFEevlNSEERfnstHNKFLNLHTE 1467
Cdd:PRK11022 84 RNlvgaEVAMIFQDPM-------TSLNPcytvgF------QIMEAIK------VHQGG---NKKTR----RQRAIDLLNQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1468 IA----EGGLN-----LSQGERQLLFIARSLLREPKIILLDEATSSIDYDsdhlIQGII--------RSEfNKSTILtIA 1530
Cdd:PRK11022 138 VGipdpASRLDvyphqLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVT----IQAQIielllelqQKE-NMALVL-IT 211
|
250 260 270
....*....|....*....|....*....|....*
gi 6321752 1531 HRLRSVIDY-DRIIVMDAGEVKEYDRPSELLKDER 1564
Cdd:PRK11022 212 HDLALVAEAaHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1339-1405 |
3.30e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.43 E-value: 3.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 1339 VIRNVSFKVDPQSKIGIVGRTGAGKSTIITALF-RLLEP-------ITGCIKIDGQDISKIDLVTLRRSITIIPQ 1405
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
808-867 |
3.47e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.10 E-value: 3.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYenCITGPLM-KNRTCILVTHN 867
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM--AILHQLRdRGHTVIIVTHD 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
661-899 |
3.60e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 44.34 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 661 KNKIEFKNATLTWNENDsdmNAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVpslepkhdlipD 740
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQ---EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII-----------D 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 741 CEGLTnsfaycSQSAWLLNDtvKNNIIFDNFYN-------EDRY-----NKVIDACGLK-RDLEILPAGDLTEIGEKGIT 807
Cdd:PRK13650 68 GDLLT------EENVWDIRH--KIGMVFQNPDNqfvgatvEDDVafgleNKGIPHEEMKeRVNEALELVGMQDFKEREPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 -LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDS-------HTAVWIYENcitgplmKNRTCILVTHN---VSLTLRnah 876
Cdd:PRK13650 140 rLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPegrleliKTIKGIRDD-------YQMTVISITHDldeVALSDR--- 209
|
250 260
....*....|....*....|...
gi 6321752 877 fAIVLENGKVKNQGTITELQSKG 899
Cdd:PRK13650 210 -VLVMKNGQVESTSTPRELFSRG 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1323-1506 |
3.62e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 44.31 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQdisKIDLVTLRRSItI 1402
Cdd:PRK11248 2 LQISHLYADYGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPGAERGV-V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 IPQDPILFAGTIKSNVD--------PYDEyDEKKIFKALSQVNLISshefeevlnSEERFnsthnkflnlhteIAEggln 1474
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAfglqlagvEKMQ-RLEIAHQMLKKVGLEG---------AEKRY-------------IWQ---- 128
|
170 180 190
....*....|....*....|....*....|..
gi 6321752 1475 LSQGERQLLFIARSLLREPKIILLDEATSSID 1506
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1473-1558 |
4.32e-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: 42.94 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1473 LNLSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIR--SEFNKSTILTIAHRLrSVIDY--DRIIVMDaG 1548
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrlSEEGKKTALVVEHDL-AVLDYlsDRIHVFE-G 147
|
90
....*....|
gi 6321752 1549 EVKEYDRPSE 1558
Cdd:cd03222 148 EPGVYGIASQ 157
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
791-890 |
4.34e-04 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 44.45 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 791 EILPAGDLTEIGEKGIT-LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncITGPLMKN-RTCILVTHNV 868
Cdd:PRK09536 122 RAMERTGVAQFADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLE--LVRRLVDDgKTAVAAIHDL 199
|
90 100
....*....|....*....|..
gi 6321752 869 SLTLRNAHFAIVLENGKVKNQG 890
Cdd:PRK09536 200 DLAARYCDELVLLADGRVRAAG 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1338-1506 |
4.45e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.40 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1338 PVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKiDLVTLrrsitiipQDPILFAGTiKSN 1417
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTY--------QKQLCFVGH-RSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1418 VDPYDEYDEKKIFKA-LSQVNLisshEFEEVLNSeerFNSTHnkFLNLHTeiaegGLnLSQGERQLLFIARSLLREPKII 1496
Cdd:PRK13540 85 INPYLTLRENCLYDIhFSPGAV----GITELCRL---FSLEH--LIDYPC-----GL-LSSGQKRQVALLRLWMSKAKLW 149
|
170
....*....|
gi 6321752 1497 LLDEATSSID 1506
Cdd:PRK13540 150 LLDEPLVALD 159
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1047-1241 |
4.52e-04 |
|
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: 44.04 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1047 LIGIIQAMLGGFKTMMTFLSGMRA------SRKIFNNL-LDLVLHAQ---IRFFDVTPVGRIMNRFSKDIEGVdQELIpy 1116
Cdd:cd18563 41 LLLLLVLGLAGAYVLSALLGILRGrllarlGERITADLrRDLYEHLQrlsLSFFDKRQTGSLMSRVTSDTDRL-QDFL-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1117 LEVTIFCLIQCASIIFLITV---ITPR-----FLTVAVIVFVLYFF---VGKWYLTASRELKRLDSitkspifqHFSETL 1185
Cdd:cd18563 118 SDGLPDFLTNILMIIGIGVVlfsLNWKlallvLIPVPLVVWGSYFFwkkIRRLFHRQWRRWSRLNS--------VLNDTL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 1186 VGVCTIRAFGDERRFIlenmNKIDQNNRAFFY--LSVTVKWFSFR-----VDMIGAFIVLASG 1241
Cdd:cd18563 190 PGIRVVKAFGQEKREI----KRFDEANQELLDanIRAEKLWATFFplltfLTSLGTLIVWYFG 248
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1320-1532 |
4.54e-04 |
|
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: 44.74 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1320 DGEIEIENLSLrYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTiitaLFRLLepiTGCIKIDGQDISKidlvTLRRS 1399
Cdd:TIGR00954 449 DNGIKFENIPL-VTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS----LFRIL---GELWPVYGGRLTK----PAKGK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1400 ITIIPQDPILFAGTIKSNVdPYDEYDEKKIFKALSQVNLISSHEFEEVLNSEERfnsthnkflnlhteiaEGGLN----- 1474
Cdd:TIGR00954 517 LFYVPQRPYMTLGTLRDQI-IYPDSSEDMKRRGLSDKDLEQILDNVQLTHILER----------------EGGWSavqdw 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321752 1475 ---LSQGERQLLFIARSLLREPKIILLDEATSSIDYDSDHLIQGIIRsEFNkSTILTIAHR 1532
Cdd:TIGR00954 580 mdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR-EFG-ITLFSVSHR 638
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
664-895 |
5.16e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 43.95 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENdSDMNAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGS-----IIVPSLEPKHDLI 738
Cdd:PRK13643 2 IKFEKVNYTYQPN-SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvgdIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 739 PDCEGLTNSFAYcsQSAWLLNDTVKNNIIF--DNFYNEDRYNKVIDAcglkRDLEILpaGDLTEIGEKG-ITLSGGQKQR 815
Cdd:PRK13643 81 PVRKKVGVVFQF--PESQLFEETVLKDVAFgpQNFGIPKEKAEKIAA----EKLEMV--GLADEFWEKSpFELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 816 ISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEnCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITEL 895
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
1028-1290 |
5.65e-04 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 43.61 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1028 MTD--SSKNKHNAFYY-LTVYFLIGIIQAML-----GGFKTMMTflsgmRASRKIFNNLLDLVLHAQIRFFDVTPVGRIM 1099
Cdd:cd18589 22 MTDwiMNKDAPEAFTAaITVMSLLTIASAVSefvcdLIYNITMS-----RIHSRLQGLVFAAVLRQEIAFFDSNQTGDIV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1100 NRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPRFLTVAV----IVFVLYFFVGKWYLTASRELKrlDSITKS 1175
Cdd:cd18589 97 SRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTAlglpLLLLVPKFVGKFQQSLAVQVQ--KSLARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1176 PifQHFSETLVGVCTIRAFGDE----RRFI--LENMNKIDQNNRAFFYLSVTVKWFSFRVDMIGafiVLASGSfILLNIA 1249
Cdd:cd18589 175 N--QVAVETFSAMKTVRSFANEegeaQRYRqrLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVG---ILYYGG-QLVTAG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 6321752 1250 NIDSGLAGISLTYAILFTDGALWLVRLYSTFEMNMNSVERL 1290
Cdd:cd18589 249 TVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
664-895 |
6.25e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 43.16 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENDSdmnafkLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLE---PKHD--LI 738
Cdd:PRK09493 2 IEFKNVSKHFGPTQV------LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvndPKVDerLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 739 PDCEGLT----NSFAYCsqsawllndTVKNNIIFDNFynEDRYNKVIDACGLKRDLeilpagdLTEIG--EKG----ITL 808
Cdd:PRK09493 76 RQEAGMVfqqfYLFPHL---------TALENVMFGPL--RVRGASKEEAEKQAREL-------LAKVGlaERAhhypSEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 809 SGGQKQRISLARAVYSSAKHVLLDDCLSAVD---SHTAVWIyencitgplMKN-----RTCILVTHNVSLTLRNAHFAIV 880
Cdd:PRK09493 138 SGGQQQRVAIARALAVKPKLMLFDEPTSALDpelRHEVLKV---------MQDlaeegMTMVIVTHEIGFAEKVASRLIF 208
|
250
....*....|....*
gi 6321752 881 LENGKVKNQGTITEL 895
Cdd:PRK09493 209 IDKGRIAEDGDPQVL 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
663-904 |
6.47e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 43.61 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 663 KIEFKNATLTWNENdSDMNAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVPSLEPKHDL----- 737
Cdd:PRK13646 2 TIRFDNVSYTYQKG-TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 738 --IPDCEGLTNSFAycsqSAWLLNDTVKNNIIF--DNF------YNEDRYNKVIDaCGLKRDLeilpagdlteIGEKGIT 807
Cdd:PRK13646 81 rpVRKRIGMVFQFP----ESQLFEDTVEREIIFgpKNFkmnldeVKNYAHRLLMD-LGFSRDV----------MSQSPFQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAhfaivlENGKVK 887
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYA------DEVIVM 219
|
250
....*....|....*...
gi 6321752 888 NQGTITELQS-KGLFKEK 904
Cdd:PRK13646 220 KEGSIVSQTSpKELFKDK 237
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
800-868 |
7.53e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 43.33 E-value: 7.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 800 EIGEkgitLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncITGPLM-KNRTCILVTHNV 868
Cdd:PRK15056 139 QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIIS--LLRELRdEGKTMLVSTHNL 202
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1044-1245 |
8.27e-04 |
|
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: 43.35 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1044 VYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSkDIEGVDQELIPYLEVTIFC 1123
Cdd:cd18782 47 VMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1124 LIQCASIIFLITVITPRfLTVAV-----IVFVLYFFVGKWYLTASRELKRLDSITKSpifqHFSETLVGVCTIRAFGDER 1198
Cdd:cd18782 126 VLFSVIYIAVLFSYSPL-LTLVVlatvpLQLLLTFLFGPILRRQIRRRAEASAKTQS----YLVESLTGIQTVKAQNAEL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6321752 1199 RFILENMNKIDQNNRAFFYLSVTVKWFSFrvdmIGAFIVLASGSFIL 1245
Cdd:cd18782 201 KARWRWQNRYARSLGEGFKLTVLGTTSGS----LSQFLNKLSSLLVL 243
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
1031-1197 |
8.74e-04 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 43.10 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1031 SSKNKHNAFYYLTVY-FLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGV 1109
Cdd:cd18590 27 GGEYQHNAFTSAIGLmCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1110 DQELIPYLEVTIFCLIQCASIIFLITVITPRFLTVAVIVFVLYFFVGKWYLTASRELKR--LDSITKSPifQHFSETLVG 1187
Cdd:cd18590 107 SRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQavQDSIAKAG--ELAREAVSS 184
|
170
....*....|
gi 6321752 1188 VCTIRAFGDE 1197
Cdd:cd18590 185 IRTVRSFKAE 194
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
791-895 |
9.37e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.48 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 791 EILPAGDLTEIGEKgiTLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENcITgPLMK--NRTCILVTHNV 868
Cdd:PRK11000 119 EVLQLAHLLDRKPK--ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIE-IS-RLHKrlGRTMIYVTHDQ 194
|
90 100
....*....|....*....|....*....
gi 6321752 869 --SLTLrnAHFAIVLENGKVKNQGTITEL 895
Cdd:PRK11000 195 veAMTL--ADKIVVLDAGRVAQVGKPLEL 221
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1353-1394 |
9.48e-04 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 43.22 E-value: 9.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6321752 1353 IGIVGRTGAGKSTIITALFrllepitgcikidGQDISKIDLV 1394
Cdd:COG3596 42 IALVGKTGAGKSSLINALF-------------GAEVAEVGVG 70
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
689-899 |
9.49e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 43.08 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 689 NIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSI------IVPSLEPKhDLIPDCE--GLTNSFAycsqSAWLLND 760
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervITAGKKNK-KLKPLRKkvGIVFQFP----EHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 761 TVKNNIIFD--NF-----YNEDRYNKVIDACGLKRDLeilpagdlteIGEKGITLSGGQKQRISLArAVYSSAKHVL-LD 832
Cdd:PRK13634 102 TVEKDICFGpmNFgvseeDAKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRVAIA-GVLAMEPEVLvLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 833 DCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITELQSKG 899
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
788-842 |
9.53e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 42.76 E-value: 9.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6321752 788 RDLEILPAGDLTEIGEKGI-TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHT 842
Cdd:PRK11248 108 IAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1038-1267 |
1.10e-03 |
|
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: 42.78 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1038 AFYYLTVYFLIGIIQamlggfKTMMTflsgMRasRKIFNNLLDLvlhaQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYL 1117
Cdd:cd18547 60 LFSYLQNRLMARVSQ------RTVYD----LR--KDLFEKLQRL----PLSYFDTHSHGDIMSRVTNDVDNISQALSQSL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1118 EVTIFCLIQCASIIFLITVITPRfLTVAVIVFV-LYFFVGKWYLTASREL--KRLDSITKspIFQHFSETLVGVCTIRAF 1194
Cdd:cd18547 124 TQLISSILTIVGTLIMMLYISPL-LTLIVLVTVpLSLLVTKFIAKRSQKYfrKQQKALGE--LNGYIEEMISGQKVVKAF 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321752 1195 GDERRFIlENMNKIDQNN-----RAFFYLSVTVKWFSFrVDMIG-AFIVLASGSFILLNIANIdsGLAGISLTYAILFT 1267
Cdd:cd18547 201 NREEEAI-EEFDEINEELykasfKAQFYSGLLMPIMNF-INNLGyVLVAVVGGLLVINGALTV--GVIQAFLQYSRQFS 275
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1323-1382 |
1.10e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 1.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNlpPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIK 1382
Cdd:PRK15064 320 LEVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
808-906 |
1.14e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 42.59 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITgpLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVK 887
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLE--LKKDMTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
90 100
....*....|....*....|.
gi 6321752 888 NQGTITEL--QSKGLFKEKYV 906
Cdd:PRK14247 225 EWGPTREVftNPRHELTEKYV 245
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
787-842 |
1.18e-03 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 42.54 E-value: 1.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 787 KRDLEILPAGDLTEIGEKGI-TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHT 842
Cdd:COG4525 113 ARAEELLALVGLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALT 169
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1037-1237 |
1.33e-03 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 42.79 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1037 NAFYYLTVYFLIGIiqamlgGFKTMMTflsgMRasRKIFNNLLDLvlhaQIRFFDVTPVGRIMNRFSKDIEGVDQELIPY 1116
Cdd:cd18552 53 GLASYLQTYLMAYV------GQRVVRD----LR--NDLFDKLLRL----PLSFFDRNSSGDLISRITNDVNQVQNALTSA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1117 LEV------TIFCLIqcaSIIFLI----TVITprFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITkspifQHFSETLV 1186
Cdd:cd18552 117 LTVlvrdplTVIGLL---GVLFYLdwklTLIA--LVVLPLAALPIRRIGKRLRKISRRSQESMGDLT-----SVLQETLS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6321752 1187 GVCTIRAFGDE----RRFILENMNKIDQNNRAFFYLSVTvkwfSFRVDMIGAFIV 1237
Cdd:cd18552 187 GIRVVKAFGAEdyeiKRFRKANERLRRLSMKIARARALS----SPLMELLGAIAI 237
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
808-904 |
1.40e-03 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 42.90 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENcITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKvk 887
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWER-LRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR-- 249
|
90
....*....|....*..
gi 6321752 888 nqgTITELQSKGLFKEK 904
Cdd:PRK13536 250 ---KIAEGRPHALIDEH 263
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1323-1554 |
1.40e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1323 IEIENLSLRYAPNLppVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIkidgqdiskidlvTLRRSITI 1402
Cdd:PRK10636 313 LKMEKVSAGYGDRI--ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKGIKL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1403 ipqdpilfaGTIKSNVDPYDEYDEkkifKALSQVNLISSHEFEEVLNSE-ERFNSTHNKFlnlhTEIAEgglNLSQGERQ 1481
Cdd:PRK10636 378 ---------GYFAQHQLEFLRADE----SPLQHLARLAPQELEQKLRDYlGGFGFQGDKV----TEETR---RFSGGEKA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 1482 LLFIARSLLREPKIILLDEATSSIDYDSDH-LIQGIIRSEFNKSTILTIAHRLRSVIDyDRIIVMDaGEVKEYD 1554
Cdd:PRK10636 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQaLTEALIDFEGALVVVSHDRHLLRSTTD-DLYLVHD-GKVEPFD 509
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1047-1197 |
1.49e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 42.30 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1047 LIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIpyLEVTIFC--L 1124
Cdd:cd18784 44 LLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVS--LNLNIFLrsL 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 1125 IQCASIIFLITVITPRFLTVAVIVFVLYFFV----GKWYLTASRELKrlDSITKSPifQHFSETLVGVCTIRAFGDE 1197
Cdd:cd18784 122 VKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVskvyGDYYKKLSKAVQ--DSLAKAN--EVAEETISSIRTVRSFANE 194
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
808-886 |
1.55e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 42.38 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncITGPLMK--NRTCILVTHNVSLTLRNAHFAIVLENGK 885
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE--LTEKIVEenNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
.
gi 6321752 886 V 886
Cdd:COG1101 227 I 227
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1017-1213 |
1.57e-03 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 42.40 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1017 GFAMDTLPLKGMTDSSknkhnAFYYLTVYFLIGIIQAmLGGFKTMMTFlsgMRASRKIFNNL-LDLVLHAQ---IRFFDV 1092
Cdd:cd18541 23 GRAIDALTAGTLTASQ-----LLRYALLILLLALLIG-IFRFLWRYLI---FGASRRIEYDLrNDLFAHLLtlsPSFYQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1093 TPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPRfLTVAV-----IVFVLYFFVGKWYLTASRElk 1167
Cdd:cd18541 94 NRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPK-LTLIAllplpLLALLVYRLGKKIHKRFRK-- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 1168 rldsitkspIFQHFS-------ETLVGVCTIRAFGDE----RRFILENMNKIDQNNR 1213
Cdd:cd18541 171 ---------VQEAFSdlsdrvqESFSGIRVIKAFVQEeaeiERFDKLNEEYVEKNLR 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
808-886 |
1.57e-03 |
|
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: 42.04 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLM--KNR----TCILVTHNVSLTLRnAHFAIVL 881
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIID------LLfeLNRergtTLVLVTHDPALAAR-CDRVLRL 219
|
....*
gi 6321752 882 ENGKV 886
Cdd:COG4181 220 RAGRL 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1330-1392 |
1.58e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 41.76 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 1330 LRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKIDGQDISKID 1392
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD 79
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
608-833 |
1.67e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.04 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 608 TTLSLFTL-LKTPLDQLSNMLSFINQSKVSLKRISDFLRMDDTEKYNQLTISPDKNKIEFKNATLTWNENdsdmnAFKLC 686
Cdd:PRK10522 266 ATYSLTLLfLRTPLLSAVGALPTLLSAQVAFNKLNKLALAPYKAEFPRPQAFPDWQTLELRNVTFAYQDN-----GFSVG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 687 GLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSIIVpslepkhdlipDCEGLT--NSFAYCSQ-SAwllndtvk 763
Cdd:PRK10522 341 PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-----------DGKPVTaeQPEDYRKLfSA-------- 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321752 764 nniIFDNFYNEDRY----NKVIDACGLKRDLEILPAGDLTEIGEKGIT---LSGGQKQRISLARAVYSSAKHVLLDD 833
Cdd:PRK10522 402 ---VFTDFHLFDQLlgpeGKPANPALVEKWLERLKMAHKLELEDGRISnlkLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
781-897 |
1.71e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.06 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 781 IDACGLKRDLEILPAgdlteigekgiTLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTavwiyenciTGPLMK--- 857
Cdd:PRK11831 128 LEAVGLRGAAKLMPS-----------ELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT---------MGVLVKlis 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 6321752 858 --NR----TCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITELQS 897
Cdd:PRK11831 188 elNSalgvTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
337-585 |
1.79e-03 |
|
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: 42.07 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 337 YLLIGMLWVLVNSIVNLLPTILMKRfleIVDN--PNRssscmNLAWLYIIGMFIcrLTLAICNSqgqfvsdkICLRIRAI 414
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKI---AIDEyiPNG-----DLSGLLIIALLF--LALNLVNW--------VASRLRIY 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 415 LIGEI---YAKGLRRRLFTSPKTSS------------------DSDSISANL-GTIINLISiDSFkvselanylyvtvqa 472
Cdd:cd18545 63 LMAKVgqrILYDLRQDLFSHLQKLSfsffdsrpvgkilsrvinDVNSLSDLLsNGLINLIP-DLL--------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 473 VIMIIVVVGLLFNF-LGVSAFAGIsiilvmfPLNFLLANLLGKFQKQTLKCTDQRISKLN----ECLQNIRIVKYFAWER 547
Cdd:cd18545 127 TLVGIVIIMFSLNVrLALVTLAVL-------PLLVLVVFLLRRRARKAWQRVRKKISNLNaylhESISGIRVIQSFARED 199
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6321752 548 NIINEIKSIRQKELRSLLK----KSLVWSVTSFLWFVTPTLV 585
Cdd:cd18545 200 ENEEIFDELNRENRKANMRavrlNALFWPLVELISALGTALV 241
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1354-1568 |
1.92e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.38 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1354 GIVGRTGAGKSTIITALFRLLEPIT-----GCIKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNVDPYDEYDEKK 1428
Cdd:pfam13304 3 VLIGPNGSGKSNLLEALRFLADFDAlviglTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLERED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1429 IFKALSQVNLISSHEFEEVLNSEERFNSTHNKFLNLH---TEIAEGGLNLSQGERQLLFIARSLLREPKIILLDEATSSi 1505
Cdd:pfam13304 83 VEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRlglDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGL- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321752 1506 dYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELLKDERGIFY 1568
Cdd:pfam13304 162 -LLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLIL 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
808-891 |
1.98e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 41.92 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEnciTGPLMKNR---TCILVTHNVSLTLRnAHFAIVLENG 884
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLE---TVRQLKEQkgiTVLSITHDLDEAAQ-ADRVIVMNKG 216
|
....*..
gi 6321752 885 KVKNQGT 891
Cdd:PRK13635 217 EILEEGT 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1307-1555 |
2.02e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 42.71 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1307 GR-ILLLNEPSWPKDGEI--EIENLSLRYAPNLPPViRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGCIKI 1383
Cdd:COG3845 239 GReVLLRVEKAPAEPGEVvlEVENLSVRDDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1384 DGQDISKIDLVTLRRS-ITIIPQDPI---LFAG-TIKSNV--DPYDEydekkifKALSQVNLISSHEFEEvlNSE---ER 1453
Cdd:COG3845 318 DGEDITGLSPRERRRLgVAYIPEDRLgrgLVPDmSVAENLilGRYRR-------PPFSRGGFLDRKAIRA--FAEeliEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1454 FN-STHnkflNLHTEIAegglNLSQGERQLLFIARSLLREPKIILLDEAT-----SSIDYdsdhlIQGIIRSEFNK---- 1523
Cdd:COG3845 389 FDvRTP----GPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTrgldvGAIEF-----IHQRLLELRDAgaav 455
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6321752 1524 ---ST----ILTIAhrlrsvidyDRIIVMDAGE-VKEYDR 1555
Cdd:COG3845 456 lliSEdldeILALS---------DRIAVMYEGRiVGEVPA 486
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
807-839 |
2.12e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 41.75 E-value: 2.12e-03
10 20 30
....*....|....*....|....*....|...
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVD 839
Cdd:COG4167 149 MLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1029-1263 |
2.17e-03 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 41.85 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1029 TDSSKNKHNAFYYLTVYFLIGIIQAMLGGFktmMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDiEG 1108
Cdd:cd18780 35 EEALRALNQAVLILLGVVLIGSIATFLRSW---LFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSD-TQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1109 VDQ--------ELIPYLEVTIFcliqcaSIIFLITvITPRFLTVAVIVFVLYFFVGKWYLTASRELKRL--DSITKSPIF 1178
Cdd:cd18780 111 VLQnavtvnlsMLLRYLVQIIG------GLVFMFT-TSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKfqDALAAASTV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1179 QhfSETLVGVCTIRAFGDERRFILENMNKIDQNNRAFFYLSVTVKWFSFRVDMI--GAFI-VLASG-------------- 1241
Cdd:cd18780 184 A--EESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAaqLAIVlVLWYGgrlvidgelttgll 261
|
250 260
....*....|....*....|...
gi 6321752 1242 -SFILLNIaNIDSGLAGISLTYA 1263
Cdd:cd18780 262 tSFLLYTL-TVAMSFAFLSSLYG 283
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
808-901 |
2.50e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 42.01 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVK 887
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
90
....*....|....*.
gi 6321752 888 NQGTITEL--QSKGLF 901
Cdd:PRK11432 217 QIGSPQELyrQPASRF 232
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1037-1238 |
2.61e-03 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 41.65 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1037 NAFYYLTVYFLIG--IIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDI----EGVD 1110
Cdd:cd18551 32 GGSSGGLLALLVAlfLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTtllrELIT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1111 QELIPYLeVTIFCLIqcASIIFLI------TVITprFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITkspifQHFSET 1184
Cdd:cd18551 112 SGLPQLV-TGVLTVV--GAVVLMFlldwvlTLVT--LAVVPLAFLIILPLGRRIRKASKRAQDALGELS-----AALERA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1185 LVGVCTIRAFGDERRFIlenmNKIDQNNRAFFYLSV-TVKWFSF-----RVDMIGAFIVL 1238
Cdd:cd18551 182 LSAIRTVKASNAEERET----KRGGEAAERLYRAGLkAAKIEALigplmGLAVQLALLVV 237
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
808-839 |
2.63e-03 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 41.98 E-value: 2.63e-03
10 20 30
....*....|....*....|....*....|..
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVD 839
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
808-906 |
2.86e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.37 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVK 887
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEE--LLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
90 100
....*....|....*....|.
gi 6321752 888 NQGTITEL--QSKGLFKEKYV 906
Cdd:PRK14267 228 EVGPTRKVfeNPEHELTEKYV 248
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
808-891 |
3.34e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 41.61 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAV----WIYEncitgpLMKNR--TCILVTHNVSLTLRNAHFAIVL 881
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKelrrWLRQ------LHEELkfTSVFVTHDQEEAMEVADRVVVM 210
|
90
....*....|
gi 6321752 882 ENGKVKNQGT 891
Cdd:PRK10851 211 SQGNIEQAGT 220
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
338-640 |
3.38e-03 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 41.24 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 338 LLIGMLWVLVNSIVNLLPTILMKRFLEIVDNPNRSsscMNLAWLYIIGMFIcrltLAICNSQGQFVSdkiclriRAILIG 417
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLT---ASQLLRYALLILL----LALLIGIFRFLW-------RYLIFG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 418 EIY--AKGLRRRLFT-----SP----KTSSdsdsisanlGTIINLISIDSFKVSELANY-LYVTVQAVIMIIVVVGLLFN 485
Cdd:cd18541 67 ASRriEYDLRNDLFAhlltlSPsfyqKNRT---------GDLMARATNDLNAVRMALGPgILYLVDALFLGVLVLVMMFT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 486 flgvsafagIS-----IILVMFPLNFLLANLLGKF-QKQTLKCTDQrISKLNECLQ----NIRIVKYFAWERNIINEIks 555
Cdd:cd18541 138 ---------ISpkltlIALLPLPLLALLVYRLGKKiHKRFRKVQEA-FSDLSDRVQesfsGIRVIKAFVQEEAEIERF-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 556 irQKELRSLLKKSLVWSVTSFLWFVTPTLVTGVTFAIC-----TFVQHEDLNAP--LAFTtlSLFTLLKTPLDQLSNMLS 628
Cdd:cd18541 206 --DKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVlwyggRLVIRGTITLGdlVAFN--SYLGMLIWPMMALGWVIN 281
|
330
....*....|..
gi 6321752 629 FINQSKVSLKRI 640
Cdd:cd18541 282 LIQRGAASLKRI 293
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
808-907 |
3.42e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 41.23 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncITGPLMKN-RTCILVTHNVSLTLRNAHFAIVLENGK- 885
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQgKTIILVTHDLDNVLEWTKRTIFFKDGKi 243
|
90 100
....*....|....*....|..
gi 6321752 886 VKNQGTITELQSKGLFKEKYVQ 907
Cdd:PRK13651 244 IKDGDTYDILSDNKFLIENNME 265
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
338-640 |
3.95e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 41.23 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 338 LLIGMLWVLVNSIVNL-LPTILMKrfleIVDNPNRSSScMNLAWLYIIGMFICRLTLAICNSQGQFVSDKICLRiraili 416
Cdd:cd18548 1 AILAPLFKLLEVLLELlLPTLMAD----IIDEGIANGD-LSYILRTGLLMLLLALLGLIAGILAGYFAAKASQG------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 417 geiYAKGLRRRLFTspKTSSDS----DSISAnlGTIINLISIDSFKVSELANYLYVT-VQAVIMIIVVVGLLFN------ 485
Cdd:cd18548 70 ---FGRDLRKDLFE--KIQSFSfaeiDKFGT--SSLITRLTNDVTQVQNFVMMLLRMlVRAPIMLIGAIIMAFRinpkla 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 486 --FLGVSAFAGISIILVMFplnfLLANLLGKFQKQTlkctDQRISKLNECLQNIRIVKYFAWERNiinEIKSIRQ--KEL 561
Cdd:cd18548 143 liLLVAIPILALVVFLIMK----KAIPLFKKVQKKL----DRLNRVVRENLTGIRVIRAFNREDY---EEERFDKanDDL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 562 RSLLKKslVWSVTSFLWFVTPTLVTGVTFAICTFVQHE---------DLNAPLAFTTLSLFTLLKtpldqLSNMLSFINQ 632
Cdd:cd18548 212 TDTSLK--AGRLMALLNPLMMLIMNLAIVAILWFGGHLinagslqvgDLVAFINYLMQILMSLMM-----LSMVFVMLPR 284
|
....*...
gi 6321752 633 SKVSLKRI 640
Cdd:cd18548 285 ASASAKRI 292
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
807-886 |
4.43e-03 |
|
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: 40.21 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMKN-----RTCILVTHNVSLTLRNAHFAIVL 881
Cdd:cd03262 135 QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLD------VMKDlaeegMTMVVVTHEMGFAREVADRVIFM 208
|
....*
gi 6321752 882 ENGKV 886
Cdd:cd03262 209 DDGRI 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
787-873 |
4.81e-03 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 40.57 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 787 KRDLEILPAGDLTEIGE-KGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncITGPL-MKNRTCIL- 863
Cdd:PRK11629 124 SRALEMLAAVGLEHRANhRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ--LLGELnRLQGTAFLv 201
|
90
....*....|
gi 6321752 864 VTHNVSLTLR 873
Cdd:PRK11629 202 VTHDLQLAKR 211
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1027-1201 |
5.07e-03 |
|
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: 40.92 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1027 GMTDSSKNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMNRFSKDI 1106
Cdd:cd18577 35 GESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1107 EGVdQELI-PYLEVTIFCLIQC-ASIIF------LITVITprfLTVAVIVFVLYFFVGKwyLTASRELKRLDSITKSPif 1178
Cdd:cd18577 115 NLI-QDGIgEKLGLLIQSLSTFiAGFIIafiyswKLTLVL---LATLPLIAIVGGIMGK--LLSKYTKKEQEAYAKAG-- 186
|
170 180
....*....|....*....|...
gi 6321752 1179 QHFSETLVGVCTIRAFGDERRFI 1201
Cdd:cd18577 187 SIAEEALSSIRTVKAFGGEEKEI 209
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
785-886 |
5.95e-03 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 40.21 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 785 GLKRDL------EILpagDLTEIGE------KgiTLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAvwiyENC-- 850
Cdd:cd03220 113 GLSRKEidekidEII---EFSELGDfidlpvK--TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ----EKCqr 183
|
90 100 110
....*....|....*....|....*....|....*..
gi 6321752 851 -ITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKV 886
Cdd:cd03220 184 rLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1021-1247 |
6.52e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). 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. 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: 349998 [Multi-domain] Cd Length: 299 Bit Score: 40.48 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1021 DTLPLKGMTDSSKNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLDLVLHAQIRFFDVTPVGRIMN 1100
Cdd:cd18554 28 DVIQGSSLTLDEKVYKLFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 1101 RFSKDIEGVDQELIPYLevtIFCLIQCASIIFLITVI---TPRFLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPI 1177
Cdd:cd18554 108 RVINDVEQTKDFITTGL---MNIWLDMITIIIAICIMlvlNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321752 1178 FQHFSETLVGVCTIRAFGDERRfILENMNKIDQN--NRAFFYLSVTVKWFSF--RVDMIGAFIVLASGSFILLN 1247
Cdd:cd18554 185 QGFLHERIQGMSVIKSFALEKH-EQKQFDKRNGHflTRALKHTRWNAKTFSAvnTITDLAPLLVIGFAAYLVIE 257
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
664-886 |
6.58e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 40.58 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 664 IEFKNATLTWNENdSDMNAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELNLISGSI------IVPSLEPKH-D 736
Cdd:PRK13641 3 IKFENVDYIYSPG-TPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhITPETGNKNlK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 737 LIPDCEGLTNSFAycsqSAWLLNDTVKNNIIFD--NF-YNEDRYN----KVIDACGLKRDLeilpagdlteIGEKGITLS 809
Cdd:PRK13641 82 KLRKKVSLVFQFP----EAQLFENTVLKDVEFGpkNFgFSEDEAKekalKWLKKVGLSEDL----------ISKSPFELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 810 GGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYEncitgpLMKN-----RTCILVTHNVSLTLRNAHFAIVLENG 884
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ------LFKDyqkagHTVILVTHNMDDVAEYADDVLVLEHG 221
|
..
gi 6321752 885 KV 886
Cdd:PRK13641 222 KL 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
808-895 |
7.68e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 40.17 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVK 887
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
....*...
gi 6321752 888 NQGTITEL 895
Cdd:PRK13652 218 AYGTVEEI 225
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
807-866 |
7.89e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 7.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPlmknRTCILVTH 866
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP----KTFIVVSH 399
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
807-895 |
7.90e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.16 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 807 TLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKV 886
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
....*....
gi 6321752 887 KNQGTITEL 895
Cdd:PRK10575 227 IAQGTPAEL 235
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
808-895 |
9.29e-03 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 40.17 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321752 808 LSGGQKQRISLARAVYSSAKHVLLDDCLSAVDSHTAVWIYENcITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVK 887
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWER-LRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
....*...
gi 6321752 888 NQGTITEL 895
Cdd:PRK13537 218 AEGAPHAL 225
|
|
| |
