|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-1533 |
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: 1605.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 7 STFWDLSL-LESPEADLPLCFEQTVLVWIPLGFLWLLAPwqLYSVYRSRTKRSSITKFYLAK--QVFVVFLLILAAIDLS 83
Cdd:TIGR00957 7 DPLWDWNVtWHTSNPDFTKCFQNTVLAWVPCFYLWVCFP--CYFLYLSRHDRGYIQMTHLNKtkTALGFLLWIVCWADLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 84 LALTEDTGQATVPPVRYTNPILYLCTWLL-VLAVQHSRQWCVrKNSWFLSLFWILSVLCGVFQFQT-LIRALLKDSKSNM 161
Cdd:TIGR00957 85 YSFWERSHGRAPAPVFLVSPTLLGITMLLaTFLIQLERRKGV-QSSGIMLTFWLVALVCALAILRSkILLALKEDAIVDP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 162 AYSYLFFVSYGFQIVLLILTAFSGPS--------DSTQTPSVTASFLSSITFSWYDRTVLKGYKHPLTLEDVWDIDEGFK 233
Cdd:TIGR00957 164 FRDTTFYIYFALVLSQLVLSCFSDKSplfsetnhDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 234 TRSVTSKFEAAMTKDLQKARQAfQRRLQKSQRKPEATLHGLNKKQSQSQDVLVLEEAKKKSEKTtkdypkswLIKSLFKT 313
Cdd:TIGR00957 244 SEMVVPVLVENWKKECKKTRKQ-PVSAVYGKKDPSKPKGSSQLDANEEVEALIVKSPHKPRKPS--------LFKVLYKT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 314 FHVVILKSFILKLIHDLLVFLNPQLLKLLIGFVKSSNSYVWFGYICAILMFAVTLIQSFCLQSYFQHCFVLGMCVRTTVM 393
Cdd:TIGR00957 315 FGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 394 SSIYKKALTLSNLARKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILAGVGVMVLLIPVN 473
Cdd:TIGR00957 395 GAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 474 GVLATKIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQITPILV 553
Cdd:TIGR00957 475 AVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLV 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 554 SVVTFSVYVLVDSANVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRLERYLGGDDLDTSAIRRVSNFD--- 630
Cdd:TIGR00957 555 ALITFAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPgeg 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 631 KAVKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSWIQNGT 710
Cdd:TIGR00957 635 NSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDS 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 711 IKDNILFGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAH 790
Cdd:TIGR00957 715 LRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 791 VGKHIFNKVVGPNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFARNWKTFmkhsgpegeATV 870
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTY---------APD 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 871 NNDSEAEDDDDGLI--PTMEEIP-EDAASLAMRRENSLRRTLSRSSRSSSRRGKSLKNSLKiknvnvLKEKEKEVEGQKL 947
Cdd:TIGR00957 866 EQQGHLEDSWTALVsgEGKEAKLiENGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSAE------LQKAEAKEETWKL 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 948 IKKEFVETGKVKFSIYLKYLQAVGWWSILFIILFYGLNNVAFIGSNLWLSAWTSDSdNLNGTNNsssHRDMRIGVFGALG 1027
Cdd:TIGR00957 940 MEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDP-MVNGTQN---NTSLRLSVYGALG 1015
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1028 LAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAG 1107
Cdd:TIGR00957 1016 ILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIG 1095
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1108 TLVMICMATPVFAIIIIPLSILYISVQVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQID 1187
Cdd:TIGR00957 1096 ALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVD 1175
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1188 INQKCVFSWITSNRWLAIRLELVGNLVVFCSALLLVIYRKTLTGDVVGFVLSNALNITQTLNWLVRMTSEAETNIVAVER 1267
Cdd:TIGR00957 1176 ENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVER 1255
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1268 ISEYINVENEAPW-VTDKRPPADWPRHGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRI 1346
Cdd:TIGR00957 1256 LKEYSETEKEAPWqIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRI 1335
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1347 LESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNLDPFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEV 1426
Cdd:TIGR00957 1336 NESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEC 1415
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1427 TEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNG 1506
Cdd:TIGR00957 1416 AEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKG 1495
|
1530 1540
....*....|....*....|....*..
gi 3219824 1507 KIVEYGSPEELLSNRGSFYLMAKEAGI 1533
Cdd:TIGR00957 1496 EVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-1535 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 1076.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 24 LCFEQTVLVWIPLGFLWLLapwqlysvyrsrTKRSSITKFYLAKQVFVVFLLILAA---------IDLSLALTEDTGQAT 94
Cdd:PLN03130 39 INISHLVLLGLCLYRIWLI------------KKDHKVQRFCLRSKWYNYFLALLAAyctaeplfrLVMGISVLNLDGQTS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 95 VPPVRYTNPILYLCTW--LLVLAVQHSRQWcVRKNSWFLSlFWILSVLCGVFQFQTLIRALlKDSKSNMAYsYLFFVSYG 172
Cdd:PLN03130 107 LPPFEIVSLIVEALTWcsMLVMIGVETKIY-IREFRWYVR-FAVIYVLVGDAVMLNLVLSV-KEYYSSFVL-YLYISEVA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 173 FQIVLLILTAFSGP------------SDSTQT-------------PSVTASFLSSITFSWYDRTVLKGYKHPLTLEDVWD 227
Cdd:PLN03130 183 AQVLFGILLLVYFPnldpypgytpigSESVDDyeyeelpggeqicPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 228 IDEGFKTRSVTSKFEAAMTKDLQKarqafqrrlqksqrkpeatlhglnkkqsqsqdvlvleeakkksekttkdyPKSWLI 307
Cdd:PLN03130 263 LDTWDQTETLYRSFQKCWDEELKK--------------------------------------------------PKPWLL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 308 KSLFKTFHVVILKSFILKLIHDLLVFLNPQLLKLLIGFVKSSNSyVWFGYICAILMFAVTLIQSFCLQSYFQHCFVLGMC 387
Cdd:PLN03130 293 RALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGEP-AWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 388 VRTTVMSSIYKKALTLSNLARKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILAGVGVMV 467
Cdd:PLN03130 372 LRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 468 LLIPVNGVLATKIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELkNLLRFGQLQSLL-IFIL 546
Cdd:PLN03130 452 LMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDEL-SWFRKAQLLSAFnSFIL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 547 QITPILVSVVTFSVYVLVdsANVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRLERYLGGDDLDTSAIRRV 626
Cdd:PLN03130 531 NSIPVLVTVVSFGVFTLL--GGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 627 SNFDKAVKFSEASFTWDPDLE-ATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENV-HGHITIQGSTAYVPQQS 704
Cdd:PLN03130 609 EPGLPAISIKNGYFSWDSKAErPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRsDASVVIRGTVAYVPQVS 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 705 WIQNGTIKDNILFGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPL 784
Cdd:PLN03130 689 WIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 785 SAVDAHVGKHIFNKVVgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFarnwKTFMKHSGp 864
Cdd:PLN03130 769 SALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLF----QKLMENAG- 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 865 EGEATVNNDSEAEDDDDGLIPTMEEIPedaaslamrrenslrrtlsrssrsssrrgkslkNSLKIKNVNVLKEKEKEveg 944
Cdd:PLN03130 842 KMEEYVEENGEEEDDQTSSKPVANGNA---------------------------------NNLKKDSSSKKKSKEGK--- 885
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 945 QKLIKKEFVETGKVKFSIYLKYLQAVG-WWSILFIILFYGLNNVAFIGSNLWLSAWTSDSdnlngtnNSSSHRDM-RIGV 1022
Cdd:PLN03130 886 SVLIKQEERETGVVSWKVLERYKNALGgAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQG-------TPKTHGPLfYNLI 958
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1023 FGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCF 1102
Cdd:PLN03130 959 YALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQI 1038
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1103 FGIAGTLVMICMATPVFAIIIIPLSILYISVQVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWN 1182
Cdd:PLN03130 1039 FQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEIN 1118
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1183 EKQIDINQKCVFSWITSNRWLAIRLELVGNLVVFCSALLLVIYRKTLTGDV-----VGFVLSNALNITQTLNWLVRMTSE 1257
Cdd:PLN03130 1119 GRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAENQAafastMGLLLSYALNITSLLTAVLRLASL 1198
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1258 AETNIVAVERISEYINVENEAPWVT-DKRPPADWPRHGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGK 1336
Cdd:PLN03130 1199 AENSLNAVERVGTYIDLPSEAPLVIeNNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGK 1278
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1337 SSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNLDPFNKYSDEEVWRALELAHLRSFVS 1416
Cdd:PLN03130 1279 SSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIR 1358
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1417 GLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMD 1496
Cdd:PLN03130 1359 RNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIID 1438
|
1530 1540 1550 1560
....*....|....*....|....*....|....*....|
gi 3219824 1497 SDKIMVLDNGKIVEYGSPEELLSNRGS-FYLMAKEAGIEN 1535
Cdd:PLN03130 1439 CDRILVLDAGRVVEFDTPENLLSNEGSaFSKMVQSTGAAN 1478
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-1538 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 1006.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 22 LPLCFEQTVLVWIPLGFLWLLAPWQLYSVYRSRTKRSSITKFYLAKQVFVVFLLILAaidLSLALTEDTGQATVPPVRYT 101
Cdd:PLN03232 37 LVMIVSHSVLLGLCFYRIWIILDNAKAQIYVLRKKYYNCVLGILACYCVVEPVLRLV---MGISLFDMDEETDLPPFEVA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 102 NPILYLCTW--LLVLAVQHSRQWcVRKNSWFLSlFWILSVLCGVFQFQTLIRALlKDSKSNMAYsYLFFVSYG----FQI 175
Cdd:PLN03232 114 SLMVEAFAWfsMLVLIGLETKQY-VKEFRWYVR-FGVVYVLVADAVLLDLVLPL-KNSINRTAL-YLCISSRCcqalFGI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 176 VLLI----LTAFSG-------PSDSTQ----------TPSVTASFLSSITFSWYDRTVLKGYKHPLTLEDVWDIDEGFKT 234
Cdd:PLN03232 190 LLLVyipeLDPYPGyhilnneSLDNVEydalrggeniCPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 235 RSVTSKFEAAMTkdlqkarqafqrrlQKSQRkpeatlhglnkkqsqsqdvlvleeakkksekttkdyPKSWLIKSLFKTF 314
Cdd:PLN03232 270 ETLIKRFQRCWT--------------EESRR------------------------------------PKPWLLRALNNSL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 315 HVVILKSFILKLIHDLLVFLNPQLLKLLIGFVKSSNSyVWFGYICAILMFAVTLIQSFCLQSYFQHCFVLGMCVRTTVMS 394
Cdd:PLN03232 300 GGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDP-AWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 395 SIYKKALTLSNLARKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILAGVGVMVLLIPVNG 474
Cdd:PLN03232 379 AIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQT 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 475 VLATKIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELkNLLRFGQLQSLL-IFILQITPILV 553
Cdd:PLN03232 459 LIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEEL-SWFRKAQLLSAFnSFILNSIPVVV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 554 SVVTFSVYVLVDSAnvLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRLERYLGGDDLDTSAIRRVSNFDKAV 633
Cdd:PLN03232 538 TLVSFGVFVLLGGD--LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAPAI 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 634 KFSEASFTWDPDLE-ATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVH-GHITIQGSTAYVPQQSWIQNGTI 711
Cdd:PLN03232 616 SIKNGYFSWDSKTSkPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATV 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 712 KDNILFGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHV 791
Cdd:PLN03232 696 RENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 792 GKHIFNKVVGPNglLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFarnwKTFMKHSGpEGEATVn 871
Cdd:PLN03232 776 AHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLF----KKLMENAG-KMDATQ- 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 872 NDSEAEDDDDGLIPTME-EIPEDAASLAMRREnslrrtlsrssrsssrRGKSLknslkiknvnvlkekekevegqkLIKK 950
Cdd:PLN03232 848 EVNTNDENILKLGPTVTiDVSERNLGSTKQGK----------------RGRSV-----------------------LVKQ 888
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 951 EFVETGKVKFSIYLKYLQAV-GWWSILFIILFYGLNNVAFIGSNLWLSAWTSDSdnlngtnNSSSHR-DMRIGVFGALGL 1028
Cdd:PLN03232 889 EERETGIISWNVLMRYNKAVgGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQS-------TPKSYSpGFYIVVYALLGF 961
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1029 AQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGT 1108
Cdd:PLN03232 962 GQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLST 1041
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1109 LVMICMATPVFAIIIIPLSILYISVQVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDI 1188
Cdd:PLN03232 1042 FALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDN 1121
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1189 NQKCVFSWITSNRWLAIRLELVGNLVVFCSALLLVIYRKTLTGDVV-----GFVLSNALNITQTLNWLVRMTSEAETNIV 1263
Cdd:PLN03232 1122 NIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAGfastmGLLLSYTLNITTLLSGVLRQASKAENSLN 1201
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1264 AVERISEYINVENEAPWV-TDKRPPADWPRHGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNC 1342
Cdd:PLN03232 1202 SVERVGNYIDLPSEATAIiENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNA 1281
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1343 LFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNLDPFNKYSDEEVWRALELAHLRSFVSGLQLGL 1422
Cdd:PLN03232 1282 LFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGL 1361
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1423 LSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMV 1502
Cdd:PLN03232 1362 DAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILV 1441
|
1530 1540 1550
....*....|....*....|....*....|....*..
gi 3219824 1503 LDNGKIVEYGSPEELLSNRGS-FYLMAKEAGIENVNH 1538
Cdd:PLN03232 1442 LSSGQVLEYDSPQELLSRDTSaFFRMVHSTGPANAQY 1478
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
306-1532 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 832.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 306 LIKSLFKTFHVVILKSFILKLIHDLLVFLNPQLLKLLIGFVKSSNSYVWFGYICAILMFAVTLIQSFCLQSYFQHCFVLG 385
Cdd:PTZ00243 234 LLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 386 MCVRTTVMSSIYKKALTLSN--LARKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILAGV 463
Cdd:PTZ00243 314 LQYRSALNALIFEKCFTISSksLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 464 GVMVLLIPVNGVLATKIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLLI 543
Cdd:PTZ00243 394 AVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 544 FILQITPILVSVVTFSVYVLvdSANVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRLERYLGGDDLDTSAI 623
Cdd:PTZ00243 474 FVNNATPTLMIAVVFTVYYL--LGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNATCSTV 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 624 RRVSNFDK-----------AVKFSEASFT-----------------------W------DPD---------LEAT----- 649
Cdd:PTZ00243 552 QDMEEYWReqrehstacqlAAVLENVDVTafvpvklprapkvktsllsralrMlcceqcRPTkrhpspsvvVEDTdygsp 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 --------------------------------------------IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEME 685
Cdd:PTZ00243 632 ssasrhiveggtgggheatptsersaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 686 NVHGHITIQGSTAYVPQQSWIQNGTIKDNILFGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRV 765
Cdd:PTZ00243 712 ISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARV 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 766 SLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDll 845
Cdd:PTZ00243 792 SLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-- 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 846 dkkgvFARN--WKTfMKHSGPEGEATVNNDSEAEDDDDGLIPTMEEIPEDAASLAMRREnslrrtlsrssrsssrRGKSL 923
Cdd:PTZ00243 868 -----FMRTslYAT-LAAELKENKDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNA----------------EGGDG 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 924 KNSlkiknvnvlkekekEVEGQKLIKKEFVETGKVKFSIYLKYLQAVG---WWsiLFIILFYGLNNVAFIGSNLWLSAWT 1000
Cdd:PTZ00243 926 AAL--------------DAAAGRLMTREEKASGSVPWSTYVAYLRFCGglhAA--GFVLATFAVTELVTVSSGVWLSMWS 989
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1001 SDSDNLNGTNNssshrdmrIGVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRF 1080
Cdd:PTZ00243 990 TRSFKLSAATY--------LYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRF 1061
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1081 SGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAIIIIPLSILYISVQVFYVATSRQLRRLDSVTKSPIYSHFS 1160
Cdd:PTZ00243 1062 SRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLE 1141
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1161 ETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWITSNRWLAIRLELVGNLVVFCSALLLVIyRKTL--TGDVVGFV- 1237
Cdd:PTZ00243 1142 EALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVI-GTMLraTSQEIGLVs 1220
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1238 --LSNALNITQTLNWLVRMTSEAETNIVAVERISEYI-NVENEA-PWVTD------KR-----------------PPADW 1290
Cdd:PTZ00243 1221 lsLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDmPELDEevdaleRRtgmaadvtgtvviepasPTSAA 1300
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1291 PRH---GEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLH 1367
Cdd:PTZ00243 1301 PHPvqaGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLR 1380
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1368 DLRERLTIIPQDPILFSGSLRMNLDPFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAV 1447
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAL 1460
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1448 LRK-SKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSFYL 1526
Cdd:PTZ00243 1461 LKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540
|
....*.
gi 3219824 1527 MAKEAG 1532
Cdd:PTZ00243 1541 SMVEAL 1546
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
191-1524 |
9.30e-167 |
|
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: 542.96 E-value: 9.30e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 191 QTPSVTASFLSSITFSWYDRTVLKGYKHPLTLEDVWDIDEGFKTRSVTSKFEaamtkdlqkarQAFQRRLQKSQRKPEat 270
Cdd:TIGR01271 3 RSPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLE-----------REWDRELASAKKNPK-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 271 lhglnkkqsqsqdvlvleeakkksekttkdypkswLIKSLFKTFHVVILKSFILKLIHDLLVFLNPQLLKLLIGFVKSSN 350
Cdd:TIGR01271 70 -----------------------------------LLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDPFN 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 351 SYVW-FGYICAILMFAVTLIQSFCLQSYFQHCFVLGMCVRTTVMSSIYKKALTLSNLARKQYTIGETVNLMSVDSQKLMD 429
Cdd:TIGR01271 115 APEReIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 430 ATNYMQLVWSSVIQITLSIFFLWRELGPSILAGVGVMVLLIPVNGVLATKIRNIQVQNMKNKDKRLKIMNEILSGIKILK 509
Cdd:TIGR01271 195 GLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 510 YFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQITPILVSVVTFSVYVLVDSanvLNAEKAFTSITLFNILRFPL 589
Cdd:TIGR01271 275 AYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALIKG---IILRRIFTTISYCIVLRMTV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 590 S-MLPMVTSSILQASVSVDRLERYLGGDD-------LDTSAI--------------------------RRVSNFDKAVKF 635
Cdd:TIGR01271 352 TrQFPGAIQTWYDSLGAITKIQDFLCKEEyktleynLTTTEVemvnvtaswdegigelfekikqnnkaRKQPNGDDGLFF 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 636 SEASFTWDPDLeatiQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSWIQNGTIKDNI 715
Cdd:TIGR01271 432 SNFSLYVTPVL----KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNI 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 716 LFGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHI 795
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 796 FNKVVGPngLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFA----------------RN---WK 856
Cdd:TIGR01271 588 FESCLCK--LMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSslllgleafdnfsaerRNsilTE 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 857 TFMKHSgPEGEATVNNDSE-------------AEDDDDGLI----------------------PTMEE------------ 889
Cdd:TIGR01271 666 TLRRVS-IDGDSTVFSGPEtikqsfkqpppefAEKRKQSIIlnpiasarkfsfvqmgpqkaqaTTIEDavrepserkfsl 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 890 IPEDAAS----------------LAMRRENSLRRTLSRSSRSSSRRGK--SLKNSLKIKNVNVLK--------------- 936
Cdd:TIGR01271 745 VPEDEQGeeslprgnqyhhglqhQAQRRQSVLQLMTHSNRGENRREQLqtSFRKKSSITQQNELAseldiysrrlskdsv 824
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 937 -EKEKEVEGQKLiKKEFVETGKVKF-----SIYLKYL---QAVGWWSILFIILFygLNNVAFIGSNLWLSAWTSDSDNL- 1006
Cdd:TIGR01271 825 yEISEEINEEDL-KECFADERENVFetttwNTYLRYIttnRNLVFVLIFCLVIF--LAEVAASLLGLWLITDNPSAPNYv 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1007 -NGTNNSSSHRDMR----------------IGV---FGALGLAQGICLlISTLWSIyacrnaSKALHGQLLTNILRAPMR 1066
Cdd:TIGR01271 902 dQQHANASSPDVQKpviitptsayyifyiyVGTadsVLALGFFRGLPL-VHTLLTV------SKRLHEQMLHSVLQAPMA 974
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1067 FFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAIIIIPLSILYISVQVFYVATSRQLRR 1146
Cdd:TIGR01271 975 VLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQ 1054
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1147 LDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWITSNRWLAIRLELVgnLVVFCSAlllVIYR 1226
Cdd:TIGR01271 1055 LESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDII--FVFFFIA---VTFI 1129
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1227 KTLTGDV----VGFVLSNALNITQTLNWLVRMTSEAETNIVAVERISEYINVENEAPWVTDKRPPAD------------- 1289
Cdd:TIGR01271 1130 AIGTNQDgegeVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKYQlstvlvienphaq 1209
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1290 --WPRHGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILeSAGGQIIIDGIDVASIGLH 1367
Cdd:TIGR01271 1210 kcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQ 1288
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1368 DLRERLTIIPQDPILFSGSLRMNLDPFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAV 1447
Cdd:TIGR01271 1289 TWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSI 1368
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1448 LRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSF 1524
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
975-1271 |
5.10e-152 |
|
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: 464.26 E-value: 5.10e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 975 ILFIILFYGLNNVAFIGSNLWLSAWTSDSDNLNGTNNSSshRDMRIGVFGALGLAQGICLLISTLWSIYACRNASKALHG 1054
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQ--RDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1055 QLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAIIIIPLSILYISVQ 1134
Cdd:cd18603 79 KLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1135 VFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWITSNRWLAIRLELVGNLV 1214
Cdd:cd18603 159 RFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLI 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1215 VFCSALLLVIYRKTLTGDVVGFVLSNALNITQTLNWLVRMTSEAETNIVAVERISEY 1271
Cdd:cd18603 239 VLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
320-609 |
7.76e-147 |
|
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: 450.38 E-value: 7.76e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 320 KSFILKLIHDLLVFLNPQLLKLLIGFVKSSNSYVWFGYICAILMFAVTLIQSFCLQSYFQHCFVLGMCVRTTVMSSIYKK 399
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 400 ALTLSNLARKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILAGVGVMVLLIPVNGVLATK 479
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 480 IRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQITPILVSVVTFS 559
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 3219824 560 VYVLVDSANVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRL 609
Cdd:cd18595 241 TYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1294-1514 |
9.64e-137 |
|
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: 420.36 E-value: 9.64e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1294 GEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERL 1373
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1374 TIIPQDPILFSGSLRMNLDPFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKI 1453
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 1454 LVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSP 1514
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1020-1525 |
7.24e-122 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 394.15 E-value: 7.24e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWM 1099
Cdd:COG1132 64 LLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1100 MCFFGIAGTLVMICMATPVFAIIIIPLSILYISVQVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFL 1179
Cdd:COG1132 144 RSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREEREL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1180 AWNEKQIDINQKCVFSWITSNRWLAIRLELVGNLVVFCSALL--LVIYRKTLT-GDVVGFVLSnALNITQTLNWLVRMTS 1256
Cdd:COG1132 224 ERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVggLLVLSGSLTvGDLVAFILY-LLRLFGPLRQLANVLN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1257 EAETNIVAVERISEYINVENEAPWVTDKRPPAdwPRHGEIQFNNYQVRYRPElDLVLKGITCNIKSGEKVGVVGRTGAGK 1336
Cdd:COG1132 303 QLQRALASAERIFELLDEPPEIPDPPGAVPLP--PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1337 SSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNL---DPfnKYSDEEVWRALELAHLRS 1413
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHE 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1414 FVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHT 1493
Cdd:COG1132 458 FIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLST 537
|
490 500 510
....*....|....*....|....*....|..
gi 3219824 1494 IMDSDKIMVLDNGKIVEYGSPEELLSNRGSFY 1525
Cdd:COG1132 538 IRNADRILVLDDGRIVEQGTHEELLARGGLYA 569
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
633-834 |
1.94e-113 |
|
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: 356.01 E-value: 1.94e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLEA---TIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSWIQNG 709
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 710 TIKDNILFGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDA 789
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 3219824 790 HVGKHIFNKVVGPNgLLAGKTRIFVTHGIHFLPQVDEIVVLGKGT 834
Cdd:cd03250 161 HVGRHIFENCILGL-LLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
321-609 |
3.45e-112 |
|
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: 356.03 E-value: 3.45e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 321 SFILKLIHDLLVFLNPQLLKLLIGFVKSSNSY-VWFGYICAILMFAVTLIQSFCLQSYFQHCFVLGMCVRTTVMSSIYKK 399
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEpLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 400 ALTLSNLARKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILAGVGVMVLLIPVNGVLATK 479
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 480 IRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQITPILVSVVTFS 559
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 3219824 560 VYVLVDsaNVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRL 609
Cdd:cd18579 242 TYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
975-1272 |
2.28e-111 |
|
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: 354.12 E-value: 2.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 975 ILFIILFYGLNNVAFIGSNLWLSAWTSDSdnlngTNNSSSHRDMRIGVFGALGLAQGICL-LISTLWSIYACRNASKALH 1053
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDW-----SSSPNSSSGYYLGVYAALLVLASVLLvLLRWLLFVLAGLRASRRLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1054 GQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAIIIIPLSILYISV 1133
Cdd:cd18580 76 DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1134 QVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWITSNRWLAIRLELVGNL 1213
Cdd:cd18580 156 QRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1214 VVFCSALLLVIYRKTLTGDVVGFVLSNALNITQTLNWLVRMTSEAETNIVAVERISEYI 1272
Cdd:cd18580 236 LALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1290-1514 |
1.65e-102 |
|
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: 325.91 E-value: 1.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1290 WPRHGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDL 1369
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1370 RERLTIIPQDPILFSGSLRMNLDPFNKYSDEEVWRALelahlrsfvsglqlgllsEVTEGGDNLSIGQRQLLCLGRAVLR 1449
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1450 KSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSP 1514
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
975-1271 |
2.71e-100 |
|
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: 323.27 E-value: 2.71e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 975 ILFIILFYGLNNVAFIGSNLWLSAWTSDSDNL-NGTNnssshrdmrIGVFGALGLAQGICLLISTLWSIYACRNASKALH 1053
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLsQGFY---------IGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1054 GQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAIIIIPLSILYISV 1133
Cdd:cd18606 72 NKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1134 QVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWITSNRWLAIRLELVGNL 1213
Cdd:cd18606 152 ANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1214 VVFCSALLLVIYRKTLTGDVVGFVLSNALNITQTLNWLVRMTSEAETNIVAVERISEY 1271
Cdd:cd18606 232 LVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1020-1530 |
1.35e-96 |
|
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: 327.95 E-value: 1.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALgLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSgDISTVDDLLP-QTLRSW 1098
Cdd:COG2274 200 IGLLLAL-LFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTgSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1099 MMCFFGIAGTLVMICMATPVFAIIIIpLSILYIsvqVFYVATSRQLRRLD---SVTKSPIYSHFSETVTGLPIIRAFEHQ 1175
Cdd:COG2274 278 LDLLFVLIFLIVLFFYSPPLALVVLL-LIPLYV---LLGLLFQPRLRRLSreeSEASAKRQSLLVETLRGIETIKALGAE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1176 QRFLA-WNE---KQIDINQKcVFSWITSNRWLAIRLELVGNLVVFCSALLLVIyRKTLTgdvVG-FVLSNALnITQTLNW 1250
Cdd:COG2274 354 SRFRRrWENllaKYLNARFK-LRRLSNLLSTLSGLLQQLATVALLWLGAYLVI-DGQLT---LGqLIAFNIL-SGRFLAP 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1251 LVRMTS---EAETNIVAVERISEYINVENEAPwvtDKRPPADWPR-HGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKV 1326
Cdd:COG2274 428 VAQLIGllqRFQDAKIALERLDDILDLPPERE---EGRSKLSLPRlKGDIELENVSFRYPGDSPPVLDNISLTIKPGERV 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1327 GVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNL---DPfnKYSDEEVW 1403
Cdd:COG2274 505 AIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEII 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1404 RALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCT 1483
Cdd:COG2274 583 EAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRT 662
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 3219824 1484 VITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSFYLMAKE 1530
Cdd:COG2274 663 VIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
975-1272 |
1.19e-94 |
|
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: 307.47 E-value: 1.19e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 975 ILFIILFYGLNNVAFIGSNLWLSAWTSDSDNLNGTNNSSSHRDMRIGVFGALGLAQGICLLISTLWSIYACRNASKALHG 1054
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1055 QLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAIIIIPLSILYISVQ 1134
Cdd:cd18604 81 RLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1135 VFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWITSNRWLAIRLELVGNLV 1214
Cdd:cd18604 161 RLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1215 VFCSALLLViYRKTLTGDVVGFVLSNALNITQTLNWLVRMTSEAETNIVAVERISEYI 1272
Cdd:cd18604 241 SFATAALLV-YGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
975-1271 |
5.88e-89 |
|
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: 291.81 E-value: 5.88e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 975 ILFIILFYGLNNVAFIGSNLWLSAWT-SDSDNLNGTNNSSSHRDMR------IGVFGALGLAQGICLLISTLWSIYACRN 1047
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTeANHDVASVVFNITSSSLEDdevsyyISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1048 ASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAIIIIPLS 1127
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1128 ILYISVQVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWITSNRWLAIRL 1207
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 1208 ELVGNLVVFCSAL--LLVIYRKTLTGDVVGFVLSNALNITQTLNWLVRMTSEAETNIVAVERISEY 1271
Cdd:cd18602 241 DYLGAVIVFLAALssLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
321-609 |
2.44e-84 |
|
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: 278.18 E-value: 2.44e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 321 SFILKLIHDLLVFLNPQLLKLLIGFVKSS-----NSYVWFGYICAILMFAVTLIQSFCLQSYFQHCFVLGMCVRTTVMSS 395
Cdd:cd18597 2 AGLLKLLADVLQVLSPLLLKYLINFVEDAylggpPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 396 IYKKALTLSNLARKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILAGVGVMVLLIPVNGV 475
Cdd:cd18597 82 IYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 476 LATKIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQITPILVSV 555
Cdd:cd18597 162 LMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASM 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 3219824 556 VTFSVYVLVDsaNVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRL 609
Cdd:cd18597 242 LSFITYYATG--HTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
976-1272 |
9.51e-82 |
|
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: 270.94 E-value: 9.51e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 976 LFIILFYGLNNVAFIGSNLWLSAWTSDSDNLNGTNNSSSHRDMrIGVFGALGLAQGICLLISTLWSIYACRNASKALHGQ 1055
Cdd:cd18605 2 ILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFINDSFNFF-LTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1056 LLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAIIIIPLSILYISVQV 1135
Cdd:cd18605 81 LLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1136 FYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWITSNRWLAIRLELVGNLVV 1215
Cdd:cd18605 161 YYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1216 FC---SALLLVIYRKTLTGDVVGFVLSNALNITQTLNWLVRMTSEAETNIVAVERISEYI 1272
Cdd:cd18605 241 TFvalTAVVQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1294-1525 |
2.03e-80 |
|
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: 265.62 E-value: 2.03e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1294 GEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERL 1373
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1374 TIIPQDPILFSGSLRMNLDPFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKI 1453
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1454 LVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSFY 1525
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
322-609 |
4.64e-80 |
|
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: 266.67 E-value: 4.64e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 322 FILKLIHDLLVFLNPQLLKLLIGFV-KSSNSYVWFGYICAILMFAVTLIQSFCLQSYFQHCFVLGMCVRTTVMSSIYKKA 400
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLeDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 401 LTLSNLA-------------------RKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILA 461
Cdd:cd18596 83 LRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 462 GVGVMVLLIPVNGVLATKIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSL 541
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 542 LIFILQITPILVSVVTFSVYVLVdSANVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRL 609
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLV-MGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
305-853 |
1.65e-79 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 274.73 E-value: 1.65e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 305 WLIKSLFKTFHVVILKSFILKLIHDLLVFLNPQLLKLLI--GFVKSSNSYVWFgyiCAILMFAVTLIQSFC--LQSYFQH 380
Cdd:COG1132 10 RRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdaLLAGGDLSALLL---LLLLLLGLALLRALLsyLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 381 cfVLGMCVRTTVMSSIYKKALTLSNLARKQYTIGETVNLMSVDSQKLMDA-TNYMQLVWSSVIQITLSI---FFLWRELG 456
Cdd:COG1132 87 --RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFlAHGLPQLVRSVVTLIGALvvlFVIDWRLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 457 PSILAGVGVMVLLIpvnGVLATKIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFG 536
Cdd:COG1132 165 LIVLLVLPLLLLVL---RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 537 QLQSLLIFILQITPILVSVVTFSVYVLVDSANVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRLERYL--G 614
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLdeP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 615 GDDLDTSAIRRVSNFDKAVKFSEASFTWDPDlEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQ 694
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 695 G-------------STAYVPQQSWIQNGTIKDNILFGS-EYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGG 760
Cdd:COG1132 401 GvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 761 QKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGS 840
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570
....*....|...
gi 3219824 841 YRDLLDKKGVFAR 853
Cdd:COG1132 558 HEELLARGGLYAR 570
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1294-1522 |
6.76e-78 |
|
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: 257.15 E-value: 6.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1294 GEIQFNNYQVRYRPElDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERL 1373
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1374 TIIPQDPILFSGSLRMNLDPFNKYSDEEVW-RALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSK 1452
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1453 ILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRG 1522
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
284-856 |
4.02e-75 |
|
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: 265.54 E-value: 4.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 284 VLVLEEAKKKSEKTTKDYPKSWLIKSLFKtFHVVILKSFILKLIHDLLVFLNPQLLKLLIGFVKSSNSYVWFgYICAILM 363
Cdd:COG2274 125 ALLLEPTPEFDKRGEKPFGLRWFLRLLRR-YRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTL-WVLAIGL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 364 FAVTLIQSF--CLQSYFqhcfVLGMCVR--TTVMSSIYKKALTLSNLARKQYTIGETVN-LMSVDS-QKLMdaTNYMQLV 437
Cdd:COG2274 203 LLALLFEGLlrLLRSYL----LLRLGQRidLRLSSRFFRHLLRLPLSFFESRSVGDLASrFRDVESiREFL--TGSLLTA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 438 WSSVIQITLSIFFLWReLGPSIlagVGVMVLLIPVNGVLAT----KIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAW 513
Cdd:COG2274 277 LLDLLFVLIFLIVLFF-YSPPL---ALVVLLLIPLYVLLGLlfqpRLRRLSREESEASAKRQSLLVETLRGIETIKALGA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 514 EPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQITPILVSVVT--FSVYVLVDSanvlnaekaftSITL-----FNIL- 585
Cdd:COG2274 353 ESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALlwLGAYLVIDG-----------QLTLgqliaFNILs 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 586 -RF--PLSMLPMVTSSILQASVSVDRLERYLGG--DDLDTSAIRRVSNFDKAVKFSEASFTWDPDLEATIQDVNLDIKPG 660
Cdd:COG2274 422 gRFlaPVAQLIGLLQRFQDAKIALERLDDILDLppEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPG 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 661 QLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAYVPQQSWIQNGTIKDNILFG-SEYNEKKY 726
Cdd:COG2274 502 ERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGdPDATDEEI 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 727 QQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVvgpNGLL 806
Cdd:COG2274 582 IEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLL 658
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 3219824 807 AGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFARNWK 856
Cdd:COG2274 659 KGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
971-1272 |
7.15e-74 |
|
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: 249.02 E-value: 7.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 971 GWWSILFIILFYGLNNVAFIGSNLWLSAW------TSDSDNLNGTNNSSSHRD-----MRIGVFGALGLAQGICLLISTL 1039
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgNTTNNVDNSTVDSGNISDnpdlnFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1040 WSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVF 1119
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1120 AIIIIPLSILYISVQVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWITS 1199
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1200 NRWLAIRLELVGNLVVFCSALLLVIYRKTLTGDVVGFVLSNALNITQTLNWLVRMTSEAETNIVAVERISEYI 1272
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
963-1522 |
1.43e-73 |
|
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: 256.99 E-value: 1.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 963 YLKYLQAVGWWSILFIILFYGLnnVAFIGSNLWLSAWTSDSdnLNGTnnssshrdmrIGVFGALGLAQGICLLISTLWSI 1042
Cdd:COG4988 18 WLALAVLLGLLSGLLIIAQAWL--LASLLAGLIIGGAPLSA--LLPL----------LGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1043 YACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFsgdISTVDDL-------LPQTLRSWMMCFFgiagTLVMICMA 1115
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLL---TEGVEALdgyfaryLPQLFLAALVPLL----ILVAVFPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1116 TPVFAIII------IPLSILYISvQVFYVATSRQLRRLDSVTkspiySHFSETVTGLPIIRAF----EHQQRFLAWNEKq 1185
Cdd:COG4988 157 DWLSGLILlvtaplIPLFMILVG-KGAAKASRRQWRALARLS-----GHFLDRLRGLTTLKLFgrakAEAERIAEASED- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1186 idinqkcvFSWITsNRWLAIR------LELVGNLVVfcsALLLViyrktltgdVVGFVLSNA-LNITQTL---------- 1248
Cdd:COG4988 230 --------FRKRT-MKVLRVAflssavLEFFASLSI---ALVAV---------YIGFRLLGGsLTLFAALfvlllapeff 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1249 --------NWLVRMTSEAetnivAVERISEYINVENEAPWVTDKRPPadWPRHGEIQFNNYQVRYrPELDLVLKGITCNI 1320
Cdd:COG4988 289 lplrdlgsFYHARANGIA-----AAEKIFALLDAPEPAAPAGTAPLP--AAGPPSIELEDVSFSY-PGGRPALDGLSLTI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1321 KSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNLDPFN-KYSD 1399
Cdd:COG4988 361 PPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpDASD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1400 EEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEF 1479
Cdd:COG4988 441 EELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA 520
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 3219824 1480 SQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRG 1522
Cdd:COG4988 521 KGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
323-609 |
3.34e-73 |
|
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: 245.92 E-value: 3.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 323 ILKLIHDLLVFLNPQLLKLLIGFVKSSNSYVWFGYICAILMFAVTLIQSFClQSYFQHCF-VLGMCVRTTVMSSIYKKAL 401
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALL-SSHYNFQMnKVSLKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 402 TLSNLARKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILAGVGVMVLLIPVNGVLATKIR 481
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 482 NIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQITPILVSVVTFSVY 561
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 3219824 562 VLVdsANVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRL 609
Cdd:cd18598 243 VLM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
321-609 |
3.56e-73 |
|
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: 245.97 E-value: 3.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 321 SFILKLIHDLLVFLNPQLLKLLIGFVKSSNSYVWFGYICAILMFAVTLIQSFCLQSYFQHCFVLGMCVRTTVMSSIYKKA 400
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 401 LTLSNLARKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILAGVGVMVLLIPVNGVLATKI 480
Cdd:cd18559 82 LRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 481 RNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQITPILVSVVTFSV 560
Cdd:cd18559 162 RQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 3219824 561 YVLVDSANVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRL 609
Cdd:cd18559 242 YVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
971-1271 |
3.35e-72 |
|
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: 244.15 E-value: 3.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 971 GWWSILFIILFYGLNNVAFIGSNLWLSAW----------TSDSDNLNGTNNSSSHRDMR--IGVFGALGLAQGICLLIST 1038
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWanleeklndtTDRVQGENSTNVDIEDLDRDfnLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1039 LWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPV 1118
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1119 FAIIIIPLSILYISVQVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWIT 1198
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1199 SNRWLAIRLELVGNLVVFCSALLLVIYRKTLTGDVVGFVLSNALNITQTLNWLVRMTSEAETNIVAVERISEY 1271
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1026-1522 |
1.65e-71 |
|
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: 251.17 E-value: 1.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1026 LGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDI----STVDDLLPQTLRSWMMC 1101
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSeqvaSAATDAFIVLVRETLTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1102 ffgIAGTLVMICMATPVFAIIIIPLSILYISVQVFyvatSRQLRRLDS---VTKSPIYSHFSETVTGLPIIRAFEHQ--- 1175
Cdd:TIGR02203 143 ---IGLFIVLLYYSWQLTLIVVVMLPVLSILMRRV----SKRLRRISKeiqNSMGQVTTVAEETLQGYRVVKLFGGQaye 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1176 -QRFLAWNEkqidinqkcvfswitSNRWLAIRLELVGNL------VVFCSALLLVIY--------RKTLTGDVVGFVLSn 1240
Cdd:TIGR02203 216 tRRFDAVSN---------------RNRRLAMKMTSAGSIsspitqLIASLALAVVLFialfqaqaGSLTAGDFTAFITA- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1241 ALNITQTLNWLVRMTSEAETNIVAVERISEYINVENEAPwvTDKRPPadwPR-HGEIQFNNYQVRYRPELDLVLKGITCN 1319
Cdd:TIGR02203 280 MIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD--TGTRAI---ERaRGDVEFRNVTFRYPGRDRPALDSISLV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1320 IKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNL---DPfNK 1396
Cdd:TIGR02203 355 IEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQ 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1397 YSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIR 1476
Cdd:TIGR02203 434 ADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALE 513
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 3219824 1477 KEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRG 1522
Cdd:TIGR02203 514 RLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1073-1525 |
4.03e-69 |
|
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: 243.91 E-value: 4.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1073 TGRIVNRFSGDISTVDDLLPQTL----RSWMMCFFGIAGT------LVMICMATPVFAIIIIPLsilyisvqVFYVATSR 1142
Cdd:COG4987 111 SGDLLNRLVADVDALDNLYLRVLlpllVALLVILAAVAFLaffspaLALVLALGLLLAGLLLPL--------LAARLGRR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1143 QLRRLdSVTKSPIYSHFSETVTGLPIIRAF----EHQQRFLAWNEKQIDINQKcvfswitSNRWLAIR---LELVGNLVV 1215
Cdd:COG4987 183 AGRRL-AAARAALRARLTDLLQGAAELAAYgaldRALARLDAAEARLAAAQRR-------LARLSALAqalLQLAAGLAV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1216 FCsALLLVIY---RKTLTG-DVVGFVLSnALNITQTLNWLVRMTSEAETNIVAVERISEyinVENEAPWVTDKRPPADWP 1291
Cdd:COG4987 255 VA-VLWLAAPlvaAGALSGpLLALLVLA-ALALFEALAPLPAAAQHLGRVRAAARRLNE---LLDAPPAVTEPAEPAPAP 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1292 RHGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRE 1371
Cdd:COG4987 330 GGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1372 RLTIIPQDPILFSGSLRMNL---DPfnKYSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVL 1448
Cdd:COG4987 410 RIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALL 487
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1449 RKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSFY 1525
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
323-609 |
7.38e-67 |
|
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: 228.66 E-value: 7.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 323 ILKLIHDLLVFLNPQLLKLLIGFV------------KSSNSYVWF------GYICAILMFAVTLIQSFCLQSYFQHCFVL 384
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVeentysssnstdKLSVSYVTVeeffsnGYVLAVILFLALLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 385 GMCVRTTVMSSIYKKALTLS--NLARKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILAG 462
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 463 VGVMVLLIPVNGVLATKIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLL 542
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 543 IFILQITPILVSVVTFSVYVLVdSANVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRL 609
Cdd:cd18591 244 TFLTQASPILVTLVTFGLYPYL-EGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1296-1525 |
2.63e-66 |
|
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: 224.03 E-value: 2.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTI 1375
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDPILFSGSLRMNLdpfnKY-----SDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRK 1450
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1451 SKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSFY 1525
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1296-1527 |
3.13e-64 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 218.25 E-value: 3.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTI 1375
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDPILFSGSLRMNLdpfnKY-----SDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRK 1450
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1451 SKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSFYLM 1527
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1055-1527 |
4.59e-64 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 229.99 E-value: 4.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1055 QLLTNI----LRAPMRFFDTTPTGRIVNRFSGDISTVDDL----LPQTLRSWMMcffgIAGTLV--------MICMATPV 1118
Cdd:PRK10790 99 QLRTDVmdaaLRQPLSAFDTQPVGQLISRVTNDTEVIRDLyvtvVATVLRSAAL----IGAMLVamfsldwrMALVAIMI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1119 FAIIIIPLSILyisvQVFYVATSRQLRRLdsvtKSPIYSHFSETVTGLPIIRAFEHQQRFlawNEKQIDINQKCVFSwit 1198
Cdd:PRK10790 175 FPAVLVVMVIY----QRYSTPIVRRVRAY----LADINDGFNEVINGMSVIQQFRQQARF---GERMGEASRSHYMA--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1199 snRWLAIRLE--LVGNLVVFCSAL----LLVIYRKTLTGDV-VGfVLSNALNITQTLNW-LVRMTSEA---ETNIVAVER 1267
Cdd:PRK10790 241 --RMQTLRLDgfLLRPLLSLFSALilcgLLMLFGFSASGTIeVG-VLYAFISYLGRLNEpLIELTTQQsmlQQAVVAGER 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1268 ISEYINVENEaPWVTDKRPPADwprhGEIQFNNYQVRYRPElDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRIL 1347
Cdd:PRK10790 318 VFELMDGPRQ-QYGNDDRPLQS----GRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYY 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1348 ESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNLDPFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEVT 1427
Cdd:PRK10790 392 PLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1428 EGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGK 1507
Cdd:PRK10790 472 EQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQ 551
|
490 500
....*....|....*....|
gi 3219824 1508 IVEYGSPEELLSNRGSFYLM 1527
Cdd:PRK10790 552 AVEQGTHQQLLAAQGRYWQM 571
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1051-1527 |
4.14e-61 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 223.83 E-value: 4.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1051 ALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQT----LRSWMMCFfgiaGTLVMICMATPVFAI---II 1123
Cdd:TIGR00958 235 RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNvnvlLRNLVMLL----GLLGFMLWLSPRLTMvtlIN 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1124 IPLSILYISV-QVFYVATSRQLRrlDSVTKSPIYSHfsETVTGLPIIRAF--EHQ--QRFLAWNEKQIDINQK-----CV 1193
Cdd:TIGR00958 311 LPLVFLAEKVfGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaaEEGeaSRFKEALEETLQLNKRkalayAG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1194 FSWITSNRWLAIRLelvgnLVVFCsALLLVIYRKTLTGDVVGFVLSNaLNITQTLNWLVRMTSEAETNIVAVERISEYIN 1273
Cdd:TIGR00958 387 YLWTTSVLGMLIQV-----LVLYY-GGQLVLTGKVSSGNLVSFLLYQ-EQLGEAVRVLSYVYSGMMQAVGASEKVFEYLD 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1274 VENEAPWVTDKRPPadwPRHGEIQFNNYQVRY--RPELdLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAG 1351
Cdd:TIGR00958 460 RKPNIPLTGTLAPL---NLEGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1352 GQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNLD-PFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGG 1430
Cdd:TIGR00958 536 GQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1431 DNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTirKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVE 1510
Cdd:TIGR00958 616 SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
490
....*....|....*..
gi 3219824 1511 YGSPEELLSNRGSFYLM 1527
Cdd:TIGR00958 694 MGTHKQLMEDQGCYKHL 710
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1296-1531 |
1.84e-60 |
|
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: 207.39 E-value: 1.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRY--RPELdLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERL 1373
Cdd:cd03249 1 IEFKNVSFRYpsRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1374 TIIPQDPILFSGSLRMNLdpfnKY-----SDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVL 1448
Cdd:cd03249 80 GLVSQEPVLFDGTIAENI----RYgkpdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1449 RKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSFYLMA 1528
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
...
gi 3219824 1529 KEA 1531
Cdd:cd03249 236 KAQ 238
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1228-1527 |
3.82e-60 |
|
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: 218.54 E-value: 3.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1228 TLT-GDvvgFVLSNA--LNITQTLNWLVRMTSEAETNIVAVERISEYINVENEapwVTDKRPPADWP-RHGEIQFNNYQV 1303
Cdd:COG5265 292 TMTvGD---FVLVNAylIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE---VADAPDAPPLVvGGGEVRFENVSF 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1304 RYRPElDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILF 1383
Cdd:COG5265 366 GYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLF 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 SGSLRMNLdpfnKY-----SDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDE 1458
Cdd:COG5265 445 NDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1459 ATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSFYLM 1527
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1296-1507 |
7.96e-60 |
|
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: 203.00 E-value: 7.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTI 1375
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDPILFSGSLRMNLdpfnkysdeevwralelahlrsfvsglqlgllsevteggdnLSIGQRQLLCLGRAVLRKSKILV 1455
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1456 LDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGK 1507
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
633-834 |
9.91e-59 |
|
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: 201.79 E-value: 9.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLeATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHI-----------------TIQG 695
Cdd:cd03290 1 VQVTNGYFSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 696 STAYVPQQSWIQNGTIKDNILFGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDA 775
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 776 DIYILDDPLSAVDAHVGKHIFNKvvgpnGLLA-----GKTRIFVTHGIHFLPQVDEIVVLGKGT 834
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQE-----GILKflqddKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
323-610 |
1.54e-56 |
|
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: 198.24 E-value: 1.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 323 ILKLIHDLLVFLNPQLLKLLIG-FVKSSNSYVWFGYICAILMFAVTLIQSFCLQSYFQHCFVLGMCVRTTVMSSIYKKAL 401
Cdd:cd18594 4 ILLFLEESLKIVQPLLLGRLVAyFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 402 TLSNLARKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILAGVGVMVLLIPVNGVLATKIR 481
Cdd:cd18594 84 KLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 482 NIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQITPILVSVVTFSVY 561
Cdd:cd18594 164 KYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 3219824 562 VLVDsaNVLNAEKAFTSITLFNILRFPLSM-LPMVTSSILQASVSVDRLE 610
Cdd:cd18594 244 VLTG--NTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1296-1525 |
9.57e-56 |
|
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: 193.86 E-value: 9.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTI 1375
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDPILFSGSLRMNL---DPfnKYSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSK 1452
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1453 ILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSFY 1525
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
624-852 |
2.79e-55 |
|
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: 194.30 E-value: 2.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 624 RRVSNFDKAVKFSEASFTWDPDLeatiQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQ 703
Cdd:cd03291 31 RKHSSDDNNLFFSNLCLVGAPVL----KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 704 SWIQNGTIKDNILFGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDP 783
Cdd:cd03291 107 SWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 784 LSAVDAHVGKHIFNKVVGPngLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFA 852
Cdd:cd03291 187 FGYLDVFTEKEIFESCVCK--LMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFS 253
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
321-609 |
5.14e-55 |
|
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: 193.55 E-value: 5.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 321 SFILKLIHDLLVFLNPQ-LLKLLIGFVKSSNSYVWFGYICAILMFAVTLIQSFCLQSYFQHCFVLGMCVRTTVMSSIYKK 399
Cdd:cd18592 2 SILLLLISLIFGFIGPTiLIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 400 ALTLSNLarKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSILAGVGVMVLLIPVNGVLATK 479
Cdd:cd18592 82 ILRLRSL--GDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 480 IRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQITPILVSVVTFS 559
Cdd:cd18592 160 TGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 3219824 560 VYVLvdSANVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRL 609
Cdd:cd18592 240 AHVA--LGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1294-1509 |
1.34e-53 |
|
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: 187.03 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1294 GEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERL 1373
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1374 TIIPQDPILFSGSLRMNLDPFNKY-SDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSK 1452
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1453 ILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIV 1509
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
361-849 |
2.50e-52 |
|
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: 194.59 E-value: 2.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 361 ILMFAVTLIQSFClqSYFQH--CFVLGMCVRTTVMSSIYKKALTLSNLARKQYTIGETVNLMS--VDSqklMDA--TNYM 434
Cdd:COG4988 62 GLLLAVLLLRALL--AWLREraAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTegVEA---LDGyfARYL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 435 -QLVWSSVIQITLSIFFLWRelgpSILAGV--GVMVLLIPVNGVL---ATKIRNiqvqnmknkDKRLKIMN-------EI 501
Cdd:COG4988 137 pQLFLAALVPLLILVAVFPL----DWLSGLilLVTAPLIPLFMILvgkGAAKAS---------RRQWRALArlsghflDR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 502 LSGIKILKYFAWEPSFQEQVQGI----RKKELKnLLRFGQLQSL-LIFILQITPILVSVvtFSVYVLVDsanvlnaekaf 576
Cdd:COG4988 204 LRGLTTLKLFGRAKAEAERIAEAsedfRKRTMK-VLRVAFLSSAvLEFFASLSIALVAV--YIGFRLLG----------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 577 TSITLFNILrFPLSMLPMVTSSI----------LQASVSVDRLERYLGGDDLDTSAIRRVSNFDK--AVKFSEASFTWDP 644
Cdd:COG4988 270 GSLTLFAAL-FVLLLAPEFFLPLrdlgsfyharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGppSIELEDVSFSYPG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 645 DLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAYVPQQSWIQNGTI 711
Cdd:COG4988 349 GRPA-LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTI 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 712 KDNILFGS-EYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAH 790
Cdd:COG4988 428 RENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAE 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 791 VGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKG 849
Cdd:COG4988 508 TEAEILQAL---RRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1294-1524 |
1.00e-51 |
|
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: 183.90 E-value: 1.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1294 GEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILeSAGGQIIIDGIDVASIGLHDLRERL 1373
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1374 TIIPQDPILFSGSLRMNLDPFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKI 1453
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 1454 LVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSF 1524
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1213-1533 |
1.40e-51 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 192.87 E-value: 1.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1213 LVVFCSALLLVIYRKTLTGDVVGFVLSNALNITQtlnwLVRMTSEAETNIVAVERISEYINVENEAPWVTDKRPPADWPR 1292
Cdd:PRK13657 255 LAILVLGAALVQKGQLRVGEVVAFVGFATLLIGR----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1293 -HGEIQFNNYQVRY---RPELDlvlkGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHD 1368
Cdd:PRK13657 331 vKGAVEFDDVSFSYdnsRQGVE----DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1369 LRERLTIIPQDPILFSGSLRMNL-----DPfnkySDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCL 1443
Cdd:PRK13657 407 LRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAI 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1444 GRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGS 1523
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGR 562
|
330
....*....|
gi 3219824 1524 FYLMAKEAGI 1533
Cdd:PRK13657 563 FAALLRAQGM 572
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1061-1529 |
1.59e-51 |
|
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: 194.79 E-value: 1.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1061 LRAPMRFFDTTPTGRIVNRFSGdISTVDDLL----PQTLRSWMMCFFgiagTLVMICMATPVFAIIIIPLSILYISVqvF 1136
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASRAMG-ISQIRRILsgstLTTLLSGIFALL----NLGLMFYYSWKLALVAVALALVAIAV--T 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1137 YVATSRQLR--RLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLA-WNEKqidinqkcvFSwitSNRWLAIRLELVGNL 1213
Cdd:TIGR03797 293 LVLGLLQVRkeRRLLELSGKISGLTVQLINGISKLRVAGAENRAFArWAKL---------FS---RQRKLELSAQRIENL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1214 V--------VFCSALLLVIYRKTLT------GDVVGF------VLSNALNITQTLnwlvrmtSEAETNIVAVERISEYIN 1273
Cdd:TIGR03797 361 LtvfnavlpVLTSAALFAAAISLLGgaglslGSFLAFntafgsFSGAVTQLSNTL-------ISILAVIPLWERAKPILE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1274 VENEAPwvTDKRPPADWprHGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLtnclFRIL------ 1347
Cdd:TIGR03797 434 ALPEVD--EAKTDPGKL--SGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLlgfetp 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1348 ESagGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNLDPFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEVT 1427
Cdd:TIGR03797 506 ES--GSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVIS 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1428 EGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKefSQCTVITIAHRLHTIMDSDKIMVLDNGK 1507
Cdd:TIGR03797 584 EGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLER--LKVTRIVIAHRLSTIRNADRIYVLDAGR 661
|
490 500
....*....|....*....|..
gi 3219824 1508 IVEYGSPEELLSNRGSFYLMAK 1529
Cdd:TIGR03797 662 VVQQGTYDELMAREGLFAQLAR 683
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
976-1272 |
2.59e-51 |
|
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: 183.18 E-value: 2.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 976 LFIILFYGLNNVAFIGSNLWLSAWTsdsdnLNGTNNSSSHRDMRIGVFGALGLAQGICLLISTLWSIYACRNASKALHGQ 1055
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWF-----DDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1056 LLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAiIIIPLSILYISVQV 1135
Cdd:cd18559 77 LYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAA-VGIPLGLLYVPVNR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1136 FYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDiNQKCVFSWITSNRWLAIRLELVGNLVV 1215
Cdd:cd18559 156 VYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1216 FCSALLLVIYRKTLTGdVVGFVLSNALNITQTLNWLVRMTSEAETNIVAVERISEYI 1272
Cdd:cd18559 235 LFASFFAYVSRHSLAG-LVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
396-856 |
2.01e-49 |
|
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: 185.74 E-value: 2.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 396 IYKKALTLSNLARKQYTIGETVNLMSVDSQKLMDAtnYMQLV---WSSVIQITLSIFFLWR---ELGPSILAGVGVMVLL 469
Cdd:COG4987 94 LYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNL--YLRVLlplLVALLVILAAVAFLAFfspALALVLALGLLLAGLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 470 IPVNGVLATKIRNIQVQNMKNkDKRLKIMnEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQL----QSLLIFI 545
Cdd:COG4987 172 LPLLAARLGRRAGRRLAAARA-ALRARLT-DLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLsalaQALLQLA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 546 LQITpiLVSVVTFSVYVLVD---SANVLnAEKAFTSITLFNILrfplSMLPMVTSSILQASVSVDRLERYLGGD-DLDTS 621
Cdd:COG4987 250 AGLA--VVAVLWLAAPLVAAgalSGPLL-ALLVLAALALFEAL----APLPAAAQHLGRVRAAARRLNELLDAPpAVTEP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 622 AIRRVSNFDKAVKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------ 695
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdl 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 696 -------STAYVPQQSWIQNGTIKDNILFGSEY-NEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSL 767
Cdd:COG4987 403 deddlrrRIAVVPQRPHLFDTTLRENLRLARPDaTDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLAL 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 768 ARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVgpnGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDK 847
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLL---EALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
....*....
gi 3219824 848 KGVFARNWK 856
Cdd:COG4987 560 NGRYRQLYQ 568
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
354-609 |
2.40e-49 |
|
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: 177.41 E-value: 2.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 354 WFGYICAILMFAVTLIQSFCLQSYFQHCFVLGMCVRTTVMSSIYKKALTLSNLARKQYTIGETVNLMSVDSQKLMDATNY 433
Cdd:cd18593 37 TEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 434 MQLVWSSVIQITLSIFFLWRELGPSILAGVGVMVLLIPVNGVLATKIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAW 513
Cdd:cd18593 117 LHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAW 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 514 EPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQITPILVSVVTFSVYVLVDsaNVLNAEKAFTSITLFNILRFPLSM-L 592
Cdd:cd18593 197 EKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLG--NILTAERVFVTMALYNAVRLTMTLfF 274
|
250
....*....|....*..
gi 3219824 593 PMVTSSILQASVSVDRL 609
Cdd:cd18593 275 PFAIQFGSELSVSIRRI 291
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1060-1525 |
6.82e-49 |
|
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: 187.25 E-value: 6.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1060 ILRAPMRFFDTTPTGRIVNRFSgDISTVDDLLPQTLRS-----WMMcffgIAGTLVMICMATPVFAIIIIPLSIlYISVQ 1134
Cdd:TIGR01193 239 LFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSlfldmWIL----VIVGLFLVRQNMLLFLLSLLSIPV-YAVII 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1135 VFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQ-RFLAWNEKQIDINQKCVFSWITSNRWLAIR--LELVG 1211
Cdd:TIGR01193 313 ILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAeRYSKIDSEFGDYLNKSFKYQKADQGQQAIKavTKLIL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1212 NLVVFCSALLLVIYRKTLTGDVVGFvlsNAL--NITQTLNWLVRMTSEAETNIVAVERISEYINVENEapWVTDKRPPAD 1289
Cdd:TIGR01193 393 NVVILWTGAYLVMRGKLTLGQLITF---NALlsYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSE--FINKKKRTEL 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1290 WPRHGEIQFNN--YQVRYRPEldlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLH 1367
Cdd:TIGR01193 468 NNLNGDIVINDvsYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1368 DLRERLTIIPQDPILFSGSLRMNLDPFNK--YSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGR 1445
Cdd:TIGR01193 545 TLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALAR 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1446 AVLRKSKILVLDEATAAVDLETDSLIQTTIRKeFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSFY 1525
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYA 703
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1219-1524 |
8.80e-48 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 181.37 E-value: 8.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1219 ALLLVIY-------RKTLTGDVVGFVLSNALNITQTLNWLVRMTSEAETNIVAVERISEYINVENEAPWVTDKRPPADwp 1291
Cdd:PRK11176 262 ALAFVLYaasfpsvMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKRVIERAK-- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1292 rhGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRE 1371
Cdd:PRK11176 340 --GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1372 RLTIIPQDPILFSGSLRMNLD--PFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLR 1449
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1450 KSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSF 1524
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1287-1503 |
2.75e-44 |
|
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: 169.77 E-value: 2.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1287 PADWPRHGEIQFNNYQVRYrPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGL 1366
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1367 HDLRERLTIIPQDPILFSGSLRMNLDPFNKY-SDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGR 1445
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1446 AVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVL 1503
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1291-1508 |
3.94e-44 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 160.33 E-value: 3.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1291 PRH--GEIQFNNYQVRYRPELD-LVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGidvASIGLH 1367
Cdd:cd03248 5 PDHlkGIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG---KPISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1368 D---LRERLTIIPQDPILFSGSLRMNLD-PFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCL 1443
Cdd:cd03248 82 EhkyLHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1444 GRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKI 1508
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
633-849 |
2.01e-43 |
|
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: 158.16 E-value: 2.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDlEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAY 699
Cdd:cd03254 3 IEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 700 VPQQSWIQNGTIKDNILFGSEYN-EKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIY 778
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 779 ILDDPLSAVDAHVGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKG 849
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
633-855 |
4.47e-43 |
|
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: 157.39 E-value: 4.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAY 699
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 700 VPQQSWIQNGTIKDNILFG-SEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIY 778
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 779 ILDDPLSAVDAHVGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFARNW 855
Cdd:cd03251 161 ILDEATSALDTESERLVQAAL---ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
633-856 |
7.90e-43 |
|
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: 156.62 E-value: 7.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLEaTIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAY 699
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 700 VPQQSWIQNGTIKDNILFGS-EYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIY 778
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 779 ILDDPLSAVDAHVGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFARNWK 856
Cdd:cd03253 160 LLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1262-1525 |
8.24e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 166.15 E-value: 8.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1262 IVAVERISEYINVENEAPWVTDKRPPADwprHGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTN 1341
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAAD---QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1342 CLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNL---DPfnKYSDEEVWRALELAHLRSFVSGL 1418
Cdd:PRK11160 385 LLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLEDD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1419 QlGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSD 1498
Cdd:PRK11160 463 K-GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFD 541
|
250 260
....*....|....*....|....*..
gi 3219824 1499 KIMVLDNGKIVEYGSPEELLSNRGSFY 1525
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1262-1527 |
9.92e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 166.17 E-value: 9.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1262 IVAVERISEYINVENEAPWVTDKRPPADWPRhgEIQFNNYQVrYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTN 1341
Cdd:PRK11174 318 VGAAESLVTFLETPLAHPQQGEKELASNDPV--TIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1342 CLFRILeSAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNLDPFNK-YSDEEVWRALELAHLRSFVSGLQL 1420
Cdd:PRK11174 395 ALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1421 GLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKI 1500
Cdd:PRK11174 474 GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQI 553
|
250 260
....*....|....*....|....*..
gi 3219824 1501 MVLDNGKIVEYGSPEELLSNRGSFYLM 1527
Cdd:PRK11174 554 WVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
633-833 |
1.51e-42 |
|
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: 153.31 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAY 699
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 700 VPQQSWIQNGTIKDNIlfgseynekkyqqvlkacallpdleilpggdmaeigekginLSGGQKQRVSLARAAYQDADIYI 779
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3219824 780 LDDPLSAVDAHVGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKG 833
Cdd:cd03228 120 LDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1073-1491 |
1.12e-40 |
|
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: 159.06 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1073 TGRIVNRFSGDISTVDDLLPQTLrswmmcfFGIAGTLVMICMATPVFAIIIIPLSIL---YISVQVFYV-ATSRQLRRLD 1148
Cdd:TIGR02868 109 RGDLLGRLGADVDALQDLYVRVI-------VPAGVALVVGAAAVAAIAVLSVPAALIlaaGLLLAGFVApLVSLRAARAA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1149 SVTKSPIYSHFSETVT----GLPIIRAFEHQQRFLAwnekQIDINQKcvfSWIT----SNRWLAIR---LELVGNLVVFc 1217
Cdd:TIGR02868 182 EQALARLRGELAAQLTdaldGAAELVASGALPAALA----QVEEADR---ELTRaerrAAAATALGaalTLLAAGLAVL- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1218 sALLLVIYRKTLTGDVVG-----FVLSnALNITQTLNWLVRMTSEAETNIVAVERISEYINVENEAPWVTDKRPPADWPR 1292
Cdd:TIGR02868 254 -GALWAGGPAVADGRLAPvtlavLVLL-PLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1293 HGEIQFNNYQVRYrPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRER 1372
Cdd:TIGR02868 332 KPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1373 LTIIPQDPILFSGSLRMNLDPFNK-YSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKS 1451
Cdd:TIGR02868 411 VSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADA 490
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 3219824 1452 KILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRL 1491
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
975-1245 |
1.93e-40 |
|
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: 151.26 E-value: 1.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 975 ILFIILFYGLNNVAFIGSNLWLSAWTsdsDNLNGTNNSSSHRDMRI-GVFGALGLAQGICLLISTLWSIYACRNASKALH 1053
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRIL---DVLLPDGDPETQALNVYsLALLLLGLAQFILSFLQSYLLNHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1054 GQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAIIIIPLSILYISV 1133
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1134 QVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWITSNRWLAIRLELVGNL 1213
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*
gi 3219824 1214 VVFCSALL---LVIYRKTLTGDVVGFVLSNALNIT 1245
Cdd:pfam00664 238 SYALALWFgayLVISGELSVGDLVAFLSLFAQLFG 272
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
632-839 |
7.95e-38 |
|
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: 141.96 E-value: 7.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 632 AVKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTA------------- 698
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqldpadlrrnig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 699 YVPQQSWIQNGTIKDNILFGSEY-NEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADI 777
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 778 YILDDPLSAVDAHVGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKG 839
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
632-830 |
2.79e-37 |
|
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: 148.59 E-value: 2.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 632 AVKFSEASFTwDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST-------------A 698
Cdd:TIGR02857 321 SLEFSGVSVA-YPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadadswrdqiA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 699 YVPQQSWIQNGTIKDNILFG-SEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADI 777
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLArPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3219824 778 YILDDPLSAVDAHVGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVL 830
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
633-856 |
5.49e-37 |
|
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: 139.98 E-value: 5.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWD--PDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST------------- 697
Cdd:cd03249 1 IEFKNVSFRYPsrPDVPI-LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlnlrwlrsqi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 698 AYVPQQSWIQNGTIKDNILFGSEY-NEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDAD 776
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 777 IYILDDPLSAVDAHVGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFARNWK 856
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEAL---DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
633-840 |
6.01e-36 |
|
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: 136.47 E-value: 6.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAY 699
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 700 VPQQSWIQNGTIKDNILFGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYI 779
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 780 LDDPLSAVDAHVGKHIfNKVVGPNglLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGS 840
Cdd:cd03244 163 LDEATASVDPETDALI-QKTIREA--FKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
653-853 |
6.36e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 145.76 E-value: 6.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 653 VNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMeNVHGHITIQGS-------TAYVPQQSWI-QN-----GTIKDNILFG- 718
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIelreldpESWRKHLSWVgQNpqlphGTLRDNVLLGn 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 719 SEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNK 798
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 799 VvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFAR 853
Cdd:PRK11174 528 L---NAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFAT 579
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
305-853 |
5.12e-35 |
|
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: 144.50 E-value: 5.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 305 WLIKSLFKTFHVVILKSFILKLIHDLLVflnPQLLKLLIGFVKssnsyvwFGYICAILMFAV-TLIQSFCLQ-------- 375
Cdd:TIGR01193 160 NIVIAAIIVTLISIAGSYYLQKIIDTYI---PHKMMGTLGIIS-------IGLIIAYIIQQIlSYIQIFLLNvlgqrlsi 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 376 ----SYFQHCFVLGMCVRTTvmssiykkaltlsnlaRKqytIGETVNLMSvDSQKLMDATnymqlvwSSVIqitLSIFF- 450
Cdd:TIGR01193 230 diilSYIKHLFELPMSFFST----------------RR---TGEIVSRFT-DASSIIDAL-------ASTI---LSLFLd 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 451 LWRELGPSILAGVGVMVLLIPVngVLATKIRNIQVQNMKNKDKRLK--------IMN----EILSGIKILKYFAWEPSFQ 518
Cdd:TIGR01193 280 MWILVIVGLFLVRQNMLLFLLS--LLSIPVYAVIIILFKRTFNKLNhdamqanaVLNssiiEDLNGIETIKSLTSEAERY 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 519 EQVQGIRKKELKNLLRFG---QLQSLLIFILQITPILVSVVTFSVYVLvdsANVLNAEKAFTSITLFNILRFPLSMLPMV 595
Cdd:TIGR01193 358 SKIDSEFGDYLNKSFKYQkadQGQQAIKAVTKLILNVVILWTGAYLVM---RGKLTLGQLITFNALLSYFLTPLENIINL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 596 TSSILQASVSVDRL-ERYL-GGDDLDTSAIRRVSNFDKAVKFSEASFTWDPDLEAtIQDVNLDIKPGQLVAVVGTVGSGK 673
Cdd:TIGR01193 435 QPKLQAARVANNRLnEVYLvDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNI-LSDISLTIKMNSKTTIVGMSGSGK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 674 SSLVSAMLGEMENVHGHITIQG-------------STAYVPQQSWIQNGTIKDNILFGSEYNEKKyQQVLKACALLP--- 737
Cdd:TIGR01193 514 STLAKLLVGFFQARSGEILLNGfslkdidrhtlrqFINYLPQEPYIFSGSILENLLLGAKENVSQ-DEIWAACEIAEikd 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 738 DLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVGpnglLAGKTRIFVTHG 817
Cdd:TIGR01193 593 DIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN----LQDKTIIFVAHR 668
|
570 580 590
....*....|....*....|....*....|....*.
gi 3219824 818 IHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFAR 853
Cdd:TIGR01193 669 LSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
975-1272 |
1.61e-34 |
|
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: 135.70 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 975 ILFIILFYGLNNVAFIGSNLWLSAWTSDSDNLNGTNNSS-------SHRD------MRIGV---FGALGLAQGIcLLIST 1038
Cdd:cd18600 19 VLILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSntyavivTFTSsyyvfyIYVGVadsLLAMGFFRGL-PLVHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1039 LWSIyacrnaSKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPV 1118
Cdd:cd18600 98 LITV------SKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1119 FAIIIIPLSILYISVQVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWIT 1198
Cdd:cd18600 172 IFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLS 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1199 SNRWLAIRLELVgnLVVFCSALLLVIYRKTLTGD-VVGFVLSNALNITQTLNWLVRMTSEAETNIVAVERISEYI 1272
Cdd:cd18600 252 TLRWFQMRIEMI--FVIFFTAVTFISIGTTGDGEgRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRIFKFI 324
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1296-1508 |
1.84e-34 |
|
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: 130.41 E-value: 1.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTI 1375
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDPILFSGSLRMNLdpfnkysdeevwralelahlrsfvsglqlgllsevteggdnLSIGQRQLLCLGRAVLRKSKILV 1455
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1456 LDEATAAVDLETDSLIQTTIRK-EFSQCTVITIAHRLHTIMDSDKIMVLDNGKI 1508
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
469-1525 |
2.38e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 144.40 E-value: 2.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 469 LIPVNGVLATKIRNIQVQ-NMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQ 547
Cdd:PTZ00265 209 LIYICGVICNKKVKINKKtSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMIN 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 548 iTPILVSVVT---FSVYVLVDSANVLNAEKAFTSITLFNIL------RFPLSM-LPMVTSSI--LQASVSVDRL--ERYL 613
Cdd:PTZ00265 289 -GFILASYAFgfwYGTRIIISDLSNQQPNNDFHGGSVISILlgvlisMFMLTIiLPNITEYMksLEATNSLYEIinRKPL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 614 GGDDLDTSAIRRVsnfdKAVKFSEASFTWDPDLEATI-QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHIT 692
Cdd:PTZ00265 368 VENNDDGKKLKDI----KKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 693 IQGS--------------TAYVPQQSWIQNGTIKDNILFG-----------SEYNEKKYQ-------------------- 727
Cdd:PTZ00265 444 INDShnlkdinlkwwrskIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsNYYNEDGNDsqenknkrnscrakcagdln 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 728 ------------QVLKACALLPDLEI---------------LPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYIL 780
Cdd:PTZ00265 524 dmsnttdsneliEMRKNYQTIKDSEVvdvskkvlihdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILIL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 781 DDPLSAVDaHVGKHIFNKVVgpNGLLAGKTRI--FVTHGIHFLPQVDEIVVL---------------------------- 830
Cdd:PTZ00265 604 DEATSSLD-NKSEYLVQKTI--NNLKGNENRItiIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnk 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 831 ----GKGT---------------ILEKGSYRDLL-DKKGVFarnwKTFMKHSGPEGEATVNNDSEAEDDDDGLIPTMEEI 890
Cdd:PTZ00265 681 nnkdDNNNnnnnnnnkinnagsyIIEQGTHDALMkNKNGIY----YTMINNQKVSSKKSSNNDNDKDSDMKSSAYKDSER 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 891 ---PEDAASLAMRRENSLRRTLSRSSRSSSRRGKSLKNSLKIKNvNVLKEKEKEVEGQKLIKKEFVETGKVKFSIYLKYL 967
Cdd:PTZ00265 757 gydPDEMNGNSKHENESASNKKSCKMSDENASENNAGGKLPFLR-NLFKRKPKAPNNLRIVYREIFSYKKDVTIIALSIL 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 968 QAVGWWSiLFIILFYGLNNVAFigsnlwlsawtsDSDNLNGTNNSSSHRDMRIGvfgalglaqgICLLIS-TLWSIY--- 1043
Cdd:PTZ00265 836 VAGGLYP-VFALLYAKYVSTLF------------DFANLEANSNKYSLYILVIA----------IAMFISeTLKNYYnnv 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1044 ACRNASKALHGQLLTNILRAPMRFFDT---TPtGRIVNRFSGDISTVDDLLPQTL---RSWMMCFFGiagTLVMICMATP 1117
Cdd:PTZ00265 893 IGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIvifTHFIVLFLV---SMVMSFYFCP 968
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1118 VFAIIIIplSILYISVQVFYV----ATSRQLRRL--------------DSVTKSPIYShFSETVTGLPIIRAFEHQQRFL 1179
Cdd:PTZ00265 969 IVAAVLT--GTYFIFMRVFAIrarlTANKDVEKKeinqpgtvfaynsdDEIFKDPSFL-IQEAFYNMNTVIIYGLEDYFC 1045
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1180 AWNEKQIDINQKCVFSWITSNRWL---AIRLELVGNLVVFCSALLLvIYRKTLTGDVVGFVLSNALNITQTLNWLVRMTS 1256
Cdd:PTZ00265 1046 NLIEKAIDYSNKGQKRKTLVNSMLwgfSQSAQLFINSFAYWFGSFL-IRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKG 1124
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1257 EAETNIVAVERI------SEYINVENEAPWVTDKRPPADwprhGEIQFNNYQVRY--RPELDlVLKGITCNIKSGEKVGV 1328
Cdd:PTZ00265 1125 DSENAKLSFEKYypliirKSNIDVRDNGGIRIKNKNDIK----GKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAI 1199
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1329 VGRTGAGKSSLTNCLFRILE------------------------------------------------------SAGGQI 1354
Cdd:PTZ00265 1200 VGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKI 1279
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1355 IIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNLDpFNK--YSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDN 1432
Cdd:PTZ00265 1280 LLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKedATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKS 1358
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1433 LSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIR--KEFSQCTVITIAHRLHTIMDSDKIMVLDN----G 1506
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtG 1438
|
1290 1300
....*....|....*....|
gi 3219824 1507 KIVE-YGSPEELLSNRGSFY 1525
Cdd:PTZ00265 1439 SFVQaHGTHEELLSVQDGVY 1458
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
318-589 |
8.29e-34 |
|
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: 132.00 E-value: 8.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 318 ILKSFILKLIHDLLVFLNPQLLKLLIGFVKSSNSYVWF-GYICAILMFAVTLIQSFC--LQSYFQHcfVLGMCVRTTVMS 394
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQaLNVYSLALLLLGLAQFILsfLQSYLLN--HTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 395 SIYKKALTLSNLARKQYTIGETVNLMSVDSQKLMDATNYMQLVWSSVIQITLSIFFLWRELGPSI-LAGVGVMVLLIPVN 473
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 474 GVLATKIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLRFGQLQSLLIFILQ-ITPIL 552
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQfIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 3219824 553 VSVVTFSVYVLVDSaNVLNAEKAFTSITLFNILRFPL 589
Cdd:pfam00664 239 YALALWFGAYLVIS-GELSVGDLVAFLSLFAQLFGPL 274
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
630-835 |
1.48e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.21 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 630 DKAVKFSEASFTWDPdlEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST--------AYVP 701
Cdd:COG1121 4 MPAIELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprrarrriGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 702 QQSWIQNG---TIKDNILFG--------SEYNEKKYQQVLKACALLpdleilpggDMAEIGEKGIN-LSGGQKQRVSLAR 769
Cdd:COG1121 82 QRAEVDWDfpiTVRDVVLMGrygrrglfRRPSRADREAVDEALERV---------GLEDLADRPIGeLSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 770 AAYQDADIYILDDPLSAVDAHVGKHIFNkvvgpngLLA-----GKTRIFVTHGIHFLPQ-VDEIVVLGKGTI 835
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
633-853 |
2.91e-33 |
|
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: 129.14 E-value: 2.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAY 699
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 700 VPQQSWIQNGTIKDNILFGSEynEKKYQQVLKACALLPDLEI---LPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDAD 776
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADP--GMSMERVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 777 IYILDDPLSAVDAHVGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFAR 853
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1301-1525 |
5.93e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 135.42 E-value: 5.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1301 YQVRYRPELDlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIG---LHDLRERLTIIP 1377
Cdd:COG1123 270 YPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1378 QDPilfSGSL--RMN--------LDPFNKYSDEEVW-RALELahLRSFvsGLQLGLLS----EvteggdnLSIGQRQLLC 1442
Cdd:COG1123 349 QDP---YSSLnpRMTvgdiiaepLRLHGLLSRAERReRVAEL--LERV--GLPPDLADryphE-------LSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1443 LGRAVLRKSKILVLDEATAAVDLetdsLIQTTI-------RKEFsQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSP 1514
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDV----SVQAQIlnllrdlQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
250
....*....|.
gi 3219824 1515 EELLSNRGSFY 1525
Cdd:COG1123 490 EEVFANPQHPY 500
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1296-1512 |
2.28e-32 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 124.73 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGlHDLRERLTI 1375
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDPILFSGSLRMNLdpfnkysdeevwralelahlrsfvsglqlgllsevtegGDNLSIGQRQLLCLGRAVLRKSKILV 1455
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1456 LDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYG 1512
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1312-1519 |
4.11e-32 |
|
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: 133.72 E-value: 4.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNL 1391
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1392 DPFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLI 1471
Cdd:COG4618 427 ARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 3219824 1472 QTTIR--KEfSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:COG4618 507 AAAIRalKA-RGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1261-1540 |
1.91e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 131.76 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1261 NIV-----AVERISEYINvenEAPWVTDKRPPADWPRhGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAG 1335
Cdd:PRK10789 278 NIVergsaAYSRIRAMLA---EAPVVKDGSEPVPEGR-GELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1336 KSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNL---DPfnKYSDEEVWRALELAHLR 1412
Cdd:PRK10789 354 KSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVH 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1413 SFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLH 1492
Cdd:PRK10789 432 DDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLS 511
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1493 TIMDSDKIMVLDNGKIVEYGSPEELLSNRGSFYLMAK----EAGIENVNHTE 1540
Cdd:PRK10789 512 ALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRyqqlEAALDDAPEIR 563
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1296-1512 |
7.39e-31 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 121.84 E-value: 7.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLV--LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRER- 1372
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1373 --LTIIPQDPIlfsGSL--RMN-----LDPFNKYSDEEVWRALELAHLRSFVsglQLGLLSEV-----TEggdnLSIGQR 1438
Cdd:cd03257 82 keIQMVFQDPM---SSLnpRMTigeqiAEPLRIHGKLSKKEARKEAVLLLLV---GVGLPEEVlnrypHE----LSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1439 QLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRK---EFsQCTVITIAHRLHTI-MDSDKIMVLDNGKIVEYG 1512
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeEL-GLTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1312-1522 |
1.49e-30 |
|
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: 121.50 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHdLRERLTIIPQDPILFSG-SLRMN 1390
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1391 LD---PFNKYSDEEV-WRALELAHLrsfvsglqLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLE 1466
Cdd:COG4555 95 IRyfaELYGLFDEELkKRIEELIEL--------LGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1467 TdsliQTTIRKEFSQC-----TVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSNRG 1522
Cdd:COG4555 167 A----RRLLREILRALkkegkTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1262-1519 |
1.89e-30 |
|
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: 128.23 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1262 IVAVERISEYINVENEapwvtdKRPPADWPR-HGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLT 1340
Cdd:TIGR01842 288 RQAYKRLNELLANYPS------RDPAMPLPEpEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1341 NCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNLDPFNKYSD-EEVWRALELAHLRSFVSGLQ 1419
Cdd:TIGR01842 362 RLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADpEKIIEAAKLAGVHELILRLP 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1420 LGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETD-SLIQTTIRKEFSQCTVITIAHRLHTIMDSD 1498
Cdd:TIGR01842 442 DGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEqALANAIKALKARGITVVVITHRPSLLGCVD 521
|
250 260
....*....|....*....|.
gi 3219824 1499 KIMVLDNGKIVEYGSPEELLS 1519
Cdd:TIGR01842 522 KILVLQDGRIARFGERDEVLA 542
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
632-853 |
3.58e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 127.63 E-value: 3.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 632 AVKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STA 698
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 699 YVPQQSWIQNGTIKDNILFGS-EYNEKKYQQVLKACALLPDLEILPGGDmAEIGEKGINLSGGQKQRVSLARAAYQDADI 777
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGLEKLLEDDKGLN-AWLGEGGRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 778 YILDDPLSAVDAHVGKHIFNkvvgpngLL----AGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFAR 853
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1296-1519 |
6.37e-30 |
|
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: 120.15 E-value: 6.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELdlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTI 1375
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDPIL-FSGSLR----M----NLDPFNKYSDEE---VWRALE---LAHL--RSFvsglqlgllsevteggDNLSIGQR 1438
Cdd:COG1120 80 VPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALErtgLEHLadRPV----------------DELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1439 QLLCLGRAVLRKSKILVLDEATAAVDL----ETDSLIQTTIRKEfsQCTVITIAHRL-HTIMDSDKIMVLDNGKIVEYGS 1513
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGP 221
|
....*.
gi 3219824 1514 PEELLS 1519
Cdd:COG1120 222 PEEVLT 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
414-852 |
1.38e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 127.15 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 414 GETVNLMSVDSQKLMD--ATNYMQLVWSSVIQITLSIFFLWreLGPSIlagvgVMVLLIPVNGV-LATKIRNIQVQNMKN 490
Cdd:TIGR00958 258 GELTSRLSSDTQTMSRslSLNVNVLLRNLVMLLGLLGFMLW--LSPRL-----TMVTLINLPLVfLAEKVFGKRYQLLSE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 491 K-----DKRLKIMNEILSGIKILKYFAWEPS----FQEQVQGI----RKKELKNLLRF--GQLQSLLIF--ILQITPILV 553
Cdd:TIGR00958 331 ElqeavAKANQVAEEALSGMRTVRSFAAEEGeasrFKEALEETlqlnKRKALAYAGYLwtTSVLGMLIQvlVLYYGGQLV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 554 --------SVVTFSVYVLVDSANVLNaekaftsitlfnilrfplsmLPMVTSSILQASVSVDRLERYLGGD-DLDTSAIR 624
Cdd:TIGR00958 411 ltgkvssgNLVSFLLYQEQLGEAVRV--------------------LSYVYSGMMQAVGASEKVFEYLDRKpNIPLTGTL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 625 RVSNFDKAVKFSEASFTWD--PDLEaTIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------- 695
Cdd:TIGR00958 471 APLNLEGLIEFQDVSFSYPnrPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqyd 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 696 ------STAYVPQQSWIQNGTIKDNILFGSEYNEK-KYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLA 768
Cdd:TIGR00958 550 hhylhrQVALVGQEPVLFSGSVRENIAYGLTDTPDeEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 769 RAAYQDADIYILDDPLSAVDAHVgkhifNKVVGPNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKK 848
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
....
gi 3219824 849 GVFA 852
Cdd:TIGR00958 705 GCYK 708
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1313-1461 |
1.68e-29 |
|
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: 115.44 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSG-SLRMNL 1391
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1392 -------DPFNKYSDEEVWRALELAhlrsfvsGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATA 1461
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
650-833 |
1.92e-29 |
|
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: 117.25 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST--------AYVPQQS---WIQNGTIKDNIL-- 716
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlekerkriGYVPQRRsidRDFPISVRDVVLmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 717 ------FGSEYNEKKYQQVLKAcallpdLEILPGGDMAE--IGEkginLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:cd03235 95 lyghkgLFRRLSKADKAKVDEA------LERVGLSELADrqIGE----LSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3219824 789 AHVGKHIFnkvvgpnGLLA-----GKTRIFVTHGIH-FLPQVDEIVVLGKG 833
Cdd:cd03235 165 PKTQEDIY-------ELLRelrreGMTILVVTHDLGlVLEYFDRVLLLNRT 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1302-1507 |
2.50e-29 |
|
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: 115.03 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1302 QVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQdpi 1381
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1382 lfsgslrmnldpfnkysdeevwralelahlrsfvsglqlgllsevteggdnLSIGQRQLLCLGRAVLRKSKILVLDEATA 1461
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 3219824 1462 AVDLETDSLIQTTIRKEFSQ-CTVITIAHRLHTIMD-SDKIMVLDNGK 1507
Cdd:cd00267 110 GLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1296-1519 |
2.57e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 117.98 E-value: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDL--VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERL 1373
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1374 TIIPQDPIlfsGSL--RMNLD-----PFN----KYSDEEVWRALELAhlrsfvsGLQLGLLS----EvteggdnLSIGQR 1438
Cdd:COG1124 82 QMVFQDPY---ASLhpRHTVDrilaePLRihglPDREERIAELLEQV-------GLPPSFLDryphQ-------LSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1439 QLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQ---TTIRKEFsQCTVITIAHRLHTI--MdSDKIMVLDNGKIVEYGS 1513
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILnllKDLREER-GLTYLFVSHDLAVVahL-CDRVAVMQNGRIVEELT 222
|
....*.
gi 3219824 1514 PEELLS 1519
Cdd:COG1124 223 VADLLA 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
292-852 |
6.72e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 123.98 E-value: 6.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 292 KKSEKTTKDYPKSWLIKSLFKTFHVVILKSFILKLIHDLLVFlnpQLLKLLI--GFVKSSNSY-VWFGYICAILMF---A 365
Cdd:PRK11176 4 DKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFML---SLLKPLLddGFGKADRSVlKWMPLVVIGLMIlrgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 366 VTLIQSFCL------------QSYFQHcfVLGMCVrttvmsSIYKKALTLSNLARKQYtigetvnlmsvDSQKLMDATNy 433
Cdd:PRK11176 81 TSFISSYCIswvsgkvvmtmrRRLFGH--MMGMPV------SFFDKQSTGTLLSRITY-----------DSEQVASSSS- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 434 mqlvwSSVIQITlsifflwRElGPSILAGVGVM-----------VLLIPVNGVL----ATKIRNIQvQNMKNKDKRLKIM 498
Cdd:PRK11176 141 -----GALITVV-------RE-GASIIGLFIMMfyyswqlslilIVIAPIVSIAirvvSKRFRNIS-KNMQNTMGQVTTS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 499 NE-ILSGIKILKYFAwepsfQEQVQGIRKKELKNLLRfgqLQSLLIFILQIT--PILVSVVTFSVYVLVDSANVLNAEKA 575
Cdd:PRK11176 207 AEqMLKGHKEVLIFG-----GQEVETKRFDKVSNRMR---QQGMKMVSASSIsdPIIQLIASLALAFVLYAASFPSVMDT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 576 FT--SIT-----LFNILRfPLSMLPMVTSSILQASVSVDRLERYLggdDLDT---SAIRRVSNFDKAVKFSEASFTWDPD 645
Cdd:PRK11176 279 LTagTITvvfssMIALMR-PLKSLTNVNAQFQRGMAACQTLFAIL---DLEQekdEGKRVIERAKGDIEFRNVTFTYPGK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 646 LEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAYVPQQSWIQNGTIK 712
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQNVHLFNDTIA 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 713 DNILFGSE--YNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAH 790
Cdd:PRK11176 435 NNIAYARTeqYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 791 VGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFA 852
Cdd:PRK11176 515 SERAIQAAL---DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1296-1507 |
8.55e-29 |
|
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: 115.26 E-value: 8.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRP---ELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGidvasiglhdlreR 1372
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1373 LTIIPQDPILFSGSLRMNL---DPFNKysdEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLR 1449
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1450 KSKILVLDEATAAVDLET-DSLIQTTIRKEFSQC-TVITIAHRLHTIMDSDKIMVLDNGK 1507
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1312-1512 |
1.96e-28 |
|
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: 113.30 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQdpILfsgslrmnl 1391
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--AL--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1392 dpfnkysdeEVWRALELAHlRSFvsglqlgllsevteggDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL----ET 1467
Cdd:cd03214 83 ---------ELLGLAHLAD-RPF----------------NELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 3219824 1468 DSLIQTTIRKEfsQCTVITIAHRL-HTIMDSDKIMVLDNGKIVEYG 1512
Cdd:cd03214 137 LELLRRLARER--GKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1296-1520 |
3.96e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 120.78 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAG---GQIIIDGIDVASIGLHDLRER 1372
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1373 LTIIPQDPilfsgslRMNLDPFNkySDEEVWRALEL-----AHLRSFVSGL--QLGLLSEVTEGGDNLSIGQRQLLCLGR 1445
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVT--VGDQIAEALENlglsrAEARARVLELleAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1446 AVLRKSKILVLDEATAAVDLETDSLIQTTIRK--EFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1297-1507 |
5.42e-28 |
|
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: 112.95 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1297 QFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTII 1376
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1377 PQDP------------ILFsgSLRmNLdpfnKYSDEEVWRALELAhLRSFvsGLQlGLLSEVTEggdNLSIGQRQLLCLG 1444
Cdd:cd03225 81 FQNPddqffgptveeeVAF--GLE-NL----GLPEEEIEERVEEA-LELV--GLE-GLRDRSPF---TLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 1445 RAVLRKSKILVLDEATAAVDLETDSLIQTTIrKEFSQC--TVITIAHRLHTIMD-SDKIMVLDNGK 1507
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
588-856 |
7.87e-28 |
|
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: 121.08 E-value: 7.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 588 PLSMLPMVTSSILQASVSVDRLERYLG-----GDDLDTSAIRrVSnfDKAVKFSEASFTWDPDLEAtIQDVNLDIKPGQL 662
Cdd:COG5265 311 PLNFLGFVYREIRQALADMERMFDLLDqppevADAPDAPPLV-VG--GGEVRFENVSFGYDPERPI-LKGVSFEVPAGKT 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 663 VAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAYVPQQSWIQNGTIKDNILFGS-EYNEKKYQQ 728
Cdd:COG5265 387 VAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaslraAIGIVPQDTVLFNDTIAYNIAYGRpDASEEEVEA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 729 VLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHI---FNKVVgpngl 805
Cdd:COG5265 467 AARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIqaaLREVA----- 541
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 3219824 806 lAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVFARNWK 856
Cdd:COG5265 542 -RGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWA 591
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
639-835 |
1.05e-27 |
|
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: 111.15 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 639 SFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST-------------AYVPQQSW 705
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisqwdpnelgdhvGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 706 IQNGTIKDNIlfgseynekkyqqvlkacallpdleilpggdmaeigekginLSGGQKQRVSLARAAYQDADIYILDDPLS 785
Cdd:cd03246 87 LFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 3219824 786 AVDaHVGKHIFNKVVGpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTI 835
Cdd:cd03246 126 HLD-VEGERALNQAIA-ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
575-816 |
1.13e-27 |
|
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: 119.77 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 575 AFTSITLFNilrfPLSMLPMVTSSILQASVSVDRLERYL----GGDDLDTSAIRRVSNFDKAVKFSEASFTWDPDLEAtI 650
Cdd:TIGR02868 277 VLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVLdaagPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPV-L 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTA-------------YVPQQSWIQNGTIKDNILF 717
Cdd:TIGR02868 352 DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVssldqdevrrrvsVCAQDAHLFDTTVRENLRL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 GS-EYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIF 796
Cdd:TIGR02868 432 ARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL 511
|
250 260
....*....|....*....|
gi 3219824 797 NKVVGPnglLAGKTRIFVTH 816
Cdd:TIGR02868 512 EDLLAA---LSGRTVVLITH 528
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
639-849 |
3.22e-27 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 118.66 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 639 SFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQ-------------GSTAYVPQQSW 705
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 706 IQNGTIKDNILFGS-EYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPL 784
Cdd:PRK10789 400 LFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 785 SAVDAHVGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKG 849
Cdd:PRK10789 480 SAVDGRTEHQILHNL---RQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
624-853 |
9.67e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 117.37 E-value: 9.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 624 RRVSNFDKAVKFSEASFTWDPDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------- 695
Cdd:PRK13657 326 IDLGRVKGAVEFDDVSFSYDNSRQG-VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtr 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 696 -----STAYVPQQSWIQNGTIKDNILFGSE-YNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLAR 769
Cdd:PRK13657 405 aslrrNIAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 770 AAYQDADIYILDDPLSAVDAHVGKHIFNKVvgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKG 849
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAAL---DELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
....
gi 3219824 850 VFAR 853
Cdd:PRK13657 562 RFAA 565
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
650-785 |
1.51e-26 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 106.96 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST-------------AYVPQQSWIQNG-TIKDNI 715
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkeiGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 716 LFGSE----YNEKKYQQVLKAcallpdLEILPGGDMAE--IGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLS 785
Cdd:pfam00005 81 RLGLLlkglSKREKDARAEEA------LEKLGLGDLADrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1312-1517 |
2.35e-26 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 108.81 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILES-----AGGQIIIDGIDVASIGLHD--LRERLTIIPQDPILFS 1384
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVleLRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1385 GSLRMNLD--------PFNKYSDEEVWRALELAhlrsfvsglqlGLLSEVTE--GGDNLSIGQRQLLCLGRAVLRKSKIL 1454
Cdd:cd03260 95 GSIYDNVAyglrlhgiKLKEELDERVEEALRKA-----------ALWDEVKDrlHALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1455 VLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEEL 1517
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
648-835 |
1.13e-25 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 113.69 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 648 ATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTA-------------YVPQQSWIQNGTIKDN 714
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdreelgrhigYLPQDVELFDGTIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 715 I-LFGSEYNEKkyqqVLKACAL---------LPDleilpGGDmAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPL 784
Cdd:COG4618 426 IaRFGDADPEK----VVAAAKLagvhemilrLPD-----GYD-TRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 785 SAVDAhvgkhifnkvVGPNGLLA--------GKTRIFVTHGIHFLPQVDEIVVLGKGTI 835
Cdd:COG4618 496 SNLDD----------EGEAALAAairalkarGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
650-839 |
2.08e-25 |
|
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: 104.82 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITiqgstayvpqqswiqngtikdniLFGSEYNEKKYQQV 729
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL-----------------------LDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 730 LKACALLPD-LEILpggDMAEIGEKGIN-LSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVGpnglLA 807
Cdd:cd03214 72 ARKIAYVPQaLELL---GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRR----LA 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 3219824 808 ---GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKG 839
Cdd:cd03214 145 rerGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1312-1507 |
3.19e-25 |
|
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: 104.19 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLH--DLRERLTIIPQDPILFSGslrm 1389
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFPH---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1390 nldpfnkysdeevwralelahlrsfvsglqLGLLSEVTEGgdnLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDS 1469
Cdd:cd03229 91 ------------------------------LTVLENIALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 3219824 1470 LIQTTIR--KEFSQCTVITIAHRLHTIMD-SDKIMVLDNGK 1507
Cdd:cd03229 138 EVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
650-837 |
8.18e-25 |
|
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: 104.09 E-value: 8.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG--------STAYVPQQS----WIqngTIKDNILF 717
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQQDallpWL---TVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 GSEYNEKKYQQVL-KACALLpdleilpggdmAEIGEKGI------NLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAH 790
Cdd:cd03293 97 GLELQGVPKAEAReRAEELL-----------ELVGLSGFenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 791 VGKHIfnkvvgpNGLL------AGKTRIFVTHGIH---FLPqvDEIVVLGK--GTILE 837
Cdd:cd03293 166 TREQL-------QEELldiwreTGKTVLLVTHDIDeavFLA--DRVVVLSArpGRIVA 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
634-834 |
1.37e-24 |
|
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: 103.32 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 634 KFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAYV 700
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 701 PQ--QSWIQNGTIKDNILFGSEYNEKKYQQVLKAcallpDLEILPGGDMAEIGEKGI-NLSGGQKQRVSLARAAYQDADI 777
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENLGLPEEEIEER-----VEEALELVGLEGLRDRSPfTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 778 YILDDPLSAVDAHVGKHIFNKVVGPNGllAGKTRIFVTHGIHFLPQV-DEIVVLGKGT 834
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKA--EGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1312-1517 |
1.58e-24 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 103.74 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVAS---IGLHDLRERLTIIPQDPILFSG--- 1385
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRMGMLFQSGALFDSltv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1386 ------SLRMNLdpfnKYSDEEVwRALELAHLRsfvsglQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEA 1459
Cdd:cd03261 95 fenvafPLREHT----RLSEEEI-REIVLEKLE------AVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1460 TAAVD----LETDSLIQtTIRKEFsQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEEL 1517
Cdd:cd03261 164 TAGLDpiasGVIDDLIR-SLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1312-1520 |
1.74e-24 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 103.81 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLfRILES-AGGQIIIDGIDVASI---GLHDLRERLTIIPQDPILFSgsl 1387
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLERpTSGSVLVDGTDLTLLsgkELRKARRRIGMIFQHFNLLS--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1388 rmnldpfNKYSDEEVWRALELAHL-RSFVSGLQLGLLSEV--TEGGD----NLSIGQRQLLCLGRAVLRKSKILVLDEAT 1460
Cdd:cd03258 96 -------SRTVFENVALPLEIAGVpKAEIEERVLELLELVglEDKADaypaQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1461 AAVDLE-TDSLIQ--TTIRKEFSqCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:cd03258 169 SALDPEtTQSILAllRDINRELG-LTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
635-839 |
2.22e-24 |
|
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: 101.62 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 635 FSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS------------TAYVPQ 702
Cdd:cd03247 3 INNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 703 QSWIQNGTIKDNIlfgseynekkyqqvlkacallpdleilpggdmaeigekGINLSGGQKQRVSLARAAYQDADIYILDD 782
Cdd:cd03247 83 RPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 783 PLSAVDAHVGKHIFNKVVgpnGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKG 839
Cdd:cd03247 125 PTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1296-1519 |
2.46e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 103.63 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELdlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVAsiglhdlRERLTI 1375
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-------RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 --IPQD-------PILFSGSLRMNLDP----FNKYSDEE---VWRALELAHLRSFvSGLQLGLLSevtegGdnlsiGQRQ 1439
Cdd:COG1121 78 gyVPQRaevdwdfPITVRDVVLMGRYGrrglFRRPSRADreaVDEALERVGLEDL-ADRPIGELS-----G-----GQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1440 LLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQ-CTVITIAHRLHTIMD-SDKIMVLdNGKIVEYGSPEEL 1517
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEV 225
|
..
gi 3219824 1518 LS 1519
Cdd:COG1121 226 LT 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1294-1490 |
1.42e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.20 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1294 GEIQFNNYQVRyRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLtnclFRILesAG------GQIIidgidvasigLH 1367
Cdd:COG4178 361 GALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRAI--AGlwpygsGRIA----------RP 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1368 DLrERLTIIPQDPILFSGSLRMNL---DPFNKYSDEEVWRALELAHLRSFVsglqlGLLSEVTEGGDNLSIGQRQLLCLG 1444
Cdd:COG4178 424 AG-ARVLFLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHLA-----ERLDEEADWDQVLSLGEQQRLAFA 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 3219824 1445 RAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHR 1490
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
639-858 |
1.76e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 107.11 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 639 SFTWDPDlEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAYVPQQSW 705
Cdd:PRK10790 347 SFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 706 IQNGTIKDNILFGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLS 785
Cdd:PRK10790 426 VLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATA 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 786 AVDAHVGKHIfnkvvgPNGLLAGK---TRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGvfaRNWKTF 858
Cdd:PRK10790 506 NIDSGTEQAI------QQALAAVRehtTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG---RYWQMY 572
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
633-835 |
2.72e-23 |
|
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: 100.24 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWD--PDLEaTIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS--TAY--------- 699
Cdd:cd03248 12 VKFQNVTFAYPtrPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpiSQYehkylhskv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 700 --VPQQSWIQNGTIKDNILFG----SEYNEKKYQQVLKACALLPDLEIlpgGDMAEIGEKGINLSGGQKQRVSLARAAYQ 773
Cdd:cd03248 91 slVGQEPVLFARSLQDNIAYGlqscSFECVKEAAQKAHAHSFISELAS---GYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 774 DADIYILDDPLSAVDAHVGKHIFNKVVGPNgllAGKTRIFVTHGIHFLPQVDEIVVLGKGTI 835
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWP---ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1312-1508 |
2.93e-23 |
|
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: 98.24 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGlHDLRERLTIIPQDPILFSG-SLRMN 1390
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPEEPSLYENlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1391 LDpfnkysdeevwralelahlrsfvsglqlgllsevteggdnLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSL 1470
Cdd:cd03230 94 LK----------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 3219824 1471 IQTTIRKEFSQ-CTVITIAHRLHTIMD-SDKIMVLDNGKI 1508
Cdd:cd03230 134 FWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
650-846 |
3.02e-23 |
|
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: 105.76 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST----------------AYVPQ---QSWIQNGT 710
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsrrslrelrrrvQMVFQdpySSLNPRMT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 711 IKDNILFG--------SEYNEKKYQQVLKACALLPD-LEILPGGdmaeigekginLSGGQKQRVSLARAAYQDADIYILD 781
Cdd:COG1123 361 VGDIIAEPlrlhgllsRAERRERVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 782 DPLSAVDAHVGKHIFNkvvgpngLLA------GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLLD 846
Cdd:COG1123 430 EPTSALDVSVQAQILN-------LLRdlqrelGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFA 494
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
650-846 |
3.59e-23 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 100.50 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------ST-------AYVPQQSWIQNG-TIKDNI 715
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslSRrelarriAYVPQEPPAPFGlTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 716 LFG--------SEYNEKKYQQVLKACALLpdleilpggDMAEIGEKGIN-LSGGQKQRVSLARAAYQDADIYILDDPLSA 786
Cdd:COG1120 97 ALGryphlglfGRPSAEDREAVEEALERT---------GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 787 VDAHVGKHIFNkvvgpngLLA------GKTRIFVThgiHFLPQV----DEIVVLGKGTILEKGSYRDLLD 846
Cdd:COG1120 168 LDLAHQLEVLE-------LLRrlarerGRTVVMVL---HDLNLAaryaDRLVLLKDGRIVAQGPPEEVLT 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
633-845 |
3.83e-23 |
|
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: 99.71 E-value: 3.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST-------------AY 699
Cdd:COG1122 1 IELENLSFSYPGGTPA-LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkknlrelrrkvGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 700 VPQQSWIQ--NGTIKDNILFGSEyN-----EKKYQQVLKACALLpdleilpggDMAEIGEKGI-NLSGGQKQRVSLARAA 771
Cdd:COG1122 80 VFQNPDDQlfAPTVEEDVAFGPE-NlglprEEIRERVEEALELV---------GLEHLADRPPhELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 772 YQDADIYILDDPLSAVDAHVGKHIFNKVvgpNGL-LAGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLL 845
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELL---KRLnKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVF 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
650-849 |
3.99e-23 |
|
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: 99.93 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------------STAYVPQQSWI-QNGTIKDNI- 715
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLyDRLTVRENIr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 716 LFGSEYNEKKYQQVLKACALLPDLeilpggDMAEIGEKGI-NLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAhVGKH 794
Cdd:COG4555 97 YFAELYGLFDEELKKRIEELIELL------GLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MARR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 795 IFNKVvgpngLLA----GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLLDKKG 849
Cdd:COG4555 170 LLREI-----LRAlkkeGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
650-837 |
4.58e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 100.55 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST--------AYVPQQS----WIqngTIKDNILF 717
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgpgpdrGVVFQEPallpWL---TVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 G-------SEYNEKKYQQVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAH 790
Cdd:COG1116 104 GlelrgvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 791 VGKHIfnkvvgpNGLLA------GKTRIFVTHGIH---FLpqVDEIVVLGK--GTILE 837
Cdd:COG1116 173 TRERL-------QDELLrlwqetGKTVLFVTHDVDeavFL--ADRVVVLSArpGRIVE 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1312-1520 |
6.44e-23 |
|
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: 99.43 E-value: 6.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDlRERLTIIP--QDPILFSG---- 1385
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRtfQIPRLFPEltvl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1386 -----------SLRMNLDPFNKYSDEEVWRALELAHlrsfvsglQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKIL 1454
Cdd:cd03219 94 envmvaaqartGSGLLLARARREEREARERAEELLE--------RVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1455 VLDEATAAVDL-ETDSLIQ--TTIRKEfsQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:cd03219 166 LLDEPAAGLNPeETEELAEliRELRER--GITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1312-1509 |
7.70e-23 |
|
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: 96.73 E-value: 7.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHD-LRERLTIIPQdpilfsgslrmn 1390
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1391 ldpfnkysdeevwralelahlrsfvsglqlgllsevteggdnLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL-ETDS 1469
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 3219824 1470 LIQtTIRKEFSQ-CTVITIAHRLHTIMD-SDKIMVLDNGKIV 1509
Cdd:cd03216 121 LFK-VIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1312-1512 |
9.00e-23 |
|
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: 97.98 E-value: 9.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHdlRERLTIIPQDPILF-------- 1383
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFphltvaen 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 --SGsLRMNLDPfnkySDEEVWRALELAhlrsfvsgLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATA 1461
Cdd:cd03259 93 iaFG-LKLRGVP----KAEIRARVRELL--------ELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1462 AVDLETDSLIQTTIRKEFSQ--CTVITIAHRLHTIMD-SDKIMVLDNGKIVEYG 1512
Cdd:cd03259 160 ALDAKLREELREELKELQRElgITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1310-1536 |
3.55e-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: 97.02 E-value: 3.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1310 DLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVAsiGLHDLRERLTIIPQDPILF------ 1383
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFphmtvy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 ---SGSLRMNLDPfnKYSDEEvwRALELAHLrsfvsglqLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEAT 1460
Cdd:cd03299 90 kniAYGLKKRKVD--KKEIER--KVLEIAEM--------LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1461 AAVDLET-DSLIQ--TTIRKEFSqCTVITIAHRLHTI-MDSDKIMVLDNGKIVEYGSPEELLSNRGSfYLMAKEAGIENV 1536
Cdd:cd03299 158 SALDVRTkEKLREelKKIRKEFG-VTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKN-EFVAEFLGFNNI 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
650-835 |
4.40e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 96.04 E-value: 4.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAYVPQQSWIQNGTIKDNIL 716
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 717 FGSEYNEKKYQQVlKACALLPDLEiLPggdmAEIGEKGI-NLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHvGKHI 795
Cdd:COG4619 96 FPFQLRERKFDRE-RALELLERLG-LP----PDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE-NTRR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 3219824 796 FNKVVGPNGLLAGKTRIFVTHGIHFLPQV-DEIVVLGKGTI 835
Cdd:COG4619 169 VEELLREYLAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
630-840 |
5.38e-22 |
|
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: 95.56 E-value: 5.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 630 DKAVKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------S 696
Cdd:cd03369 4 HGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 697 TAYVPQQSWIQNGTIKDNILFGSEYNEKKYQQVLKacallpdleilpggdmaeIGEKGINLSGGQKQRVSLARAAYQDAD 776
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 777 IYILDDPLSAVDAHVgKHIFNKVVgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGS 840
Cdd:cd03369 146 VLVLDEATASIDYAT-DALIQKTI--REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1296-1520 |
6.51e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.37 E-value: 6.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTI 1375
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDP------------ILFsgSLRMNLDPFNKYSDeevwRALELAHlrsfvsglQLGLLSEVTEGGDNLSIGQRQLLCL 1443
Cdd:PRK13632 88 IFQNPdnqfigatveddIAF--GLENKKVPPKKMKD----IIDDLAK--------KVGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1444 GRAVLRKSKILVLDEATAAVDLETDSLIQTTIR--KEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1312-1520 |
1.04e-21 |
|
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: 95.19 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHD-LRERLTIIPQDPILFSG-SLRM 1389
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1390 NL--------DPFNKYSDEEVWRAL-ELAHLRSfvsglQLgllsevtegGDNLSIGQRQLLCLGRAVLRKSKILVLDEAT 1460
Cdd:cd03224 95 NLllgayarrRAKRKARLERVYELFpRLKERRK-----QL---------AGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1461 AAvdletdslIQTTIRKEFSQC---------TVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:cd03224 161 EG--------LAPKIVEEIFEAirelrdegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
650-839 |
1.13e-21 |
|
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: 95.27 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG----------------STAYVPQQSwiqNG---- 709
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQDP---MSslnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 710 --TIKDNIL-------FGSEYNEKKYQQVLKACALLPDLEIL---PGGdmaeigekginLSGGQKQRVSLARAAYQDADI 777
Cdd:cd03257 98 rmTIGEQIAeplrihgKLSKKEARKEAVLLLLVGVGLPEEVLnryPHE-----------LSGGQRQRVAIARALALNPKL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 778 YILDDPLSAVDAHVGKHIFNkvvgpngLLA------GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKG 839
Cdd:cd03257 167 LIADEPTSALDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
650-839 |
1.69e-21 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 94.51 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-----------STAYVPQQ-SWIQNGTIKDNILF 717
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDyALFPHLTVAENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 GSEYNEKKYQQVLKACallpdLEILPGGDMAEIGEKGIN-LSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVG---- 792
Cdd:cd03259 96 GLKLRGVPKAEIRARV-----RELLELVGLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALDAKLReelr 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3219824 793 ---KHIFNKvvgpngllAGKTRIFVTHGI-HFLPQVDEIVVLGKGTILEKG 839
Cdd:cd03259 171 eelKELQRE--------LGITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
650-847 |
1.71e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.13 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------------STAYVPQQSWIQNG-TIKDNIL 716
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 717 F-------GSEYNEKKYQQVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVDA 789
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 790 hVGKHIFNKVVgpNGLLA-GKTRIFVThgiHFLPQV----DEIVVLGKGTILEKGSYRDLLDK 847
Cdd:COG1131 165 -EARRELWELL--RELAAeGKTVLLST---HYLEEAerlcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1296-1523 |
1.89e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.34 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELD-LVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLT 1374
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1375 IIPQDPI-LFSGSLRMNLDPF---NK---YSD--EEVWRALELAHLRSFVsglqlgllsevTEGGDNLSIGQRQLLCLGR 1445
Cdd:PRK13650 85 MVFQNPDnQFVGATVEDDVAFgleNKgipHEEmkERVNEALELVGMQDFK-----------EREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1446 AVLRKSKILVLDEATAAVDLETD-SLIQT--TIRKEFsQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSnRG 1522
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS-RG 231
|
.
gi 3219824 1523 S 1523
Cdd:PRK13650 232 N 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
639-846 |
2.12e-21 |
|
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: 99.98 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 639 SFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMEN---VHGHITIQGST-------------AYVPQ 702
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDllelsealrgrriGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 703 QSWIQ-NG-TIKDNILFGSEyNEKKYQQVLKACALlpdlEILPGGDMAEIGEKGIN-LSGGQKQRVSLARAAYQDADIYI 779
Cdd:COG1123 91 DPMTQlNPvTVGDQIAEALE-NLGLSRAEARARVL----ELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 780 LDDPLSAVDAHVGKHIFnkvvgpnGLLA------GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLLD 846
Cdd:COG1123 166 ADEPTTALDVTTQAEIL-------DLLRelqrerGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
650-835 |
6.13e-21 |
|
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: 92.94 E-value: 6.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSaMLGEMENV-HGHITIQG-----------------STAYVPQQ-SWIQNGT 710
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGtdisklsekelaafrrrHIGFVFQSfNLLPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 711 IKDNILFGSEYNEKKYQQVLKACALLpdLEILpggDMAEIGEKGIN-LSGGQKQRVSLARAAYQDADIYILDDPLSAVDA 789
Cdd:cd03255 99 ALENVELPLLLAGVPKKERRERAEEL--LERV---GLGDRLNHYPSeLSGGQQQRVAIARALANDPKIILADEPTGNLDS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 3219824 790 HVGKHIFNKVVGPNGlLAGKTRIFVTHGIHFLPQVDEIVVLGKGTI 835
Cdd:cd03255 174 ETGKEVMELLRELNK-EAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1302-1534 |
6.90e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.03 E-value: 6.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1302 QVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRE---------- 1371
Cdd:PRK10070 33 QILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkkiamvf 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1372 -RLTIIPQDPILFSGSLRMNLDPFNKYSDEEvwRALELahLRsfvsglQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRK 1450
Cdd:PRK10070 113 qSFALMPHMTVLDNTAFGMELAGINAEERRE--KALDA--LR------QVGLENYAHSYPDELSGGMRQRVGLARALAIN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1451 SKILVLDEATAAVdletDSLIQTTIRKEF------SQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSNRGS 1523
Cdd:PRK10070 183 PDILLMDEAFSAL----DPLIRTEMQDELvklqakHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
250
....*....|.
gi 3219824 1524 FYLMAKEAGIE 1534
Cdd:PRK10070 259 DYVRTFFRGVD 269
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1297-1508 |
7.53e-21 |
|
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: 92.60 E-value: 7.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1297 QFNNYQVRYRPELdlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVAsiglhDLRERLTII 1376
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1377 PQD-------PILFSGSLRMNLDP----FNKYSDEE---VWRALE---LAHLRSfvsgLQLGllsevteggdNLSIGQRQ 1439
Cdd:cd03235 74 PQRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALErvgLSELAD----RQIG----------ELSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1440 LLCLGRAVLRKSKILVLDEATAAVDLETD----SLIQTTIRKEfsqCTVITIAHRLHTIMDS-DKIMVLDNGKI 1508
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQediyELLRELRREG---MTILVVTHDLGLVLEYfDRVLLLNRTVV 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1313-1520 |
1.47e-20 |
|
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: 97.45 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRiLESAGGQIIIDGIDVASIG---LHDLRERLTIIPQDPilFsGSL-- 1387
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1388 RMN-----------LDPfnKYSDEE----VWRALElahlrsfvsglQLGLLSEV-----TEggdnLSIGQRQLLCLGRAV 1447
Cdd:COG4172 378 RMTvgqiiaeglrvHGP--GLSAAErrarVAEALE-----------EVGLDPAArhrypHE----FSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1448 LRKSKILVLDEATAAVDLetdsLIQTTI-------RKEFsQCTVITIAHRLHTI--MdSDKIMVLDNGKIVEYGSPEELL 1518
Cdd:COG4172 441 ILEPKLLVLDEPTSALDV----SVQAQIldllrdlQREH-GLAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVF 514
|
..
gi 3219824 1519 SN 1520
Cdd:COG4172 515 DA 516
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1296-1510 |
1.47e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.04 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASI---GLHDLRER 1372
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1373 LTIIPQDPILFSG---------SLRMnldpfNKYSDEEVWRALELAhLRsfvsglQLGLLSEVTEGGDNLSIGQRQLLCL 1443
Cdd:COG2884 81 IGVVFQDFRLLPDrtvyenvalPLRV-----TGKSRKEIRRRVREV-LD------LVGLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1444 GRAVLRKSKILVLDEATAAVDLET-DSLIQttIRKEFSQ--CTVItIA-HRLHtIMDS--DKIMVLDNGKIVE 1510
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRrgTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
650-834 |
2.53e-20 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 89.23 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGStayvpqqswiqngtikdnilfgsEYNEKKYQQV 729
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----------------------DIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 730 LKACALLPDLeilpggdmaeigekginlSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVvgpNGLLA-G 808
Cdd:cd00267 72 RRRIGYVPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELL---RELAEeG 130
|
170 180
....*....|....*....|....*..
gi 3219824 809 KTRIFVTHGIHFLPQV-DEIVVLGKGT 834
Cdd:cd00267 131 RTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
633-845 |
3.48e-20 |
|
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: 91.59 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWdPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSaMLGEM-ENVHGHITIQG-------------STA 698
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINRLiEPTSGEIFIDGedireqdpvelrrKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 699 YVPQQ-SWIQNGTIKDNI-----LFGseYNEKKYQQvlKACALLPDLEILPGGDMAEIGEKginLSGGQKQRVSLARAAY 772
Cdd:cd03295 79 YVIQQiGLFPHMTVEENIalvpkLLK--WPKEKIRE--RADELLALVGLDPAEFADRYPHE---LSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 773 QDADIYILDDPLSAVDAHVGKHIFNKVVGPNGLLaGKTRIFVTHGI-HFLPQVDEIVVLGKGTILEKGSYRDLL 845
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1296-1523 |
7.05e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 92.83 E-value: 7.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLV--LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRiLESA-GGQIIIDGIDVASIGLHDLRE- 1371
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LERPtSGSVLVDGVDLTALSERELRAa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1372 RLTI--IPQDPILFSgS----------LRMnldpfNKYSDEEVW-RALELahlrsfvsgLQL-GLlsevTEGGD----NL 1433
Cdd:COG1135 81 RRKIgmIFQHFNLLS-SrtvaenvalpLEI-----AGVPKAEIRkRVAEL---------LELvGL----SDKADaypsQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1434 SIGQRQLLCLGRAVLRKSKILVLDEATAAVDLE-TDS---LIQtTIRKEFsQCTVITIAHRLHTIMD-SDKIMVLDNGKI 1508
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSildLLK-DINREL-GLTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
250
....*....|....*
gi 3219824 1509 VEYGSPEELLSNRGS 1523
Cdd:COG1135 220 VEQGPVLDVFANPQS 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
652-846 |
7.26e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.90 E-value: 7.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAMLG-EMENvHGHITIQGSTAYV---PQQSWI----QNG------TIKDNILF 717
Cdd:COG1118 20 DVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPD-SGRIVLNGRDLFTnlpPRERRVgfvfQHYalfphmTVAENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 GseynekkyqqvlkacallpdLEILPGGDmAEIGEK-----------GI------NLSGGQKQRVSLARAAYQDADIYIL 780
Cdd:COG1118 99 G--------------------LRVRPPSK-AEIRARveellelvqleGLadrypsQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 781 DDPLSAVDAHVGK-------HIFNKVvgpngllaGKTRIFVTHgihflpQVDE-------IVVLGKGTILEKGSYRDLLD 846
Cdd:COG1118 158 DEPFGALDAKVRKelrrwlrRLHDEL--------GGTTVFVTH------DQEEaleladrVVVMNQGRIEQVGTPDEVYD 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1312-1517 |
1.31e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.31 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHD-LRERLTIIPQDPIL-------- 1382
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLvpnlsvae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1383 --FSGSLRMNLDPFNkysdeevWRALE---LAHLRSFvsGLQLGLLSEVteggDNLSIGQRQLLCLGRAVLRKSKILVLD 1457
Cdd:COG1129 99 niFLGREPRRGGLID-------WRAMRrraRELLARL--GLDIDPDTPV----GDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1458 EATAAVDL-ETDSLIQtTIRKEFSQ-CTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEEL 1517
Cdd:COG1129 166 EPTASLTErEVERLFR-IIRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1312-1508 |
2.23e-19 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 88.32 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDL----RERLTIIPQDPILFSG-- 1385
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFNLLPDlt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1386 -----SLRMNLDPFNKYSDEEvwRALELAHlrsfvsglQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEAT 1460
Cdd:cd03255 99 alenvELPLLLAGVPKKERRE--RAEELLE--------RVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 3219824 1461 AAVDLETDSLIQTTIRK--EFSQCTVITIAHRLHTIMDSDKIMVLDNGKI 1508
Cdd:cd03255 169 GNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1313-1520 |
3.22e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.72 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVA--SIGLHDLRERLTIIPQDP---------- 1380
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyqlfeetie 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1381 --ILFsGSLRMNLdpfnkySDEE----VWRALELahlrsfvsglqLGLLSEVTEGGD--NLSIGQRQLLCLGRAVLRKSK 1452
Cdd:PRK13637 103 kdIAF-GPINLGL------SEEEienrVKRAMNI-----------VGLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1453 ILVLDEATAAVDL----ETDSLIQtTIRKEFsQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK13637 165 ILILDEPTAGLDPkgrdEILNKIK-ELHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKE 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
651-846 |
4.66e-19 |
|
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: 88.32 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSW----IQ------------NGTIKDN 714
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrVQmvfqdpyaslhpRHTVDRI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 715 I-----LFGSEYNEKKYQQVLKACALLPD-LEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:COG1124 102 LaeplrIHGLPDREERIAELLEQVGLPPSfLDRYPH-----------QLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 789 AHVGKHIFNkvvgpngLLA------GKTRIFVTHGI----HFlpqVDEIVVLGKGTILEKGSYRDLLD 846
Cdd:COG1124 171 VSVQAEILN-------LLKdlreerGLTYLFVSHDLavvaHL---CDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
633-852 |
4.81e-19 |
|
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: 88.43 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-STAYVPQQSWIQNGTI 711
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 712 --KDNILF-GS-EYN---EKKYQ-----QVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYI 779
Cdd:cd03288 100 ilQDPILFsGSiRFNldpECKCTddrlwEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 780 LDDPLSAVDAHVgKHIFNKVVgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKK-GVFA 852
Cdd:cd03288 180 MDEATASIDMAT-ENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFA 250
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1296-1520 |
6.07e-19 |
|
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: 87.74 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYrPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTI 1375
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDPILFSG-SLRMN--LDP-FNKYSDEEV-WRALELAHLrsfvsgLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRK 1450
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKIrERADELLAL------VGLDPAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1451 SKILVLDEATAAVDLET-DSL------IQTTIRKefsqcTVITIAHRL-HTIMDSDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:cd03295 154 PPLLLMDEPFGALDPITrDQLqeefkrLQQELGK-----TIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1296-1490 |
6.89e-19 |
|
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: 85.28 E-value: 6.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVrYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLtnclFRIL----ESAGGQIIIDGidvasiglhdlRE 1371
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRALaglwPWGSGRIGMPE-----------GE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1372 RLTIIPQDPILFSGSLRmnldpfnkysdEEV---WralelahlrsfvsglqlgllsevtegGDNLSIGQRQLLCLGRAVL 1448
Cdd:cd03223 65 DLLFLPQRPYLPLGTLR-----------EQLiypW--------------------------DDVLSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 3219824 1449 RKSKILVLDEATAAVDLETDSLIQTTIRKEFsqCTVITIAHR 1490
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
650-847 |
1.39e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 89.36 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGeMENV-HGHITIQG-----------STAYVPQqSWI--QNGTIKDNI 715
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPtSGEILIGGrdvtdlppkdrNIAMVFQ-SYAlyPHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 716 LFG--------SEYNEKkyqqVLKACALL---PDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPL 784
Cdd:COG3839 97 AFPlklrkvpkAEIDRR----VREAAELLgleDLLDRKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 785 SAVDAHVG-------KHIFNKVvgpngllaGKTRIFVTHGihflpQV------DEIVVLGKGTILEKGSYRDLLDK 847
Cdd:COG3839 162 SNLDAKLRvemraeiKRLHRRL--------GTTTIYVTHD-----QVeamtlaDRIAVMNDGRIQQVGTPEELYDR 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1296-1519 |
1.65e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.38 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTI 1375
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDPI-LFSGS---------LRMNLDPfnkySDEEVWR---ALELAHLRSFVsglqlgllsevTEGGDNLSIGQRQLLC 1442
Cdd:PRK13635 86 VFQNPDnQFVGAtvqddvafgLENIGVP----REEMVERvdqALRQVGMEDFL-----------NREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1443 LGRAVLRKSKILVLDEATAAVDLETDSLIQTTIR--KEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1296-1534 |
1.78e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.55 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSS---LTNCLFRILESAGGQIIIDGIDVASIGLHDLRER 1372
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1373 LTIIPQDPI-LFSGSLRMNLDPFNkYSDEEVWRALELAHLRSFVSglQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKS 1451
Cdd:PRK13640 86 VGIVFQNPDnQFVGATVGDDVAFG-LENRAVPRPEMIKIVRDVLA--DVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1452 KILVLDEATAAVDLETDSLIQTTIRK--EFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRgsfyLMAK 1529
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV----EMLK 238
|
....*
gi 3219824 1530 EAGIE 1534
Cdd:PRK13640 239 EIGLD 243
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1313-1521 |
1.86e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.60 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDG--IDVASIGLHDLRERLTIIPQDP--ILFSGSLR 1388
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1389 MNLD--PFN-KYSDEEVWRALELAHLRSFVSGLQlgllsevTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL 1465
Cdd:PRK13636 102 QDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLK-------DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1466 ETDSLIQTTIRKEFSQ--CTVITIAHRLHTI-MDSDKIMVLDNGKIVEYGSPEELLSNR 1521
Cdd:PRK13636 175 MGVSEIMKLLVEMQKElgLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1020-1268 |
1.88e-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: 87.61 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWM 1099
Cdd:cd07346 42 ALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1100 MCFFGIAGTLVMICMATPVFAIIIIPLSILYISVQVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAF--EHQ-- 1175
Cdd:cd07346 122 SDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFaaEERei 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1176 QRFLAWNEKQIDINqkcvfswITSNRWLAIRLELVGNLVVFCSALLLV-----IYRKTLT-GDVVGFVLSNALnITQTLN 1249
Cdd:cd07346 202 ERFREANRDLRDAN-------LRAARLSALFSPLIGLLTALGTALVLLyggylVLQGSLTiGELVAFLAYLGM-LFGPIQ 273
|
250
....*....|....*....
gi 3219824 1250 WLVRMTSEAETNIVAVERI 1268
Cdd:cd07346 274 RLANLYNQLQQALASLERI 292
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
630-847 |
1.94e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.55 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 630 DKAVKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSS---LVSAMLGEMENVHGHITIQGSTaYVPQQSW- 705
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGIT-LTAKTVWd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 706 --------IQN-------GTIKDNILFGSEYNEKKYQQVLKACAllpdlEILPGGDMAE-IGEKGINLSGGQKQRVSLAR 769
Cdd:PRK13640 82 irekvgivFQNpdnqfvgATVGDDVAFGLENRAVPRPEMIKIVR-----DVLADVGMLDyIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 770 AAYQDADIYILDDPLSAVDAHVGKHIFN---KVVGPNGLlagkTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLD 846
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKlirKLKKKNNL----TVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
.
gi 3219824 847 K 847
Cdd:PRK13640 233 K 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1296-1519 |
2.16e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.11 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTI 1375
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDPI-LFSGS---------LRMNLDPFNKYSdEEVWRALElahlrsfvsglQLGLLSEVTEGGDNLSIGQRQLLCLGR 1445
Cdd:PRK13648 88 VFQNPDnQFVGSivkydvafgLENHAVPYDEMH-RRVSEALK-----------QVDMLERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 1446 AVLRKSKILVLDEATAAVDLETDSLIQTTIR--KEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1296-1518 |
2.31e-18 |
|
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: 86.29 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRY--RPeldlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFR-ILESAGGQIII-----DGIDV----AS 1363
Cdd:COG1119 4 LELRNVTVRRggKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLfgerrGGEDVwelrKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1364 IGL------HDLRERLTIIpqDPIL--FSGSlrmnLDPFNKYSDEEVWRA------LELAHL--RSFVSglqlgllsevt 1427
Cdd:COG1119 80 IGLvspalqLRFPRDETVL--DVVLsgFFDS----IGLYREPTDEQRERArellelLGLAHLadRPFGT----------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1428 eggdnLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRK--EFSQCTVITIAHRLHTIMDS-DKIMVLD 1504
Cdd:COG1119 143 -----LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLK 217
|
250
....*....|....
gi 3219824 1505 NGKIVEYGSPEELL 1518
Cdd:COG1119 218 DGRVVAAGPKEEVL 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
633-845 |
2.52e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 86.72 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSW------- 705
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirkkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 706 --IQN-------GTIKDNILFGSEyN--------EKKYQQVLKACallpdleilpggDMAEIGEKG-INLSGGQKQRVSL 767
Cdd:TIGR04520 81 mvFQNpdnqfvgATVEDDVAFGLE-NlgvpreemRKRVDEALKLV------------GMEDFRDREpHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 768 ARAAYQDADIYILDDPLSAVDahvgkhifnkvvgPNG---LLA---------GKTRIFVTHGIHFLPQVDEIVVLGKGTI 835
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLD-------------PKGrkeVLEtirklnkeeGITVISITHDMEEAVLADRVIVMNKGKI 214
|
250
....*....|
gi 3219824 836 LEKGSYRDLL 845
Cdd:TIGR04520 215 VAEGTPREIF 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1312-1520 |
3.22e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 86.24 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILE-----SAGGQIIIDGIDV--ASIGLHDLRERLTIIPQDPILFS 1384
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1385 GS--------LRMNLDPFNKYSDEEVWRALELAhlrsfvsglqlGLLSEV----TEGGDNLSIGQRQLLCLGRAVLRKSK 1452
Cdd:COG1117 106 KSiydnvaygLRLHGIKSKSELDEIVEESLRKA-----------ALWDEVkdrlKKSALGLSGGQQQRLCIARALAVEPE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1453 ILVLDEATAAVD-LETdSLIQTTIRKEFSQCTVITIAHRlhtiMD-----SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:COG1117 175 VLLMDEPTSALDpIST-AKIEELILELKKDYTIVIVTHN----MQqaarvSDYTAFFYLGELVEFGPTEQIFTN 243
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1296-1508 |
5.82e-18 |
|
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: 84.38 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYrPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVAsiGLHD-----LR 1370
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1371 ERLTIIPQDPILFSgslrmNLDPFnkysdEEVWRALELAH-----LRSFVSGL--QLGLLSEVTEGGDNLSIGQRQLLCL 1443
Cdd:cd03292 78 RKIGVVFQDFRLLP-----DRNVY-----ENVAFALEVTGvppreIRKRVPAAleLVGLSHKHRALPAELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1444 GRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMD--SDKIMVLDNGKI 1508
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1296-1520 |
6.33e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.81 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYrPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIG-LHDLRERLT 1374
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1375 IIPQDP-ILFSG-SLRMNLdpfnKYSDEEVwrALELAHLRSFV--SGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRK 1450
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDL----AFGPENL--CLPPIEIRKRVdrALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 1451 SKILVLDEATAAVDLETDSLIQTTIRKEFSQC-TVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1296-1476 |
6.51e-18 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 83.68 E-value: 6.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELdlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGlHDLRERLTI 1375
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDPILFSG-SLRMNLDpF------NKYSDEEVWRALELAHLRSFvSGLQLGLLSEvteggdnlsiGQRQLLCLGRAVL 1448
Cdd:COG4133 80 LGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGLAGL-ADLPVRQLSA----------GQKRRVALARLLL 147
|
170 180
....*....|....*....|....*...
gi 3219824 1449 RKSKILVLDEATAAVDLETDSLIQTTIR 1476
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
652-834 |
7.76e-18 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 82.62 E-value: 7.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG---------------STAYVPQQ-SWIQNGTIKDNI 715
Cdd:cd03229 18 DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDfALFPHLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 716 LFGseynekkyqqvlkacallpdleilpggdmaeigekginLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHI 795
Cdd:cd03229 98 ALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 3219824 796 FNKVVGPNGLLaGKTRIFVTHGIHFLPQV-DEIVVLGKGT 834
Cdd:cd03229 140 RALLKSLQAQL-GITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1312-1512 |
9.50e-18 |
|
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: 82.98 E-value: 9.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCL--FRILESAGGQIIIDGIdvaSIGLHDLRERLTIIPQDPILFsGSLrm 1389
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILH-PTL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1390 nldpfnkysdeEVWRALEL-AHLRSfvsglqlgllsevteggdnLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETD 1468
Cdd:cd03213 98 -----------TVRETLMFaAKLRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 3219824 1469 SLIQTTIRKEFSQ-CTVITIAHRLHTIMDS--DKIMVLDNGKIVEYG 1512
Cdd:cd03213 148 LQVMSLLRRLADTgRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
631-816 |
1.40e-17 |
|
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: 84.62 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 631 KAVKFSEASFTWDPDLEAT-----IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG---------- 695
Cdd:cd03294 16 KAFKLLAKGKSKEEILKKTgqtvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrke 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 696 --------------STAYVPQQswiqngTIKDNILFGSEYN-------EKKYQQVLKACALLPDLEILPGgdmaeigekg 754
Cdd:cd03294 96 lrelrrkkismvfqSFALLPHR------TVLENVAFGLEVQgvpraerEERAAEALELVGLEGWEHKYPD---------- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 755 iNLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKvvgpngLLA-----GKTRIFVTH 816
Cdd:cd03294 160 -ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE------LLRlqaelQKTIVFITH 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
650-835 |
1.40e-17 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 82.06 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGstayvpqqswiqngtiKDNIlfgseyneKKYQQV 729
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG----------------KDIK--------KEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 730 LKACALLPDLEILPGgDMaeIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVGPNGllAGK 809
Cdd:cd03230 72 KRRIGYLPEEPSLYE-NL--TVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK--EGK 146
|
170 180
....*....|....*....|....*..
gi 3219824 810 TRIFVTHGIHFLPQV-DEIVVLGKGTI 835
Cdd:cd03230 147 TILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
650-847 |
1.68e-17 |
|
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: 83.54 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG--STAYVPQQSWI----------QNGTIKDNILF 717
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedATDVPVQERNVgfvfqhyalfRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 GseynekkyqqvlkacallpdLEILPGG---DMAEIGEKGINL-----------------SGGQKQRVSLARAAYQDADI 777
Cdd:cd03296 98 G--------------------LRVKPRSerpPEAEIRAKVHELlklvqldwladrypaqlSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 778 YILDDPLSAVDAHVGKH-------IFNKVvgpngllaGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLLDK 847
Cdd:cd03296 158 LLLDEPFGALDAKVRKElrrwlrrLHDEL--------HVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
628-848 |
1.86e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 84.27 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 628 NFDKAVKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSWIQ 707
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 708 N---------------GTIKDNILFGSE---YNEKKYQQVLKACALLPDLEILpggdmaeIGEKGINLSGGQKQRVSLAR 769
Cdd:PRK13632 83 KkigiifqnpdnqfigATVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 770 AAYQDADIYILDDPLSAVDAHvGKHIFNKVVGPNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKK 848
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
318-609 |
1.88e-17 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 84.52 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 318 ILKSFILKLIHDLLVFLNPQLLKLLIGFVKSSNSYVWFGYIcAILMFAVTLIQSFClqSYFQH--CFVLGMCVRTTVMSS 395
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWI-ALLLLLLALLRALL--SYLRRylAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 396 IYKKALTLSNLARKQYTIGETVNLMSVDSQKLMD-ATNYMQLVWSSVIQITLSIFFL----WRelgpsiLAGVG--VMVL 468
Cdd:cd07346 78 LFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALVILfylnWK------LTLVAllLLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 469 LIPVNGVLATKIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPS----FQEQVQGIRKKELKNLLRFGQLQSLLIF 544
Cdd:cd07346 152 YVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPLIGL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 545 ILQITPILVSVV--------TFSVYVLVdsanvlnaekAFtsITLFNILRFPLSMLPMVTSSILQASVSVDRL 609
Cdd:cd07346 232 LTALGTALVLLYggylvlqgSLTIGELV----------AF--LAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
651-846 |
1.94e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 83.32 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS----------------TAYVPQQSWIQNG-TIKD 713
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDSlTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 714 NILFG----SEYNEKKYQQV----LKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLS 785
Cdd:cd03261 97 NVAFPlrehTRLSEEEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 786 AVDAhVGKHIFNKVVGP-NGLLaGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLLD 846
Cdd:cd03261 166 GLDP-IASGVIDDLIRSlKKEL-GLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
649-835 |
2.13e-17 |
|
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: 82.30 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 649 TIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG----------STAYVPQQSWIQNG--TIKDNIL 716
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVDYQLFtdSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 717 FGSEYNEKKYQQVLKacaLLPDLEILpggDMAEigEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAH----VG 792
Cdd:cd03226 95 LGLKELDAGNEQAET---VLKDLDLY---ALKE--RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmerVG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 3219824 793 KhIFNKVVGpngllAGKTRIFVTHGIHFLPQV-DEIVVLGKGTI 835
Cdd:cd03226 167 E-LIRELAA-----QGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1296-1520 |
2.70e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 85.24 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNN----YQVRYRPELdlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRE 1371
Cdd:PRK11153 2 IELKNiskvFPQGGRTIH--ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1372 -RLTI--IPQDpilfsgslrmnldpFNKYSD----EEVWRALELAHL-RSFVSGLQLGLLSEV--TEGGD----NLSIGQ 1437
Cdd:PRK11153 80 aRRQIgmIFQH--------------FNLLSSrtvfDNVALPLELAGTpKAEIKARVTELLELVglSDKADrypaQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1438 RQLLCLGRAVLRKSKILVLDEATAAVDLE-TDSLIQ--TTIRKEFSqCTVITIAHRlhtiMD-----SDKIMVLDNGKIV 1509
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPAtTRSILEllKDINRELG-LTIVLITHE----MDvvkriCDRVAVIDAGRLV 220
|
250
....*....|.
gi 3219824 1510 EYGSPEELLSN 1520
Cdd:PRK11153 221 EQGTVSEVFSH 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1312-1509 |
3.20e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.21 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHdlrERLTIIP---QDPIL------ 1382
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEY---KRAKYIGrvfQDPMMgtapsm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1383 -------------FSGSLRMNLDPFNKysdeevwralelAHLRSFVSGLQLGL---LSEVTEggdNLSIGQRQLLCLGRA 1446
Cdd:COG1101 98 tieenlalayrrgKRRGLRRGLTKKRR------------ELFRELLATLGLGLenrLDTKVG---LLSGGQRQALSLLMA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1447 VLRKSKILVLDEATAAVDLET-DSLIQTT---IRKEfsQCTVITIAHRLH--------TIMdsdkimvLDNGKIV 1509
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTaALVLELTekiVEEN--NLTTLMVTHNMEqaldygnrLIM-------MHEGRII 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
651-829 |
3.57e-17 |
|
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: 81.76 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------------STAYVPQQS-WIQNGTIKDNILF 717
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADgLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 -----GSEYNEKKYQQVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHvG 792
Cdd:COG4133 99 waalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-G 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 3219824 793 KHIFNKVVgpNGLLA-GKTRIFVTHGIHFLPQVDEIVV 829
Cdd:COG4133 167 VALLAELI--AAHLArGGAVLLTTHQPLELAAARVLDL 202
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1296-1523 |
3.90e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.50 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRpelDLVLKgITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHdlrER-LT 1374
Cdd:COG3840 2 LRLDDLTYRYG---DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA---ERpVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1375 IIPQDPILFSG-SLRMN----LDPFNKYSDEEVWRALELAHlrsfvsglQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLR 1449
Cdd:COG3840 75 MLFQENNLFPHlTVAQNiglgLRPGLKLTAEQRAQVEQALE--------RVGLAGLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1450 KSKILVLDEATAAVD----LETDSLIQtTIRKEFsQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSNRGS 1523
Cdd:COG3840 147 KRPILLLDEPFSALDpalrQEMLDLVD-ELCRER-GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
632-839 |
5.81e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.01 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 632 AVKFSEASFTWDPDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITI----------QGSTAYVP 701
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTA-LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlgqptrqalqKNLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 702 QQS---WIQNGTIKDNILFGsEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGI-NLSGGQKQRVSLARAAYQDADI 777
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMG-RYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIgELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 778 YILDDPLSAVDAHVGKHIFNkvvgpngLL-----AGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKG 839
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIIS-------LLrelrdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1313-1506 |
5.84e-17 |
|
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: 81.61 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRER----LTIIPQDPILFSGSLR 1388
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1389 MNL---DPFNKYSDEEVwraLELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL 1465
Cdd:cd03290 97 ENItfgSPFNKQRYKAV---TDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 3219824 1466 E-TDSLIQTTIRK--EFSQCTVITIAHRLHTIMDSDKIMVLDNG 1506
Cdd:cd03290 174 HlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1320-1520 |
5.96e-17 |
|
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: 82.69 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1320 IKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRE--RLTI---------IPQDPILFSGSLR 1388
Cdd:cd03294 47 VREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrRKKIsmvfqsfalLPHRTVLENVAFG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1389 MNLDPFNKYSDEEvwRALELAHLrsfvsglqLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVdletD 1468
Cdd:cd03294 127 LEVQGVPRAEREE--RAAEALEL--------VGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL----D 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1469 SLIQTTIRKEF------SQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:cd03294 193 PLIRREMQDELlrlqaeLQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1312-1520 |
1.03e-16 |
|
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: 81.05 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDlRERLTII--PQDPILFSG-SLR 1388
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1389 MNLD---PFNKYSDEEVWRALE-------LAHLRSfvsglQLGLlsevteggdNLSIGQRQLLCLGRAVLRKSKILVLDE 1458
Cdd:cd03218 94 ENILavlEIRGLSKKEREEKLEelleefhITHLRK-----SKAS---------SLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1459 ATAAVDLETDSLIQTTIR--KEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKilKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1312-1519 |
1.37e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.36 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPIL-FSGS---- 1386
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTveev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1387 LRMNLDPF---NKYSDEEVWRALE---LAHL--RSFVSglqlgllsevteggdnLSIGQRQLLCLGRaVL-------RKS 1451
Cdd:PRK13548 97 VAMGRAPHglsRAEDDALVAAALAqvdLAHLagRDYPQ----------------LSGGEQQRVQLAR-VLaqlwepdGPP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1452 KILVLDEATAAVDLETDsliQTTIR--KEF---SQCTVITIAHRLH-TIMDSDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQ---HHVLRlaRQLaheRGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1296-1508 |
1.62e-16 |
|
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: 79.88 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELdlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDV--ASIGLHDLRERL 1373
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1374 TIIPQDPILFSgslRMN------LDPFN--KYSDEEVwRALELAHLRsfvsglQLGLLSEVTEGGDNLSIGQRQLLCLGR 1445
Cdd:cd03262 79 GMVFQQFNLFP---HLTvlenitLAPIKvkGMSKAEA-EERALELLE------KVGLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1446 AVLRKSKILVLDEATAAVDLET-DSLIQTTIRKEFSQCTVITIAHRlhtiMD-----SDKIMVLDNGKI 1508
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELvGEVLDVMKDLAEEGMTMVVVTHE----MGfarevADRVIFMDDGRI 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
650-831 |
1.73e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.06 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST--------AYVPQQS----WIqngTIKDNILF 717
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKDallpWL---NVLDNVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 GSeynekKYQQVLKACALLPDLEILPGGDMAEIGEKGI-NLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIf 796
Cdd:COG4525 100 GL-----RLRGVPKAERRARAEELLALVGLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 3219824 797 nkvvgpNGLL------AGKTRIFVTHGIhflpqvDEIVVLG 831
Cdd:COG4525 174 ------QELLldvwqrTGKGVFLITHSV------EEALFLA 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
644-788 |
1.89e-16 |
|
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: 80.69 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 644 PDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS----------------TAYVPQQ-SWI 706
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQfNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 707 QNGTIKDNILFG---------SEYNEKKYQQVLKACALLPDLEILpggDMAEIgeKGINLSGGQKQRVSLARAAYQDADI 777
Cdd:cd03256 91 ERLSVLENVLSGrlgrrstwrSLFGLFPKEEKQRALAALERVGLL---DKAYQ--RADQLSGGQQQRVAIARALMQQPKL 165
|
170
....*....|.
gi 3219824 778 YILDDPLSAVD 788
Cdd:cd03256 166 ILADEPVASLD 176
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1312-1524 |
2.49e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPIL---FSGS-- 1386
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVRqv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1387 LRMN-------LDPFNKYSDEEVWRALELAHLRSFVSglqlgllSEVTEggdnLSIGQRQLLCLGRAVLRKSKILVLDEA 1459
Cdd:PRK09536 98 VEMGrtphrsrFDTWTETDRAAVERAMERTGVAQFAD-------RPVTS----LSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1460 TAAVDL----ETDSLIQTTIRKEFsqcTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN---RGSF 1524
Cdd:PRK09536 167 TASLDInhqvRTLELVRRLVDDGK---TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTAdtlRAAF 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
650-837 |
2.96e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 79.70 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSaMLGEMENV-HGHITIQG---STA--------------YVPQQS-WIQNGT 710
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdiSSLserelarlrrrhigFVFQFFnLLPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 711 IKDNILFGSEYNEKKYQQVLK-ACALLPDLEIlpgGDMAE--IGEkginLSGGQKQRVSLARAAYQDADIYILDDPLSAV 787
Cdd:COG1136 103 ALENVALPLLLAGVSRKERRErARELLERVGL---GDRLDhrPSQ----LSGGQQQRVAIARALVNRPKLILADEPTGNL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 788 DAHVGKHIFNkvvgpngLLA------GKTRIFVTHGIHFLPQVDEIVVLGKGTILE 837
Cdd:COG1136 176 DSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
628-847 |
3.46e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 80.57 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 628 NFDKAVKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTayVPQQSW-- 705
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA--ITDDNFek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 706 --------IQN-------GTIKDNILFGSEYNEKKYQQVLKACAllpdlEILPGGDMAEIGEKGIN-LSGGQKQRVSLAR 769
Cdd:PRK13648 81 lrkhigivFQNpdnqfvgSIVKYDVAFGLENHAVPYDEMHRRVS-----EALKQVDMLERADYEPNaLSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 770 AAYQDADIYILDDPLSAVDAHVGKHIFNKVvgpNGLLAGK--TRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDK 847
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLV---RKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1296-1520 |
4.55e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 79.37 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELdlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDV--ASIGLHDLRERL 1373
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1374 TIIPQDPILFS----------GSLRMNldPFNKYSDEEVWRALeLAhlrsfvsglQLGLLSEVTEGGDNLSIGQRQLLCL 1443
Cdd:PRK09493 80 GMVFQQFYLFPhltalenvmfGPLRVR--GASKEEAEKQAREL-LA---------KVGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1444 GRAVLRKSKILVLDEATAAVDLETDSLIQTTIR---KEFSQCTVIT----IAHRLHTimdsdKIMVLDNGKIVEYGSPEE 1516
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIVTheigFAEKVAS-----RLIFIDKGRIAEDGDPQV 222
|
....
gi 3219824 1517 LLSN 1520
Cdd:PRK09493 223 LIKN 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1312-1520 |
5.28e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 79.57 E-value: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILE-----SAGGQIIIDGIDVASIGLHDLRERLTIIPQDP------ 1380
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1381 -ILFSGSLRMNLDPFNKYSDE---EVWRALELAHLRSFVSglqlgllSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVL 1456
Cdd:PRK14247 98 sIFENVALGLKLNRLVKSKKElqeRVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1457 DEATAAVDLETDSLIQTTIRKEFSQCTVITIAH------RLhtimdSDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1296-1512 |
5.81e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 78.56 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLV--LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVAS--------IG 1365
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepaearrrLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1366 LHD----LRERLTIIPQdpILFSGSLR-MNLDPFNkysdeevwralelAHLRSFVSGLQLGLLSEVTEGGdnLSIGQRQL 1440
Cdd:cd03266 82 FVSdstgLYDRLTAREN--LEYFAGLYgLKGDELT-------------ARLEELADRLGMEELLDRRVGG--FSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1441 LCLGRAVLRKSKILVLDEATAAVD-LETDSLIQTTIRKEFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYG 1512
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
650-847 |
5.90e-16 |
|
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: 78.82 E-value: 5.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-STAYVPQ---------QSW--IQNGTIKDNILF 717
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkDITNLPPhkrpvntvfQNYalFPHLTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 GSEYNEKKYQQVLKACAllpdlEILPGGDMAEIGEKGIN-LSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHI- 795
Cdd:cd03300 96 GLRLKKLPKAEIKERVA-----EALDLVQLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMq 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 796 -----FNKVVgpngllaGKTRIFVTHGI-HFLPQVDEIVVLGKGTILEKGSYRDLLDK 847
Cdd:cd03300 171 lelkrLQKEL-------GITFVFVTHDQeEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
650-838 |
6.97e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 79.36 E-value: 6.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVP--------QQS----WiQNgtIKDNILF 717
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfQNEgllpW-RN--VQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 GSEYnekkyQQVLKACALLPDLEILPGGDMAEIGEKGI-NLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAhvgkhiF 796
Cdd:PRK11248 94 GLQL-----AGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA------F 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3219824 797 NKVVGPNGLL-----AGKTRIFVTHGIH---FLpqVDEIVVL--GKGTILEK 838
Cdd:PRK11248 163 TREQMQTLLLklwqeTGKQVLLITHDIEeavFM--ATELVLLspGPGRVVER 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
650-840 |
7.95e-16 |
|
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: 78.38 E-value: 7.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAM-----LGEMENVHGHITIQGSTAYVPQQSWIQ---------------NG 709
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDVLElrrrvgmvfqkpnpfPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 710 TIKDNILFG--------SEYNEKKYQQVLKACALLPDLeilpgGDMAeigeKGINLSGGQKQRVSLARAAYQDADIYILD 781
Cdd:cd03260 96 SIYDNVAYGlrlhgiklKEELDERVEEALRKAALWDEV-----KDRL----HALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 782 DPLSAVDAHVGKHIFNKVVGpnglLAGKTRI-FVTHGIHflpQV----DEIVVLGKGTILEKGS 840
Cdd:cd03260 167 EPTSALDPISTAKIEELIAE----LKKEYTIvIVTHNMQ---QAarvaDRTAFLLNGRLVEFGP 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
649-839 |
9.27e-16 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 77.68 E-value: 9.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 649 TIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-----------STAYVPQQ-SWIQNGTIKDNIL 716
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 717 FG--------SEYNEKkyqqVLKACALLpDLEILpggdmaeIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:cd03301 95 FGlklrkvpkDEIDER----VREVAELL-QIEHL-------LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3219824 789 AHVGKHIFNKVVGPNGLLaGKTRIFVTHG-IHFLPQVDEIVVLGKGTILEKG 839
Cdd:cd03301 163 AKLRVQMRAELKRLQQRL-GTTTIYVTHDqVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
650-847 |
1.07e-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: 80.53 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGeMENV-HGHITIQG-----------STAYVPQqswiqNG------TI 711
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FETPdSGRILLDGrdvtglppekrNVGMVFQ-----DYalfphlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 712 KDNILFG--------SEYNEKkyqqVLKACALLpdleilpggDMAEIGEKGIN-LSGGQKQRVSLARA-AYQdADIYILD 781
Cdd:COG3842 95 AENVAFGlrmrgvpkAEIRAR----VAELLELV---------GLEGLADRYPHqLSGGQQQRVALARAlAPE-PRVLLLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 782 DPLSAVDAHVG-------KHIFNKVvgpngllaGKTRIFVTHGihflpQV------DEIVVLGKGTILEKGSYRDLLDK 847
Cdd:COG3842 161 EPLSALDAKLReemreelRRLQREL--------GITFIYVTHD-----QEealalaDRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1313-1517 |
1.19e-15 |
|
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: 77.80 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASiGLHDLRERLTIIPQDPILFSG-SLRMNL 1391
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1392 DPFNKY----SDEEVWRALELahLRSFvsglqlgllsEVTEGGDNL----SIGQRQLLCLGRAVLRKSKILVLDEATAAV 1463
Cdd:cd03265 95 YIHARLygvpGAERRERIDEL--LDFV----------GLLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 1464 DLETDSLIQTTIRK--EFSQCTVITIAHrlhtIMD-----SDKIMVLDNGKIVEYGSPEEL 1517
Cdd:cd03265 163 DPQTRAHVWEYIEKlkEEFGMTILLTTH----YMEeaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1296-1519 |
1.25e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.98 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDL-VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLT 1374
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1375 IIPQDPI-LFSGSLRMNLDPFNKYSD----EEVWRALELAHlrsfvsgLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLR 1449
Cdd:PRK13642 85 MVFQNPDnQFVGATVEDDVAFGMENQgiprEEMIKRVDEAL-------LAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1450 KSKILVLDEATAAVDLETDSLIQTTIR--KEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
650-790 |
1.52e-15 |
|
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: 77.70 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSL---VSAMLGEMENVHGHITIQG----------STAYVPQQS-WIQNGTIKDNI 715
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDDiLLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 716 LF-----GSEYNEKKYQQVLKACALLPDLEILPGGdmaeiGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAH 790
Cdd:cd03234 103 TYtailrLPRKSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
644-789 |
2.18e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 644 PDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITI--QGSTAYVPQQSWIQNGTIKDNILF---G 718
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatA 452
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 719 SEYNEKKYQQVLKACAlLPDLEilpgGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDA 789
Cdd:COG4178 453 EAFSDAELREALEAVG-LGHLA----ERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
651-788 |
2.35e-15 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 77.40 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG----------------STAYVPQQ-------SWIQ 707
Cdd:COG3638 20 DDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqdvtalrgralrrlrrRIGMIFQQfnlvprlSVLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 708 N---------GTIKdnILFGSEYNEkkyqQVLKACALLPDLEILpggDMAEigEKGINLSGGQKQRVSLARAAYQDADIY 778
Cdd:COG3638 100 NvlagrlgrtSTWR--SLLGLFPPE----DRERALEALERVGLA---DKAY--QRADQLSGGQQQRVAIARALVQEPKLI 168
|
170
....*....|
gi 3219824 779 ILDDPLSAVD 788
Cdd:COG3638 169 LADEPVASLD 178
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
644-788 |
2.43e-15 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 77.34 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 644 PDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG----------------STAYVPQQ-SWI 706
Cdd:TIGR02315 12 PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgkklrklrrRIGMIFQHyNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 707 QNGTIKDNILFG------------SEYNEKKYQqvlKACALLPDLEILpggDMAEIgeKGINLSGGQKQRVSLARAAYQD 774
Cdd:TIGR02315 92 ERLTVLENVLHGrlgykptwrsllGRFSEEDKE---RALSALERVGLA---DKAYQ--RADQLSGGQQQRVAIARALAQQ 163
|
170
....*....|....
gi 3219824 775 ADIYILDDPLSAVD 788
Cdd:TIGR02315 164 PDLILADEPIASLD 177
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
652-840 |
2.66e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 79.36 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS-----------TAYVPQQ-SWIQNGTIKDNILFG- 718
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAFGl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 719 ----------SEYNEKKYQQVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:PRK10851 100 tvlprrerpnAAAIKAKVTQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 789 AHVGKHI------------FnkvvgpngllagkTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGS 840
Cdd:PRK10851 169 AQVRKELrrwlrqlheelkF-------------TSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGT 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
650-837 |
2.79e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.54 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQgstayVPQQSWIQNGTIKDNILFGSEYNEKKYqqV 729
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDAVE--L 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 730 LKACALlpdleilpgGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVD---AHVGKHIFNKVVGPngll 806
Cdd:COG2401 119 LNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARR---- 185
|
170 180 190
....*....|....*....|....*....|....
gi 3219824 807 AGKTRIFVTHG---IHFLpQVDEIVVLGKGTILE 837
Cdd:COG2401 186 AGITLVVATHHydvIDDL-QPDLLIFVGYGGVPE 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
650-845 |
3.70e-15 |
|
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: 76.47 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSaMLGEMEN-VHGHITIQG----------------STAYVPQQ-SWIQNGTI 711
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGtdltllsgkelrkarrRIGMIFQHfNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 712 KDNILfgseynekkyqqvlkacalLPdLEILpGGDMAEIGEK--------GI---------NLSGGQKQRVSLARAAYQD 774
Cdd:cd03258 100 FENVA-------------------LP-LEIA-GVPKAEIEERvlellelvGLedkadaypaQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 775 ADIYILDDPLSAVDAHVGKHIFNKVVGPNGLLaGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLL 845
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINREL-GLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVF 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1313-1516 |
3.71e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVAsigLHDLRE--RLTI--IPQDPILF----- 1383
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR---IRSPRDaiALGIgmVHQHFMLVpnltv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 ----------SGSLRMNLDPFNKysdeevwRALELAhlRSFvsGLQLGLLSEVteggDNLSIGQRQLLCLGRAVLRKSKI 1453
Cdd:COG3845 98 aenivlglepTKGGRLDRKAARA-------RIRELS--ERY--GLDVDPDAKV----EDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1454 LVLDEATaAV--DLETDSLIQtTIRKEFSQ-CTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEE 1516
Cdd:COG3845 163 LILDEPT-AVltPQEADELFE-ILRRLAAEgKSIIFITHKLREVMAiADRVTVLRRGKVVGTVDTAE 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1318-1512 |
3.95e-15 |
|
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: 75.99 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1318 CNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIglhDLRER-LTIIPQDPILF------------- 1383
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA---PPADRpVSMLFQENNLFahltveqnvglgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 SGSLRMNldpfnkysdEEVWRALELAHLRSFVSGLQLGLlsevtegGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAV 1463
Cdd:cd03298 96 SPGLKLT---------AEDRQAIEVALARVGLAGLEKRL-------PGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1464 D--LETDSL-IQTTIRKEfSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYG 1512
Cdd:cd03298 160 DpaLRAEMLdLVLDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
652-835 |
3.95e-15 |
|
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: 74.39 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTayvpqqswIQNGTIKDnilfgseynekkyqqvlk 731
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE--------VSFASPRD------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 732 acALlpdleilpggdmaeigEKGIN----LSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFnKVVGpnGLLA 807
Cdd:cd03216 72 --AR----------------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF-KVIR--RLRA 130
|
170 180 190
....*....|....*....|....*....|
gi 3219824 808 -GKTRIFVTHGIHFLPQV-DEIVVLGKGTI 835
Cdd:cd03216 131 qGVAVIFISHRLDEVFEIaDRVTVLRDGRV 160
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
653-845 |
4.36e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 76.71 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 653 VNLDIKPGQLVAVVGTVGSGKSSLVSAM--LGEMENVH---GHITIQGSTAYVPQQSWI-----------QN------GT 710
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCInlLEQPEAGTirvGDITIDTARSLSQQKGLIrqlrqhvgfvfQNfnlfphRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 711 IKDNILFGSEY--NEKKYQQVLKACALLpdleilpggdmAEIGEKGIN------LSGGQKQRVSLARAAYQDADIYILDD 782
Cdd:PRK11264 102 VLENIIEGPVIvkGEPKEEATARARELL-----------AKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 783 PLSAVDAHVGKHIFNKVVGpnglLA--GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLL 845
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQ----LAqeKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALF 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1298-1524 |
7.88e-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: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1298 FNNYQVRYRPeldlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGidvasiglhdlreRLTIIP 1377
Cdd:cd03291 42 FSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1378 QDPILFSGSLRMNLdPFNKYSDEEVWRALELA-HLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVL 1456
Cdd:cd03291 105 QFSWIMPGTIKENI-IFGVSYDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1457 DEATAAVDLETDSLI-QTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNRGSF 1524
Cdd:cd03291 184 DSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1020-1180 |
9.92e-15 |
|
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: 76.67 E-value: 9.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWM 1099
Cdd:cd18547 48 LLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1100 MCFFGIAGTLVMICMATPVFAII---IIPLSILYISV-----QVFYVATSRQLRRLDsvtkspiySHFSETVTGLPIIRA 1171
Cdd:cd18547 128 SSILTIVGTLIMMLYISPLLTLIvlvTVPLSLLVTKFiakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKA 199
|
....*....
gi 3219824 1172 FEHQQRFLA 1180
Cdd:cd18547 200 FNREEEAIE 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
633-837 |
1.17e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 74.70 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------STAYVPQ---- 702
Cdd:COG2884 2 IRFENVSKRYPGGREA-LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlKRREIPYlrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 703 -----QSW--IQNGTIKDNILFGSEYNEKKYQQVLKACAllpdlEILpggDMAEIGEKG----INLSGGQKQRVSLARAA 771
Cdd:COG2884 81 igvvfQDFrlLPDRTVYENVALPLRVTGKSRKEIRRRVR-----EVL---DLVGLSDKAkalpHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 772 YQDADIYILDDPLSAVDAHVGKHI------FNKVvgpngllaGKTRIFVTHGIHFLPQVDE-IVVLGKGTILE 837
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEImelleeINRR--------GTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1311-1541 |
1.31e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1311 LVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIG-LHDLRERLTIIPQDP--------- 1380
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivativ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1381 ---ILFsGSLRMNLDP--FNKYSDEEVwRALELAHLRSFVSGLqlgllsevteggdnLSIGQRQLLCLGRAVLRKSKILV 1455
Cdd:PRK13633 104 eedVAF-GPENLGIPPeeIRERVDESL-KKVGMYEYRRHAPHL--------------LSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1456 LDEATAAVDLETDSLIQTTIRK--EFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLSNrgsfYLMAKEAGI 1533
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE----VEMMKKIGL 243
|
....*...
gi 3219824 1534 ENVNHTEL 1541
Cdd:PRK13633 244 DVPQVTEL 251
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
648-851 |
2.13e-14 |
|
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: 75.28 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 648 ATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLgEMENVHGHITIQGST-------------AYVPQQSWIQNGTIKDN 714
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSwnsvplqkwrkafGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 715 ILFGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAhVGKH 794
Cdd:cd03289 97 LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 795 IFNKVVgpNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLLDKKGVF 851
Cdd:cd03289 176 VIRKTL--KQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1295-1527 |
2.24e-14 |
|
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: 74.30 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1295 EIQFNNYQVRYR--PELDlvlkGITCNIKSGEKVGVVGRTGAGKSSLtnclFRI---LESA-GGQIIIDGIDVASiglHD 1368
Cdd:cd03296 2 SIEVRNVSKRFGdfVALD----DVSLDIPSGELVALLGPSGSGKTTL----LRLiagLERPdSGTILFGGEDATD---VP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1369 LRER--------------LTIIpqDPILFSGSLRMNLDPFNKYS-DEEVWRALELAHLrsfvSGLQLGLLSEvteggdnL 1433
Cdd:cd03296 71 VQERnvgfvfqhyalfrhMTVF--DNVAFGLRVKPRSERPPEAEiRAKVHELLKLVQL----DWLADRYPAQ-------L 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1434 SIGQRQLLCLGRAVLRKSKILVLDEATAAVDletdsliqTTIRKEFSQ----------CTVITIAHRLHTIMD-SDKIMV 1502
Cdd:cd03296 138 SGGQRQRVALARALAVEPKVLLLDEPFGALD--------AKVRKELRRwlrrlhdelhVTTVFVTHDQEEALEvADRVVV 209
|
250 260
....*....|....*....|....*
gi 3219824 1503 LDNGKIVEYGSPEELLSNRGSFYLM 1527
Cdd:cd03296 210 MNKGRIEQVGTPDEVYDHPASPFVY 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
633-834 |
2.45e-14 |
|
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: 71.71 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLeaTIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST--AYVPQqswiqngt 710
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVkiGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 711 ikdnilfgseynekkyqqvlkacallpdleilpggdmaeigekginLSGGQKQRVSLARAAYQDADIYILDDPLSAVDah 790
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD-- 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 3219824 791 vgkhIFNKVVGPNGLLA-GKTRIFVTHGIHFLPQV-DEIVVLGKGT 834
Cdd:cd03221 103 ----LESIEALEEALKEyPGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1312-1520 |
2.59e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.70 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGI------DVASIGLHDLRERLTIIPQDPILFSG 1385
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1386 -SLRMNLD-PFNKY---SDEEVWRALELAhLRSFvsGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEAT 1460
Cdd:PRK14246 105 lSIYDNIAyPLKSHgikEKREIKKIVEEC-LRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 1461 AAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
650-839 |
3.28e-14 |
|
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: 73.02 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSWIQNGTIKDNILFgseYNEKKYQQV 729
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGF---YPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 730 LKACALLPDL------EILPGGDMAEIGEKGI-NLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVGP 802
Cdd:cd03268 93 LRLLARLLGIrkkridEVLDVVGLKDSAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSL 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 3219824 803 NGllAGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKG 839
Cdd:cd03268 173 RD--QGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
621-845 |
3.50e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 74.49 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 621 SAIRRVSNFDKAVKFSeASFTWDPDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG----- 695
Cdd:COG4167 2 SALLEVRNLSKTFKYR-TGLFRRQQFEA-VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkley 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 696 -----------------STAYVPQQswiQNGTIKD-----NILFGSEYNEKKYQQVLKACALLPD-LEILPggDMaeige 752
Cdd:COG4167 80 gdykyrckhirmifqdpNTSLNPRL---NIGQILEeplrlNTDLTAEEREERIFATLRLVGLLPEhANFYP--HM----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 753 kginLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNkvvgpngLL------AGKTRIFVTH--GI--HFlp 822
Cdd:COG4167 150 ----LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIIN-------LMlelqekLGISYIYVSQhlGIvkHI-- 216
|
250 260
....*....|....*....|...
gi 3219824 823 qVDEIVVLGKGTILEKGSYRDLL 845
Cdd:COG4167 217 -SDKVLVMHQGEVVEYGKTAEVF 238
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1296-1510 |
3.82e-14 |
|
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: 73.27 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELD--LVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGlhdlrERL 1373
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1374 TIIPQDPILF---------SGSLRMNLDPfNKYSDEEVWRALELAHLRSF-------VSGlqlgllsevteggdnlsiGQ 1437
Cdd:cd03293 76 GYVFQQDALLpwltvldnvALGLELQGVP-KAEARERAEELLELVGLSGFenayphqLSG------------------GM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1438 RQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRK--EFSQCTVITIAHRLH-TIMDSDKIMVLDN--GKIVE 1510
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1022-1268 |
4.35e-14 |
|
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: 74.52 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1022 VFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMC 1101
Cdd:cd18557 41 ILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1102 FFGIAGTLVMICMATPVFAIIIIPLSILYISVQVFYVATSRQLRR--LDSVTKSPiySHFSETVTGLPIIRAF---EHQ- 1175
Cdd:cd18557 121 ILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKevQDALAKAG--QVAEESLSNIRTVRSFsaeEKEi 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1176 QRFLAWNEKQIDINQKCVFsWITSNRWLAIRLELVGNLVVFCSALLLVIYRKTLTGDVVGFVL------SNALNITQTLN 1249
Cdd:cd18557 199 RRYSEALDRSYRLARKKAL-ANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILytimvaSSVGGLSSLLA 277
|
250
....*....|....*....
gi 3219824 1250 WLVRMTSeaetnivAVERI 1268
Cdd:cd18557 278 DIMKALG-------ASERV 289
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
650-844 |
4.79e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.53 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------------------STAYVPQQSwiqngtI 711
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvthrsiqqrdicmvfqSYALFPHMS------L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 712 KDNILFGSEY----NEKKYQQVLKACALLpdleilpggDMAEIGEKGIN-LSGGQKQRVSLARAAYQDADIYILDDPLSA 786
Cdd:PRK11432 96 GENVGYGLKMlgvpKEERKQRVKEALELV---------DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 787 VDAHVGKHIFNKVVGPNGLLaGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDL 844
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQF-NITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1296-1512 |
5.34e-14 |
|
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: 72.61 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELdlVLKGITCNIKSGeKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVaSIGLHDLRERLTI 1375
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDpilFSGSLRMNLDPFNKY-----------SDEEVWRALELahlrsfvsglqLGLLSEVTEGGDNLSIGQRQLLCLG 1444
Cdd:cd03264 77 LPQE---FGVYPNFTVREFLDYiawlkgipskeVKARVDEVLEL-----------VNLGDRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1445 RAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMDS-DKIMVLDNGKIVEYG 1512
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
651-835 |
5.53e-14 |
|
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: 72.56 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSWIQ----------------NGTIKDN 714
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqkvgmvfqqfnlfpHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 715 ILFGseynEKKYQQVLKACALLPDLEILPGGDMAE-IGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGK 793
Cdd:cd03262 97 ITLA----PIKVKGMSKAEAEERALELLEKVGLADkADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 3219824 794 HIFNKVVGpnglLA--GKTRIFVTHGIHFLPQV-DEIVVLGKGTI 835
Cdd:cd03262 173 EVLDVMKD----LAeeGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
633-845 |
5.90e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 73.87 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWdPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTA-------------- 698
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqgirklvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 699 ---YVPQQSWIQNgTIKDNILFGSEynekkyqqvlKACalLPDLEILPGGDMAeIGEKGI---------NLSGGQKQRVS 766
Cdd:PRK13644 81 ivfQNPETQFVGR-TVEEDLAFGPE----------NLC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 767 LARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVGPNGllAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLL 845
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1520 |
6.45e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.96 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1303 VRYR-PELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDG--IDVASIGLHDLRERLTIIPQD 1379
Cdd:PRK13639 7 LKYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1380 P--ILFSGSLRMNL--DPFN-KYSDEEVWRALELAhlrsfvsglqlglLSEV-TEGGDN-----LSIGQRQLLCLGRAVL 1448
Cdd:PRK13639 87 PddQLFAPTVEEDVafGPLNlGLSKEEVEKRVKEA-------------LKAVgMEGFENkpphhLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1449 RKSKILVLDEATAAVDLETDSLIQTTIRKEFSQ-CTVITIAHRLHTI-MDSDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
654-788 |
6.56e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.08 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 654 NLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS--TAYVPQQSWI-----QNG-----TIKDNILFG--- 718
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRPVsmlfqENNlfshlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 719 ----SEYNEKKYQQVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
645-839 |
7.30e-14 |
|
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: 72.33 E-value: 7.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 645 DLEATIQDVNLDIK---PGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST-----------------AYVPQQ- 703
Cdd:cd03297 5 DIEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiGLVFQQy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 704 SWIQNGTIKDNILFGSEYNEKKYQQVLKAcallpdlEILPGGDMAEIGEKGI-NLSGGQKQRVSLARAAYQDADIYILDD 782
Cdd:cd03297 85 ALFPHLNVRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 783 PLSAVDAHVGKHIFNKVvgpNGLLA--GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKG 839
Cdd:cd03297 158 PFSALDRALRLQLLPEL---KQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1315-1519 |
7.32e-14 |
|
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: 76.38 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1315 GITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIII----DGIDVASIGLhDLRERLT----IIPQDPILFSGs 1386
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRAKryigILHQEYDLYPH- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1387 lRMNLDPFNKYSDEEVwrALELAHLRSFVSGLQLGLLSEVTEG-----GDNLSIGQRQLLCLGRAVLRKSKILVLDEATA 1461
Cdd:TIGR03269 380 -RTVLDNLTEAIGLEL--PDELARMKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1462 AVDLETDSLIQTTI---RKEFSQcTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:TIGR03269 457 TMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
652-847 |
9.24e-14 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 72.37 E-value: 9.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS-----------TAYVPQQ-SWIQNGTIKDNILFG- 718
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAYGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 719 ---SEYNEKKYQQVLKACALLPDLEILpggdmaeiGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHI 795
Cdd:cd03299 97 kkrKVDKKEIERKVLEIAEMLGIDHLL--------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 796 FN--KVVGPNgllAGKTRIFVTHG-IHFLPQVDEIVVLGKGTILEKGSYRDLLDK 847
Cdd:cd03299 169 REelKKIRKE---FGVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1310-1517 |
1.08e-13 |
|
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: 72.27 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1310 DLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHdlRERLTIIPQDPILF------ 1383
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFphltvf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 ---SGSLRMNLDPFNKYsDEEVWRALELAHLRSFVSglqlgllsevtEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEAT 1460
Cdd:cd03300 91 eniAFGLRLKKLPKAEI-KERVAEALDLVQLEGYAN-----------RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 1461 AAVDLETDSLIQTTIrKEFSQCTVITIAHRLH----TIMDSDKIMVLDNGKIVEYGSPEEL 1517
Cdd:cd03300 159 GALDLKLRKDMQLEL-KRLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
650-846 |
1.22e-13 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 71.70 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------ST--------AYVPQ-QSWIQNGTIKDN 714
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglPPheraragiGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 715 ILFGSE-YNEKKYQQVL-KACALLPDLEilpggDMAeiGEKGINLSGGQKQRVSLARAAYQDADIYILDDP---LSAVda 789
Cdd:cd03224 96 LLLGAYaRRRAKRKARLeRVYELFPRLK-----ERR--KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK-- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 790 hVGKHIFNKVVGPNGLlaGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLLD 846
Cdd:cd03224 167 -IVEEIFEAIRELRDE--GVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1312-1510 |
1.61e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.41 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASI---GLHDLRERLTIIPQDPI------- 1381
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSIsavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1382 ----LFSGSLR--MNLDPfnkysDEEVWRALELahLRSFvsGLQLGLLSEVTEggdNLSIGQRQLLCLGRAVLRKSKILV 1455
Cdd:PRK10419 107 tvreIIREPLRhlLSLDK-----AERLARASEM--LRAV--DLDDSVLDKRPP---QLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1456 LDEATAAVDLetdsLIQTTI-------RKEF-SQCTVITiaHRLHTIMD-SDKIMVLDNGKIVE 1510
Cdd:PRK10419 175 LDEAVSNLDL----VLQAGVirllkklQQQFgTACLFIT--HDLRLVERfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
639-839 |
1.93e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 72.36 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 639 SFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTaYVPQQSW---------IQN- 708
Cdd:PRK13635 12 SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvgmvFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 709 ------GTIKDNILFGSEYNE-------KKYQQVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDA 775
Cdd:PRK13635 91 dnqfvgATVQDDVAFGLENIGvpreemvERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 776 DIYILDDPLSAVDAhVGKHifnKVVGPNGLLAGKTRIFV---THGIHFLPQVDEIVVLGKGTILEKG 839
Cdd:PRK13635 160 DIIILDEATSMLDP-RGRR---EVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
650-840 |
3.20e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.20 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAYVPQQSWIQNG-TIKDNI 715
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 716 LFG-SEYN-------EKKYQQVLKAcalLPDLEIlpggdmAEIGEKGI-NLSGGQKQRVSLARAAYQDADIYILDDPLSA 786
Cdd:PRK11231 98 AYGrSPWLslwgrlsAEDNARVNQA---MEQTRI------NHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 787 VDahvgkhiFNKVVGPNGLL-----AGKTRIFVthgIHFLPQV----DEIVVLGKGTILEKGS 840
Cdd:PRK11231 169 LD-------INHQVELMRLMrelntQGKTVVTV---LHDLNQAsrycDHLVVLANGHVMAQGT 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1312-1517 |
3.69e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIG---LHDLreRLTIIPQDPILFSG-SL 1387
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQL--GIYLVPQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1388 RMNLdPFNKYSDEEVWRALE--LAHLrsfvsGLQLGLlsEVTEGgdNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVD- 1464
Cdd:PRK15439 104 KENI-LFGLPKRQASMQKMKqlLAAL-----GCQLDL--DSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTASLTp 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1465 LETDSLIQtTIRKEFSQ-CTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEEL 1517
Cdd:PRK15439 174 AETERLFS-RIRELLAQgVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1317-1519 |
4.13e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.38 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1317 TCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDvasiglHDL----RERLTIIPQDPILFSG-SLRMN- 1390
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtppsRRPVSMLFQENNLFSHlTVAQNi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1391 ---LDPFNKYSDEEVWRALELAHlrsfvsglQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVD--- 1464
Cdd:PRK10771 93 glgLNPGLKLNAAQREKLHAIAR--------QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpal 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1465 -LETDSLIQTTIRKEfsQCTVITIAHRLHtimDSDKI----MVLDNGKIVEYGSPEELLS 1519
Cdd:PRK10771 165 rQEMLTLVSQVCQER--QLTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLS 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1310-1476 |
4.63e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 69.69 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1310 DLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVAsiglhdlreRLTIIPQDPILFSG---- 1385
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA---------EQRDEPHENILYLGhlpg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1386 -----SLRMNLD---PFNKYSDEEVWRALELAHLRSFvSGLQLGllsevteggdNLSIGQRQLLCLGRAVLRKSKILVLD 1457
Cdd:TIGR01189 84 lkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTGF-EDLPAA----------QLSAGQQRRLALARLWLSRRPLWILD 152
|
170
....*....|....*....
gi 3219824 1458 EATAAVDLETDSLIQTTIR 1476
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLR 171
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1312-1512 |
4.76e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 70.25 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGL-HDLRERLTIIpqDPILFSGSLrMN 1390
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgGGFNPELTGR--ENIYLNGRL-LG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1391 LDPfnKYSDEEVWRALELAHLRSFVSgLQLGllsevteggdNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSL 1470
Cdd:cd03220 114 LSR--KEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 3219824 1471 IQTTIRKEFSQC-TVITIAHRLHTIMD-SDKIMVLDNGKIVEYG 1512
Cdd:cd03220 181 CQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1312-1503 |
5.08e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.18 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGidVASIGLhdLRERLTIIPQDPILFSGSLRMNL 1391
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG--GARVAY--VPQRSEVPDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1392 ----DPFNKYSDE---EVWRALELAHLRSFvSGLQLgllsevteggDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVD 1464
Cdd:NF040873 83 warrGLWRRLTRDdraAVDDALERVGLADL-AGRQL----------GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 3219824 1465 LETDSLIQTTIRKEFS-QCTVITIAHRLHTIMDSDKIMVL 1503
Cdd:NF040873 152 AESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1312-1520 |
5.40e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.31 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDlRERLTI--IPQDPILFSG-SLR 1388
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1389 MNL-------DPFNKYSDEEvwRALEL------AHLRSFVsglqlgllsevtegGDNLSIGQRQLLCLGRAVLRKSKILV 1455
Cdd:PRK10895 97 DNLmavlqirDDLSAEQRED--RANELmeefhiEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1456 LDEATAAVD----LETDSLIQtTIRKefSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK10895 161 LDEPFAGVDpisvIDIKRIIE-HLRD--SGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1312-1519 |
5.60e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.81 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSG-SLR-- 1388
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1389 --------MNLdpFNKYSDEE---VWRALELAHLRSFVSGLqlgllseVTEggdnLSIGQRQLLCLGRAVLRKSKILVLD 1457
Cdd:PRK11231 97 vaygrspwLSL--WGRLSAEDnarVNQAMEQTRINHLADRR-------LTD----LSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1458 EATAAVDL----ETDSLIQttirkEFSQC--TVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:PRK11231 164 EPTTYLDInhqvELMRLMR-----ELNTQgkTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
633-816 |
6.38e-13 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 69.74 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG---------STAYVPQQ 703
Cdd:cd03292 1 IEFINVTKTYPNGTAA-LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 704 --------SWIQNGTIKDNILFGSEYNEKKYQQVLKACALLPDLEILPGG--DMAEigekgiNLSGGQKQRVSLARAAYQ 773
Cdd:cd03292 80 igvvfqdfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKhrALPA------ELSGGEQQRVAIARAIVN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 3219824 774 DADIYILDDPLSAVDAHVGKHIFNKVVGPNglLAGKTRIFVTH 816
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKIN--KAGTTVVVATH 194
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1311-1520 |
6.87e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.40 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1311 LVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHD--------------LRERLTII 1376
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarmgvvrtfqhvrLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1377 -----PQDPILFSGSLR--MNLDPFNKYSDEEVWRA---LElahlrsfvsglQLGLLSEVTEGGDNLSIGQRQLLCLGRA 1446
Cdd:PRK11300 99 enllvAQHQQLKTGLFSglLKTPAFRRAESEALDRAatwLE-----------RVGLLEHANRQAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1447 VLRKSKILVLDEATAAVD-LETDSLIQ--TTIRKEFsQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNN 244
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
644-816 |
7.30e-13 |
|
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: 67.95 E-value: 7.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 644 PDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITI--QGSTAYVPQQSWIQNGTIKDNIlfgsey 721
Cdd:cd03223 11 PDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQRPYLPLGTLREQL------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 722 nekkyqqvlkacallpdleILPGGDMaeigekginLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVG 801
Cdd:cd03223 85 -------------------IYPWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE 136
|
170
....*....|....*
gi 3219824 802 pngllAGKTRIFVTH 816
Cdd:cd03223 137 -----LGITVISVGH 146
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1296-1521 |
7.38e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.01 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLVLKG---ITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDV----ASIGLHD 1368
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1369 LRERLTIIPQDP--ILFSGSLRMNLD--PFNKYSDEEVWRALELAHLRsfvsglQLGLLSEVTEGGD-NLSIGQRQLLCL 1443
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEfgPKNFGFSEDEAKEKALKWLK------KVGLSEDLISKSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1444 GRAVLRKSKILVLDEATAAVDLET-DSLIQTTIRKEFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSNR 1521
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1296-1520 |
7.96e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.45 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYrpELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGgQIIIDG--------IDVASIGLH 1367
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES-EVRVEGrveffnqnIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1368 DLRERLTIIPQDPILFSGSLRMNLdpfnKYSDEEV-WR-ALELAHL-RSFVSGLQL--GLLSEVTEGGDNLSIGQRQLLC 1442
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVgWRpKLEIDDIvESALKDADLwdEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1443 LGRAVLRKSKILVLDEATAAVD----LETDSLIQTTIRKefSQCTVITIAHRLHTIMD-SDKIMVLDN-----GKIVEYG 1512
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFG 238
|
....*...
gi 3219824 1513 SPEELLSN 1520
Cdd:PRK14258 239 LTKKIFNS 246
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
651-783 |
8.42e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.79 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST--AYVPQ-QSWIQNGTIKDNILFGSEYNEKKYQ 727
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLriGYLPQePPLDDDLTVLDTVLDGDAELRALEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 728 QVLKACALLPDLEILpGGDMAEIGEK--------------------GI----------NLSGGQKQRVSLARAAYQDADI 777
Cdd:COG0488 95 ELEELEAKLAEPDED-LERLAELQEEfealggweaearaeeilsglGFpeedldrpvsELSGGWRRRVALARALLSEPDL 173
|
....*.
gi 3219824 778 YILDDP 783
Cdd:COG0488 174 LLLDEP 179
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
633-855 |
9.50e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.58 E-value: 9.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWD---PDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST------------ 697
Cdd:PRK13646 3 IRFDNVSYTYQkgtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 698 -----AYVPQ--QSWIQNGTIKDNILFGSEYNEKKYQQVL-KACALLPDLeilpgGDMAEIGEKG-INLSGGQKQRVSLA 768
Cdd:PRK13646 83 vrkriGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKnYAHRLLMDL-----GFSRDVMSQSpFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 769 RAAYQDADIYILDDPLSAVDAHvGKHIFNKVVGPNGLLAGKTRIFVTHGIHFLPQ-VDEIVVLGKGTILEKGSYRDLLdK 847
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF-K 235
|
....*...
gi 3219824 848 KGVFARNW 855
Cdd:PRK13646 236 DKKKLADW 243
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
651-790 |
9.62e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.75 E-value: 9.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS----TAYVPQQSWI--QNG-----TIKDNILFGS 719
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEACHYLghRNAmkpalTVAENLEFWA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 720 E-YNEKKYQQVLKACAL-LPDLEILPGGdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAH 790
Cdd:PRK13539 99 AfLGGEELDIAAALEAVgLAPLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
654-788 |
9.69e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 69.40 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 654 NLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS--TAYVPQQ---SWI-QNG------TIKDNILFG--- 718
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdlTALPPAErpvSMLfQENnlfphlTVAQNIGLGlrp 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 719 ----SEYNEKKYQQVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:COG3840 99 glklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
650-844 |
1.12e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.43 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIqGSTAYVPQ--------------------QSWIQNG 709
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkklkplrkkvgivfqfpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 710 TIKDNILFG-------SEYNEKKYQQVLKACALLPDLeilpggdmaeIGEKGINLSGGQKQRVSLARAAYQDADIYILDD 782
Cdd:PRK13634 102 TVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 783 PLSAVDAHVGKHI---FNKVVGPNGLlagkTRIFVTHGIHFLPQ-VDEIVVLGKGTILEKGSYRDL 844
Cdd:PRK13634 172 PTAGLDPKGRKEMmemFYKLHKEKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1312-1520 |
1.26e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.39 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDV-ASIGL-------HDLRERLTIIPQDPILF 1383
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLsqqkgliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 ----------SGSLRMNLDPfnkySDEEVWRALELAhlrsfvsgLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKI 1453
Cdd:PRK11264 98 phrtvleniiEGPVIVKGEP----KEEATARARELL--------AKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1454 LVLDEATAAVDLETDSLIQTTIRKEFSQC-TVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
650-790 |
1.27e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.80 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST-------------AYVPQQS------------ 704
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPladwspaelarrrAVLPQHSslsfpftveevv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 705 ------WIQNGTIKDNILfgseynekkyQQVLKACallpDLEILPGGDMAEigekginLSGGQKQRVSLARA----AYQD 774
Cdd:PRK13548 98 amgrapHGLSRAEDDALV----------AAALAQV----DLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqlWEPD 156
|
170
....*....|....*....
gi 3219824 775 AD--IYILDDPLSAVD-AH 790
Cdd:PRK13548 157 GPprWLLLDEPTSALDlAH 175
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
650-847 |
1.30e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIqGST---AYVPQQswiQ-----NGTIKDNIlfgSEY 721
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETvkiGYFDQH---QeeldpDKTVLDEL---RDG 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 722 NEKKYQQvlKACALLPDLeiLPGGDMAE--IGekgiNLSGGQKQRVSLARAAYQDADIYILDDP-----LSAVDAHVgkh 794
Cdd:COG0488 404 APGGTEQ--EVRGYLGRF--LFSGDDAFkpVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldIETLEALE--- 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 795 ifnkvvgpNGLL--AGkTRIFVTHGIHFLPQV-DEIVVLGKGTILEK-GSYRDLLDK 847
Cdd:COG0488 473 --------EALDdfPG-TVLLVSHDRYFLDRVaTRILEFEDGGVREYpGGYDDYLEK 520
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1312-1519 |
1.70e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.76 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCL--FRILESAGGQII---------------------------------I 1356
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1357 DGIDVASIGLHDLRERLTIIPQDPILFSGSLR-----MNLDPFNKYS-DEEVWRALELAHlrsfvsglQLGLLSEVTEGG 1430
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvLEALEEIGYEgKEAVGRAVDLIE--------MVQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1431 DNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIR---KEFSQCTVITiAHRLHTIMD-SDKIMVLDNG 1506
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeavKASGISMVLT-SHWPEVIEDlSDKAIWLENG 245
|
250
....*....|...
gi 3219824 1507 KIVEYGSPEELLS 1519
Cdd:TIGR03269 246 EIKEEGTPDEVVA 258
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1312-1520 |
1.96e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 70.56 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNClfrI--LESA-GGQIIIDGIDVAsIGLHdLRER--------------LT 1374
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRI---IagLETPdSGRIVLNGRDLF-TNLP-PRERrvgfvfqhyalfphMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1375 IipQDPILFSgsLRMnLDPFNKYSDEEVWRALELAHLrsfvSGLqlgllsevtegGD----NLSIGQRQLLCLGRAVLRK 1450
Cdd:COG1118 92 V--AENIAFG--LRV-RPPSKAEIRARVEELLELVQL----EGL-----------ADrypsQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1451 SKILVLDEATAAVDletdsliqTTIRKE----------FSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:COG1118 152 PEVLLLDEPFGALD--------AKVRKElrrwlrrlhdELGGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVYD 223
|
.
gi 3219824 1520 N 1520
Cdd:COG1118 224 R 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1304-1519 |
2.07e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.27 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1304 RYRPELdlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDG--IDVASIGLHDLRERLTIIPQDP- 1380
Cdd:PRK13638 10 RYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1381 --ILFSG-------SLRmNLDpfnkYSDEEVWR----ALELAHLRSFVSG-LQLgllsevteggdnLSIGQRQLLCLGRA 1446
Cdd:PRK13638 88 qqIFYTDidsdiafSLR-NLG----VPEAEITRrvdeALTLVDAQHFRHQpIQC------------LSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1447 VLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCT-VITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1313-1519 |
2.19e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.05 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPI----------- 1381
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1382 LFSGSLRMNLDPFNKYSDEEVWRALElahlrsfvsglQLGLLSE-VTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEAT 1460
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLR-----------QVGLLPDhASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1461 AAVDLETDS-LIQTTIR-KEFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:PRK15112 178 ASLDMSMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
651-846 |
2.65e-12 |
|
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: 68.47 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG---STAYVPQQSWI--------QNG------TIKD 713
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKELYELrrrigmlfQGGalfdslTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 714 NILFG----SEYNEKKYQQ----VLKACALLPDLEILPggdmAEigekginLSGGQKQRVSLARAAYQDADIYILDDPLS 785
Cdd:COG1127 102 NVAFPlrehTDLSEAEIRElvleKLELVGLPGAADKMP----SE-------LSGGMRKRVALARALALDPEILLYDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 786 AVDAhVGKHIFNKvvgpngLLA------GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLLD 846
Cdd:COG1127 171 GLDP-ITSAVIDE------LIRelrdelGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1312-1531 |
3.00e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.55 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIidgidVASIGLHDLRERLTIIPQDPILFsgslrmnl 1391
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQDARLL-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1392 dPFNKYSDeEV-------WRALELAHLRSfvsglqLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVD 1464
Cdd:PRK11247 94 -PWKKVID-NVglglkgqWRDAALQALAA------VGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1465 ----LETDSLIQTTIRKE-FsqcTVITIAHRL-HTIMDSDKIMVLDNGKI-----VEYGSPEEllsnRGSFYLMAKEA 1531
Cdd:PRK11247 166 altrIEMQDLIESLWQQHgF---TVLLVTHDVsEAVAMADRVLLIEEGKIgldltVDLPRPRR----RGSARLAELEA 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1312-1516 |
3.15e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.18 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGiDVASI-----GLH-DL--RERltiipqdpILF 1383
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSALlelgaGFHpELtgREN--------IYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 SGSLrMNLdpfnkySDEEVwRALeLAHLRSFvSGLqlgllsevtegGD-------NLSIGQRQLLCLGRAVLRKSKILVL 1456
Cdd:COG1134 112 NGRL-LGL------SRKEI-DEK-FDEIVEF-AEL-----------GDfidqpvkTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1457 DEATAAVDletdsliqttirKEFSQ-------------CTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEE 1516
Cdd:COG1134 171 DEVLAVGD------------AAFQKkclarirelresgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEE 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1309-1532 |
4.01e-12 |
|
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: 69.74 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1309 LDLVLKGITcniksgekvGVVGRTGAGKSSLTNCLfrilesAG------GQIIIDG---------IDVAsigLHdlRERL 1373
Cdd:COG4148 20 FTLPGRGVT---------ALFGPSGSGKTTLLRAI------AGlerpdsGRIRLGGevlqdsargIFLP---PH--RRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1374 TIIPQDPILFSG-SLRMNLD--------PFNKYSDEEVWRALELAHL-RSFVsglqlgllsevteggDNLSIGQRQLLCL 1443
Cdd:COG4148 80 GYVFQEARLFPHlSVRGNLLygrkraprAERRISFDEVVELLGIGHLlDRRP---------------ATLSGGERQRVAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1444 GRAVLRKSKILVLDEATAAVDLETDSLIQ---TTIRKEFSqCTVITIAH------RLhtimdSDKIMVLDNGKIVEYGSP 1514
Cdd:COG4148 145 GRALLSSPRLLLMDEPLAALDLARKAEILpylERLRDELD-IPILYVSHsldevaRL-----ADHVVLLEQGRVVASGPL 218
|
250
....*....|....*....
gi 3219824 1515 EELLSNRGSF-YLMAKEAG 1532
Cdd:COG4148 219 AEVLSRPDLLpLAGGEEAG 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1312-1520 |
4.02e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGG-----QIIIDGIDVASI-GLHDLRERLTIIPQDPILFSG 1385
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1386 SLRMNLDP---FNKYSDEEVWRALELAHLRSFvsGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAA 1462
Cdd:PRK14271 116 SIMDNVLAgvrAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1463 VDLETDSLIQTTIRKEFSQCTVITIAHRL-HTIMDSDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
628-840 |
4.23e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.50 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 628 NFDKAVKFSEASFTWD---PDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHiTIQGSTAY----- 699
Cdd:PRK13645 2 DFSKDIILDNVSYTYAkktPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDYAIpanlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 700 -----------------VPQQSWIQNgTIKDNILFGSEYNEKKYQQVLKACALLPDLEILPGgDMAEigEKGINLSGGQK 762
Cdd:PRK13645 81 kikevkrlrkeiglvfqFPEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPE-DYVK--RSPFELSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 763 QRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVGPNGlLAGKTRIFVTHGI-HFLPQVDEIVVLGKGTILEKGS 840
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNK-EYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1314-1520 |
4.60e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.96 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1314 KGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIG---LHDLRERLTIIPQDPiLFSGSLRMN 1390
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDP-LASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1391 L-----DPFNKY----SDEEVWRALELAHLRsfvsglqLGLLSEVTeggdN-----LSIGQRQLLCLGRAVLRKSKILVL 1456
Cdd:PRK15079 117 IgeiiaEPLRTYhpklSRQEVKDRVKAMMLK-------VGLLPNLI----NrypheFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1457 DEATAAVDLETDS----LIQtTIRKEFSqCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK15079 186 DEPVSALDVSIQAqvvnLLQ-QLQREMG-LSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1312-1519 |
5.89e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.91 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDP--ILFSGSLRM 1389
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1390 NL--DPFNKYSDEEVwraleLAHLRSFVSGLqLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLE- 1466
Cdd:PRK13652 99 DIafGPINLGLDEET-----VAHRVSSALHM-LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQg 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 1467 TDSLIQ--TTIRKEFSQcTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:PRK13652 173 VKELIDflNDLPETYGM-TVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1020-1225 |
5.95e-12 |
|
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: 68.18 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWM 1099
Cdd:cd18544 44 ALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1100 MCFFGIAGTLVMICMATP---VFAIIIIPLsILYISV--QVFYVATSRQLRRLDSVtkspIYSHFSETVTGLPIIRAFEH 1174
Cdd:cd18544 124 GDLLLLIGILIAMFLLNWrlaLISLLVLPL-LLLATYlfRKKSRKAYREVREKLSR----LNAFLQESISGMSVIQLFNR 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1175 QQRFLawnEKQIDINQKCVFSWITSNRWLAI-R--LELVGNLvvfcsALLLVIY 1225
Cdd:cd18544 199 EKREF---EEFDEINQEYRKANLKSIKLFALfRplVELLSSL-----ALALVLW 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1323-1520 |
6.42e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1323 GEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDG--IDVASIG-LHDLRERLTIIPQDPIlfsgslrMNLDPFNK--Y 1397
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGkLQALRRDIQFIFQDPY-------ASLDPRQTvgD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1398 SDEEVWRALELAH---LRSFVSGL--QLGLLSE-VTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLI 1471
Cdd:PRK10261 423 SIMEPLRVHGLLPgkaAAARVAWLleRVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1472 QT---TIRKEFSqCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK10261 503 INlllDLQRDFG-IAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
700-853 |
6.54e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 6.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 700 VPQQSWIQNGTIKDNILFGSEynEKKYQQVLKAC---ALLPDLEILPGGDMAEIGEKGINLSGGQKQRVSLARAAYQDAD 776
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKE--DATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 777 IYILDDPLSAVDAHVGKHIFNKVVGPNGlLAGKTRIFVTHGIHFLPQVDEIVVLGK----GTILE-KGSYRDLLD-KKGV 850
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVDIKD-KADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGV 1457
|
...
gi 3219824 851 FAR 853
Cdd:PTZ00265 1458 YKK 1460
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
650-839 |
6.81e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAM-LGEMENvHGHITIQGSTAYVPQQswIQNGTI-----KDNILFgSEYN- 722
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPD-SGQLNIAGHQFDFSQK--PSEKAIrllrqKVGMVF-QQYNl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 723 -------------------EKKYQQVLKACALLPDLEIlpgGDMAEigEKGINLSGGQKQRVSLARAAYQDADIYILDDP 783
Cdd:COG4161 94 wphltvmenlieapckvlgLSKEQAREKAMKLLARLRL---TDKAD--RFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 784 LSAVDAHVGKHIFNKVvgpNGLLA-GKTRIFVTHGIHFLPQVDEIVV-LGKGTILEKG 839
Cdd:COG4161 169 TAALDPEITAQVVEII---RELSQtGITQVIVTHEVEFARKVASQVVyMEKGRIIEQG 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
650-843 |
7.71e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.82 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST-AYVPQ---------QSW--IQNGTIKDNILF 717
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDiTHVPAenrhvntvfQSYalFPHMTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 G--------SEYNEKkyqqVLKACALLpDLEilpggDMAEigEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDA 789
Cdd:PRK09452 110 GlrmqktpaAEITPR----VMEALRMV-QLE-----EFAQ--RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 790 HVGKHIFNKVVGPNGLLaGKTRIFVTHGI-HFLPQVDEIVVLGKGTILEKGSYRD 843
Cdd:PRK09452 178 KLRKQMQNELKALQRKL-GITFVFVTHDQeEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1296-1512 |
8.82e-12 |
|
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: 66.15 E-value: 8.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELdlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDL----RE 1371
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIgylpEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1372 R-----LTIIPQdpILFSGSLR-MNLDPFNKYSDEEVWRaLELAHLRSfvsglqlgllSEVTEggdnLSIGQRQLLCLGR 1445
Cdd:cd03269 79 RglypkMKVIDQ--LVYLAQLKgLKKEEARRRIDEWLER-LELSEYAN----------KRVEE----LSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1446 AVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQ-CTVITIAHRLHTIMD-SDKIMVLDNGKIVEYG 1512
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1312-1512 |
9.23e-12 |
|
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: 66.12 E-value: 9.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHD-----------LRERLTIIpqDP 1380
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiamvfqnyaLYPHMTVY--DN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1381 ILFSgsLRMNLDPfnkySDEEVWRALELAHLrsfvsgLQLG-LLSEVTeggDNLSIGQRQLLCLGRAVLRKSKILVLDEA 1459
Cdd:cd03301 93 IAFG--LKLRKVP----KDEIDERVREVAEL------LQIEhLLDRKP---KQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1460 TAAVdletDSLIQTTIRKEFS------QCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYG 1512
Cdd:cd03301 158 LSNL----DAKLRVQMRAELKrlqqrlGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
651-830 |
9.72e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGemenVH----GHITIQGST--------------AYVPQQ-SWIQNGTI 711
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSG----VYqpdsGEILLDGEPvrfrsprdaqaagiAIIHQElNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 712 KDNILFGSEY------NEKK-YQQVLKACALLpDLEILPGgdmAEIGEkginLSGGQKQRVSLARAAYQDADIYILDDPL 784
Cdd:COG1129 97 AENIFLGREPrrggliDWRAmRRRARELLARL-GLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3219824 785 SAVDAHVGKHIFnKVVgpNGLLA-GKTRIFVThgiHFLPQV----DEIVVL 830
Cdd:COG1129 169 ASLTEREVERLF-RII--RRLKAqGVAIIYIS---HRLDEVfeiaDRVTVL 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
628-846 |
9.84e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.91 E-value: 9.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 628 NFDKAVKFSEASFTWDPDLEAT-----IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGstayvpq 702
Cdd:PRK10070 17 HPQRAFKYIEQGLSKEQILEKTglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 703 qswIQNGTIKDNILfgSEYNEKKYQQVLKACALLPDLEIL---------PGGDMAEIGEKGIN----------------- 756
Cdd:PRK10070 90 ---VDIAKISDAEL--REVRRKKIAMVFQSFALMPHMTVLdntafgmelAGINAEERREKALDalrqvglenyahsypde 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 757 LSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVGPNGlLAGKTRIFVTHGIHFLPQV-DEIVVLGKGTI 835
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQA-KHQRTIVFISHDLDEAMRIgDRIAIMQNGEV 243
|
250
....*....|.
gi 3219824 836 LEKGSYRDLLD 846
Cdd:PRK10070 244 VQVGTPDEILN 254
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
611-848 |
1.01e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.32 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 611 RYLGGDDLDTSAIRRVSNFdkAVKFSEASFTWDPdlEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGH 690
Cdd:PRK13536 22 KHQGISEAKASIPGSMSTV--AIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 691 ITIQGstAYVPQQSWI---------------QNGTIKDNILFGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEkgi 755
Cdd:PRK13536 98 ITVLG--VPVPARARLararigvvpqfdnldLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSD--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 756 nLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVvgpNGLLA-GKTRIFVThgiHFLPQV----DEIVVL 830
Cdd:PRK13536 173 -LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL---RSLLArGKTILLTT---HFMEEAerlcDRLCVL 245
|
250
....*....|....*...
gi 3219824 831 GKGTILEKGSYRDLLDKK 848
Cdd:PRK13536 246 EAGRKIAEGRPHALIDEH 263
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
645-841 |
1.08e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.32 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 645 DLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-STAYVPQ---------QSW--IQNGTIK 712
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPPyqrpinmmfQSYalFPHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 713 DNILFGSEYNEKKYQQVLKACAllpdlEILPGGDMAEI-GEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHV 791
Cdd:PRK11607 110 QNIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3219824 792 GKHIFNKVVgpnGLL--AGKTRIFVTHGihflpQVDEIVVLGKGTILEKGSY 841
Cdd:PRK11607 185 RDRMQLEVV---DILerVGVTCVMVTHD-----QEEAMTMAGRIAIMNRGKF 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
626-833 |
1.09e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.98 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 626 VSNFDKAVKFSEASFTWDPdlEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAmLGEMENVHGHITIQGSTAYVPQQSW 705
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 706 IQNGTI------------KDNILFGSEYNEKKYQqvLKACALLPDLEI-------LPGGDM-----AEIGEKGINLSGGQ 761
Cdd:PRK14258 78 ERRVNLnrlrrqvsmvhpKPNLFPMSVYDNVAYG--VKIVGWRPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 762 KQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIfNKVVGPNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKG 833
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
651-840 |
1.18e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 66.64 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTA--------YVPQQSwiqnGtiKDNILFGSE-- 720
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSallelgagFHPELT----G--RENIYLNGRll 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 721 -YNEKKYQQVLKacallpdlEILpggDMAEIGEKgINL-----SGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKH 794
Cdd:COG1134 117 gLSRKEIDEKFD--------EIV---EFAELGDF-IDQpvktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 3219824 795 IFNKVvgpNGLLA-GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGS 840
Cdd:COG1134 185 CLARI---RELREsGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGD 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
646-845 |
1.20e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.12 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 646 LEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG----------------------STAYVPQQ 703
Cdd:PRK15112 26 VEA-VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqrirmifqdpSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 704 --SWIQNGTIKDNILFGSEYNEKKYQQVLKACALLPD-LEILPggDMaeigekginLSGGQKQRVSLARAAYQDADIYIL 780
Cdd:PRK15112 105 riSQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYP--HM---------LAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 781 DDPLSAVDAHVGKHIFNKVVGPNGlLAGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLL 845
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQE-KQGISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVL 238
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
964-1458 |
1.34e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 69.06 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 964 LKYLQAVGWWSILFIILFYGLNNVAfigsNLWLSAWTSDSdnLNGTNNSSShrdMRIGVFGALGLAqgicLLISTLWS-I 1042
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLA----NAGLIALINQA--LNATGAALA---RLLLLFAGLLVL----LLLSRLASqL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1043 YACRNASKALH---GQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPqtlrswMMCFFGIAGTLVMICMA---- 1115
Cdd:COG4615 71 LLTRLGQHAVArlrLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV------RLPELLQSVALVLGCLAylaw 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1116 --TPVFAIIIIplsILYISVQVFYVATSRQLRRLDSV--TKSPIYSHFSETVTG-----LPIIRAFE-HQQRFLAWNEKQ 1185
Cdd:COG4615 145 lsPPLFLLTLV---LLGLGVAGYRLLVRRARRHLRRAreAEDRLFKHFRALLEGfkelkLNRRRRRAfFDEDLQPTAERY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1186 IDINQKCVFSWITSNRWLAIRLELVGNLVVFCSALLLVIYRKTLTGDVVGFV-----LSNALNITQTLnwlvrmtSEAEt 1260
Cdd:COG4615 222 RDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFVLVLLflrgpLSQLVGALPTL-------SRAN- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1261 niVAVERISEyinVE----NEAPWVTDKRPPADWPRHGEIQFNNYQVRYRPELD---LVLKGITCNIKSGEKVGVVGRTG 1333
Cdd:COG4615 294 --VALRKIEE---LElalaAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1334 AGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGslrmNLDPFNKYSDEEV--W-RALELAH 1410
Cdd:COG4615 369 SGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR----LLGLDGEADPARAreLlERLELDH 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 3219824 1411 LRSFVSGLqlglLSEVteggdNLSIGQRQLLCLGRAVLRKSKILVLDE 1458
Cdd:COG4615 445 KVSVEDGR----FSTT-----DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1312-1531 |
1.68e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGidvasiglhdlRERLTIIPQDPILFSGS----- 1386
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDLtvldt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1387 LRMNLDPFNK-------------YSDEEVWRALELAH-------------LRSFVSGLQLGllsevTEGGD----NLSIG 1436
Cdd:COG0488 82 VLDGDAELRAleaeleeleaklaEPDEDLERLAELQEefealggweaearAEEILSGLGFP-----EEDLDrpvsELSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1437 QRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKefSQCTVITIAH-R--LHTImdSDKIMVLDNGKIVEYgs 1513
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdRyfLDRV--ATRILELDRGKLTLY-- 230
|
250 260
....*....|....*....|
gi 3219824 1514 peellsnRG--SFYLMAKEA 1531
Cdd:COG0488 231 -------PGnySAYLEQRAE 243
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
602-783 |
1.71e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 602 ASVSVDRLERYLGGDDLDTSAIRRVSNFDKAVkFSEASFTWDPdleaTIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAML 681
Cdd:COG1129 225 AELTEDELVRLMVGRELEDLFPKRAAAPGEVV-LEVEGLSVGG----VVRDVSFSVRAGEILGIAGLVGAGRTELARALF 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 682 GEMENVHGHITIQGST--------------AYVP----QQSWIQNGTIKDNILFGS--EY------NEKKYQQVlkACAL 735
Cdd:COG1129 300 GADPADSGEIRLDGKPvrirsprdairagiAYVPedrkGEGLVLDLSIRENITLASldRLsrggllDRRRERAL--AEEY 377
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 3219824 736 LPDLEILPGGDMAEIGekgiNLSGGQKQRVSLARAAYQDADIYILDDP 783
Cdd:COG1129 378 IKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1296-1518 |
1.96e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.75 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELdlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHdLRERLTI 1375
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQ----DPILfsgSLRMNLDPFNKY-------SDEEVWRALELAHLRSFVSglqlgllSEVTEggdnLSIGQRQLLCLG 1444
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLENKAD-------AKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1445 RAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITI-------AHRLhtimdSDKIMVLDNGKIVEYGSPEEL 1517
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHAL 225
|
.
gi 3219824 1518 L 1518
Cdd:PRK13537 226 I 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1312-1518 |
2.11e-11 |
|
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: 64.86 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCL--FRILESAGGQIIIDGIDVASIGLHDlRER--LTIIPQDPILFSGsL 1387
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIPG-V 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1388 RMNLdpfnkysdeevwralelahlrsfvsglqlgLLSEVTEGgdnLSIGQR------QLLCLgravlrKSKILVLDEATA 1461
Cdd:cd03217 93 KNAD------------------------------FLRYVNEG---FSGGEKkrneilQLLLL------EPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1462 AVDLETDSLIQTTIRKEFSQ-CTVITIAH--RLHTIMDSDKIMVLDNGKIVEYGSPEELL 1518
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEgKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELAL 193
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
650-839 |
2.28e-11 |
|
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: 64.49 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVH--GHITIQG----------STAYVPQqswiqngtikDNILF 717
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGrpldkrsfrkIIGYVPQ----------DDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 GseynEKKYQQVLKACALLpdleilpggdmaeigeKGInlSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFN 797
Cdd:cd03213 95 P----TLTVRETLMFAAKL----------------RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 3219824 798 KVVGpnglLA--GKTRIFVTH-----GIHFLpqvDEIVVLGKGTILEKG 839
Cdd:cd03213 153 LLRR----LAdtGRTIICSIHqpsseIFELF---DKLLLLSQGRVIYFG 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
650-846 |
2.43e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.50 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAM--LGEMEN----VHGhITIQGSTA----------YVPQQSWI-QNGTIK 712
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSgdliVDG-LKVNDPKVderlirqeagMVFQQFYLfPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 713 DNILFGSeyneKKYQQVLKACALLPDLEILPGGDMAE-IGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHV 791
Cdd:PRK09493 96 ENVMFGP----LRVRGASKEEAEKQARELLAKVGLAErAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 792 gKHIFNKVVGPnglLA--GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLLD 846
Cdd:PRK09493 172 -RHEVLKVMQD---LAeeGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1312-1517 |
2.62e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 67.05 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLtncLfRILesAG------GQIIIDGIDVASIGLHdlRERLTIIPQDPILFS- 1384
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTL---L-RMI--AGfetpdsGRILLDGRDVTGLPPE--KRNVGMVFQDYALFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1385 ---------GsLRMNldpfnKYSDEE----VWRALELAHLRSFvsglqlgllsevtegGD----NLSIGQRQLLCLGRAV 1447
Cdd:COG3842 92 ltvaenvafG-LRMR-----GVPKAEirarVAELLELVGLEGL---------------ADryphQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1448 LRKSKILVLDEATAAVDLETDSLIQTTIR---KEFsQCTVITIAHrlhtimD-------SDKIMVLDNGKIVEYGSPEEL 1517
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRrlqREL-GITFIYVTH------DqeealalADRIAVMNDGRIEQVGTPEEI 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
649-788 |
2.82e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.57 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 649 TIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAmLGEMENVHGHITIQGSTAY---------------------VPQQSWIQ 707
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRS-INRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 708 NGTIKDNILFGSEYNEKKYQQVLKACALlpdlEILPGGDMAE-----IGEKGINLSGGQKQRVSLARAAYQDADIYILDD 782
Cdd:PRK14239 99 PMSIYENVVYGLRLKGIKDKQVLDEAVE----KSLKGASIWDevkdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
....*.
gi 3219824 783 PLSAVD 788
Cdd:PRK14239 175 PTSALD 180
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
652-839 |
3.06e-11 |
|
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: 64.44 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------STAYVPQQSWIQNG------TIKDNILFGS 719
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaaPPADRPVSMLFQENnlfahlTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 720 ----EYNEKKYQQVLKACAL--LPDLEI-LPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVG 792
Cdd:cd03298 96 spglKLTAEDRQAIEVALARvgLAGLEKrLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 793 KHIFNKVvgpNGLLA--GKTRIFVTHgihflpQVDEI-------VVLGKGTILEKG 839
Cdd:cd03298 165 AEMLDLV---LDLHAetKMTVLMVTH------QPEDAkrlaqrvVFLDNGRIAAQG 211
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1020-1191 |
3.07e-11 |
|
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: 65.91 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFgalgLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWM 1099
Cdd:cd18552 46 IGLF----LLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1100 MCFFGIAGTL-VMICMATP--VFAIIIIPLSILYISVqvfyvaTSRQLRRL-----DSVTKspIYSHFSETVTGLPIIRA 1171
Cdd:cd18552 122 RDPLTVIGLLgVLFYLDWKltLIALVVLPLAALPIRR------IGKRLRKIsrrsqESMGD--LTSVLQETLSGIRVVKA 193
|
170 180
....*....|....*....|....
gi 3219824 1172 F---EHQ-QRFLAWNEKQIDINQK 1191
Cdd:cd18552 194 FgaeDYEiKRFRKANERLRRLSMK 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
650-833 |
3.10e-11 |
|
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: 64.61 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST---------AYVPQQSWI-QNGTIKDNIL-FG 718
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldiaarnriGYLPEERGLyPKMKVIDQLVyLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 719 SEYNEKKYQQVLKACALLPDLEIlpgGDMAEigEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAhVGKHIFNK 798
Cdd:cd03269 96 QLKGLKKEEARRRIDEWLERLEL---SEYAN--KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKD 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 3219824 799 VVgpNGLL-AGKTRIFVTHGIHFLPQV-DEIVVLGKG 833
Cdd:cd03269 170 VI--RELArAGKTVILSTHQMELVEELcDRVLLLNKG 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
650-789 |
3.12e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.47 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHI--------TIQGSTAYVPQQS----WiqnGTIKDNILF 717
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaplaEAREDTRLMFQDArllpW---KKVIDNVGL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 718 GSEYN-EKKYQQVLKACALlpdleilpgGDMAeiGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDA 789
Cdd:PRK11247 105 GLKGQwRDAALQALAAVGL---------ADRA--NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
652-845 |
3.18e-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: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST-----------------AYVPQQ-SWIQNGTIKD 713
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrriGYVFQEaRLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 714 NILFG-----SEYNEKKYQQVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:TIGR02142 95 NLRYGmkrarPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 789 AHVGKHIFNKVVGpnglLAGKTRI---FVTHGI-HFLPQVDEIVVLGKGTILEKGSYRDLL 845
Cdd:TIGR02142 164 DPRKYEILPYLER----LHAEFGIpilYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
650-788 |
3.35e-11 |
|
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: 64.87 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG--------------STAYVPQQSWI-QNGTIKDN 714
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIfRKLTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 715 ILFGSEYNEKKYQQVL-KACALLPDLEILPGGDmaeigEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:cd03218 96 ILAVLEIRGLSKKEREeKLEELLEEFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1313-1512 |
3.88e-11 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 64.24 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIK---SGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGI----DVASIGLHDLRERLTIIPQDPILFSG 1385
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1386 -SLRMNLdpfnkysdEEVWRALELAHLRSFVSGL--QLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAA 1462
Cdd:cd03297 90 lNVRENL--------AFGLKRKRNREDRISVDELldLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1463 VDLETDSLIQ---TTIRKEFsQCTVITIAHRLHTI-MDSDKIMVLDNGKIVEYG 1512
Cdd:cd03297 162 LDRALRLQLLpelKQIKKNL-NIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1312-1518 |
3.91e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.39 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGlHDLRERLTIIPQ-DPILFSGSLRMN 1390
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQfDNLDLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1391 LDPFNKY-------SDEEVWRALELAHLRSFVSglqlgllSEVTEggdnLSIGQRQLLCLGRAVLRKSKILVLDEATAAV 1463
Cdd:PRK13536 135 LLVFGRYfgmstreIEAVIPSLLEFARLESKAD-------ARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1464 DLETDSLIQTTIRKEFSQC-TVITIAHrlhtIMDS-----DKIMVLDNG-KIVEyGSPEELL 1518
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGkTILLTTH----FMEEaerlcDRLCVLEAGrKIAE-GRPHALI 260
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1278-1519 |
4.58e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.30 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1278 APWVTD-KRPPA--DWPRhgeIQFNNYQVRYrPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQI 1354
Cdd:PRK10522 305 APYKAEfPRPQAfpDWQT---LELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1355 IIDGIDVASIGLHDLRERLTIIPQDPILFSgslRMnLDPFNKYSDEEV---WRA-LELAHLRSFVSGLQLGLlsevtegg 1430
Cdd:PRK10522 381 LLDGKPVTAEQPEDYRKLFSAVFTDFHLFD---QL-LGPEGKPANPALvekWLErLKMAHKLELEDGRISNL-------- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1431 dNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDletdsliqTTIRKEFSQC----------TVITIAHRLHTIMDSDKI 1500
Cdd:PRK10522 449 -KLSKGQKKRLALLLALAEERDILLLDEWAADQD--------PHFRREFYQVllpllqemgkTIFAISHDDHYFIHADRL 519
|
250 260
....*....|....*....|
gi 3219824 1501 MVLDNGKIVE-YGSPEELLS 1519
Cdd:PRK10522 520 LEMRNGQLSElTGEERDAAS 539
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
646-788 |
4.76e-11 |
|
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: 63.22 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 646 LEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST--------------AYVP----QQSWIQ 707
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPvtrrsprdairagiAYVPedrkREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 708 NGTIKDNILfgseynekkyqqvlkacalLPDLeilpggdmaeigekginLSGGQKQRVSLARAAYQDADIYILDDPLSAV 787
Cdd:cd03215 92 DLSVAENIA-------------------LSSL-----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
.
gi 3219824 788 D 788
Cdd:cd03215 136 D 136
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
650-845 |
4.99e-11 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 64.72 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHG-HITIQGST-------------AYV-P--QQSWIQNGTIK 712
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedvwelrkriGLVsPalQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 713 DNIL---FGS-----EYNEkkyQQVLKACALLPDLeilpggDMAEIGEKGIN-LSGGQKQRVSLARAAYQDADIYILDDP 783
Cdd:COG1119 99 DVVLsgfFDSiglyrEPTD---EQRERARELLELL------GLAHLADRPFGtLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 784 LSAVDAHvGKHIFNKVVgpnGLLAG---KTRIFVTHGIHFLPQ-VDEIVVLGKGTILEKGSYRDLL 845
Cdd:COG1119 170 TAGLDLG-ARELLLALL---DKLAAegaPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
650-839 |
5.55e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 64.09 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQ-QSWIQNG-TIKDNILF-GSEYN--EK 724
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGlGGGFNPElTGRENIYLnGRLLGlsRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 725 KYQQVLKacallpdlEILpggDMAEIGE------KgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAH----VGKH 794
Cdd:cd03220 118 EIDEKID--------EII---EFSELGDfidlpvK--TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 3219824 795 IFNKVVGpngllaGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKG 839
Cdd:cd03220 185 LRELLKQ------GKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1313-1527 |
5.63e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGID--------VASIGLHDLRERLTIIPQDPI--- 1381
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldhklAAQLGIGIIYQELSVIDELTVlen 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1382 LFSGSLrmnldPFNKYSDEEV--WRALElahLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEA 1459
Cdd:PRK09700 101 LYIGRH-----LTKKVCGVNIidWREMR---VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1460 TAAV-DLETDSL--IQTTIRKEFSqcTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEElLSNRGSFYLM 1527
Cdd:PRK09700 173 TSSLtNKEVDYLflIMNQLRKEGT--AIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSD-VSNDDIVRLM 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
652-846 |
6.93e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 64.24 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGeMENV-HGHITIQGSTAYVPQQSWIQ----------------NGTIKDN 714
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCINL-LEEPdSGTITVDGEDLTDSKKDINKlrrkvgmvfqqfnlfpHLTVLEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 715 ILFGSeynekkyQQVLK---------ACALLpdleilpggDMAEIGEKG----INLSGGQKQRVSLARA-AYqDADIYIL 780
Cdd:COG1126 98 VTLAP-------IKVKKmskaeaeerAMELL---------ERVGLADKAdaypAQLSGGQQQRVAIARAlAM-EPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 781 DDPLSAVDahvgkhifnkvvgP---NGLLA--------GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLLD 846
Cdd:COG1126 161 DEPTSALD-------------PelvGEVLDvmrdlakeGMTMVVVTHEMGFAREVaDRVVFMDGGRIVEEGPPEEFFE 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1312-1519 |
6.95e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGgQIIIDGIDVASIG---LHDLRERLTIIPQDP-------- 1380
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-EIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPnsslnprl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1381 ----ILFSGsLRMNLDPFNKYSDEE-VWRALElahlrsfvsglQLGLLSEV-----TEggdnLSIGQRQLLCLGRAVLRK 1450
Cdd:PRK15134 380 nvlqIIEEG-LRVHQPTLSAAQREQqVIAVME-----------EVGLDPETrhrypAE----FSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1451 SKILVLDEATAAVDLETDSLIQTTIRK--EFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSlqQKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
650-839 |
7.71e-11 |
|
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: 63.54 E-value: 7.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-STAYVPQQSWIQNG------------TIKDNIL 716
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLGfvsdstglydrlTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 717 -FGSEYNekkyqqvLKACALLPDLEILPGG-DMAEIGEK-GINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDahvgk 793
Cdd:cd03266 101 yFAGLYG-------LKGDELTARLEELADRlGMEELLDRrVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD----- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 794 hifnkVVGPNGLL--------AGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKG 839
Cdd:cd03266 169 -----VMATRALRefirqlraLGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1304-1519 |
7.88e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.61 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1304 RYRPELDLvLKGITCNIKSGEKVGVVGRTGAGKSSLTNCL-FRILESA--GGQIIIDGIdvaSIGLHDLRERLTIIPQDP 1380
Cdd:TIGR00955 33 RERPRKHL-LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVkgSGSVLLNGM---PIDAKEMRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1381 IL-----------FSGSLRMnldPFNKYSDE------EVWRALEL---AHLRSFVSGLQLGllsevteggdnLSIGQRQL 1440
Cdd:TIGR00955 109 LFiptltvrehlmFQAHLRM---PRRVTKKEkrervdEVLQALGLrkcANTRIGVPGRVKG-----------LSGGERKR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1441 LCLGRAVLRKSKILVLDEATAAVD-LETDSLIQTTIRKEFSQCTVITIAHR-LHTIMDS-DKIMVLDNGKIVEYGSPEEL 1517
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLDsFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELfDKIILMAEGRVAYLGSPDQA 254
|
..
gi 3219824 1518 LS 1519
Cdd:TIGR00955 255 VP 256
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
619-837 |
7.99e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 63.61 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 619 DTSAIRRVSNFDKAVkfseasftWDPDLEATI-QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-- 695
Cdd:COG4181 4 SSAPIIELRGLTKTV--------GTGAGELTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 696 ---------------STAYVpQQSW--IQNGTIKDNI-----LFGSEYNEKKYQQVLKACALLPDLEILPGGdmaeigek 753
Cdd:COG4181 76 lfaldedararlrarHVGFV-FQSFqlLPTLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 754 ginLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFnkvvgpnGLL------AGKTRIFVTHGIHFLPQVDEI 827
Cdd:COG4181 147 ---LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQII-------DLLfelnreRGTTLVLVTHDPALAARCDRV 216
|
250
....*....|
gi 3219824 828 VVLGKGTILE 837
Cdd:COG4181 217 LRLRAGRLVE 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
650-843 |
8.09e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.68 E-value: 8.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG---------------STAYVPQQSWIQ--NGTIK 712
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPEYQlfEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 713 DNILFG----SEYNEKKYQQVLKACALLpdleilpGGDMAEIGEKG-INLSGGQKQRVSLARAAYQDADIYILDDPLSAV 787
Cdd:PRK13637 103 KDIAFGpinlGLSEEEIENRVKRAMNIV-------GLDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 788 DAHVGKHIFNKVvgpnGLLAGK---TRIFVTHGIHFLPQ-VDEIVVLGKGTILEKGSYRD 843
Cdd:PRK13637 176 DPKGRDEILNKI----KELHKEynmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
651-839 |
8.26e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.82 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------------------STAYVPQQSwiqngtIK 712
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvppaergvgmvfqSYALYPHLS------VA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 713 DNILFG---SEYNEKKYQQVLKACAllpdlEILPGGDMAEIGEKGinLSGGQKQRVSLARAAYQDADIYILDDPLSAVDA 789
Cdd:PRK11000 94 ENMSFGlklAGAKKEEINQRVNQVA-----EVLQLAHLLDRKPKA--LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3219824 790 HVGKHIFNKVVGPNGLLaGKTRIFVTHG-IHFLPQVDEIVVLGKGTILEKG 839
Cdd:PRK11000 167 ALRVQMRIEISRLHKRL-GRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
653-840 |
8.44e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.26 E-value: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 653 VNLDIKPGQLVAVVGTVGSGKSSLV---SAMLGEMENVHGHITIQGST------------------AYVPQQ-SWIQNGT 710
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLrhlSGLITGDKSAGSHIELLGRTvqregrlardirksrantGYIFQQfNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 711 IKDNILFG------------SEYNEKKYQQVLKAcallpdleiLPGGDMAEIGEKGIN-LSGGQKQRVSLARAAYQDADI 777
Cdd:PRK09984 103 VLENVLIGalgstpfwrtcfSWFTREQKQRALQA---------LTRVGMVHFAHQRVStLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 778 YILDDPLSAVDAHVGKHIFNKVVGPNGlLAGKTRIFVTHGIHF-LPQVDEIVVLGKGTILEKGS 840
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQ-NDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGS 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
632-861 |
9.40e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.47 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 632 AVKFSEASFTWDPD--LEAT-IQDVNLDIKPGQLVAVVGTVGSGKSSLV---SAML----GEMENVHGHITIQGSTAYV- 700
Cdd:PRK13641 2 SIKFENVDYIYSPGtpMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLkpssGTITIAGYHITPETGNKNLk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 701 ------------PQQSWIQNGTIKD------NILFGSEYNEKKYQQVLKACALLPDLeilpggdmaeIGEKGINLSGGQK 762
Cdd:PRK13641 82 klrkkvslvfqfPEAQLFENTVLKDvefgpkNFGFSEDEAKEKALKWLKKVGLSEDL----------ISKSPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 763 QRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVgpNGLLAGKTRIFVTHGIHFLPQ-VDEIVVLGKGTILEKGSy 841
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFK--DYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHAS- 228
|
250 260
....*....|....*....|.
gi 3219824 842 rdlldKKGVFA-RNWktFMKH 861
Cdd:PRK13641 229 -----PKEIFSdKEW--LKKH 242
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1301-1520 |
1.22e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.60 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1301 YQVR---YRPElDLV--LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVAS---IGLHDLRER 1372
Cdd:PRK11308 15 YPVKrglFKPE-RLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1373 LTIIPQDPIlfsGSlrmnLDPFNKYSD--EE---VWRALELAHLRSFVSGL--QLGLLSEVTEGGDNL-SIGQRQLLCLG 1444
Cdd:PRK11308 94 IQIVFQNPY---GS----LNPRKKVGQilEEpllINTSLSAAERREKALAMmaKVGLRPEHYDRYPHMfSGGQRQRIAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1445 RAVLRKSKILVLDEATAAVDLEtdslIQTTI-------RKEFSQCTVItIAHRL----HTimdSDKIMVLDNGKIVEYGS 1513
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDVS----VQAQVlnlmmdlQQELGLSYVF-ISHDLsvveHI---ADEVMVMYLGRCVEKGT 238
|
....*..
gi 3219824 1514 PEELLSN 1520
Cdd:PRK11308 239 KEQIFNN 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
647-853 |
1.44e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.60 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 647 EATIQ---DVNLDIKPGQLVAVVGTVGSGKSSLvSAMLGEMEN-VHGHITIQGSTAYVPQQSWIQNGTIKDNILFGSEYN 722
Cdd:PRK11308 25 ERLVKaldGVSFTLERGKTLAVVGESGCGKSTL-ARLLTMIETpTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 723 ----EKKYQQVLKAcallPdLEI---LPGGD--------MAEIGEKGIN-------LSGGQKQRVSLARAAYQDADIYIL 780
Cdd:PRK11308 104 slnpRKKVGQILEE----P-LLIntsLSAAErrekalamMAKVGLRPEHydryphmFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 781 DDPLSAVDAHVGKHIFNkvvgpngLLA------GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGsyrdllDKKGVFAR 853
Cdd:PRK11308 179 DEPVSALDVSVQAQVLN-------LMMdlqqelGLSYVFISHDLSVVEHIaDEVMVMYLGRCVEKG------TKEQIFNN 245
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1291-1490 |
1.52e-10 |
|
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: 65.93 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1291 PRHGEIQFNNYQVRYR------PELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLtnclFRILESA----GGQIIIDGid 1360
Cdd:TIGR00954 440 PGRGIVEYQDNGIKFEniplvtPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSL----FRILGELwpvyGGRLTKPA-- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1361 vasiglhdlRERLTIIPQDPILFSGSLR------MNLDPFNK--YSDEEVWRALELAHLRSFVSglQLGLLSEVTEGGDN 1432
Cdd:TIGR00954 514 ---------KGKLFYVPQRPYMTLGTLRdqiiypDSSEDMKRrgLSDKDLEQILDNVQLTHILE--REGGWSAVQDWMDV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1433 LSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKefSQCTVITIAHR 1490
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1312-1509 |
1.58e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 63.12 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGID--------VASIGLHdLRERLTIIPQDPILf 1383
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkfLRRIGVV-FGQKTQLWWDLPVI- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 sGSLRMNLDPFNKYSDEEVWRALELAHLrsfvsgLQLG-LLSEVTEggdNLSIGQRQLLCLGRAVLRKSKILVLDEATAA 1462
Cdd:cd03267 114 -DSFYLLAAIYDLPPARFKKRLDELSEL------LDLEeLLDTPVR---QLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1463 VDLETdsliQTTIRK------EFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIV 1509
Cdd:cd03267 184 LDVVA----QENIRNflkeynRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1311-1511 |
1.66e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.47 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1311 LVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIdGIDVaSIG-----LHDLRERLTIIpqdpilfsg 1385
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-KIGyfdqhQEELDPDKTVL--------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1386 slrmnldpfnkysdEEVWRALELA---HLRSFvsgLQLGLLSevtegGD-------NLSIGQRQLLCLGRAVLRKSKILV 1455
Cdd:COG0488 398 --------------DELRDGAPGGteqEVRGY---LGRFLFS-----GDdafkpvgVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1456 LDEATAAVDLET-----DSLiqttirKEFsQCTVITIAH-R--LHTImdSDKIMVLDNGKIVEY 1511
Cdd:COG0488 456 LDEPTNHLDIETlealeEAL------DDF-PGTVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
650-845 |
1.66e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.86 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------------STAYVPQQSWIQ-NGTIKDNI 715
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLSfEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 716 LFG--------SEYNEKKYQQVLKAcallpdleiLPGGDMAEIGEKGI-NLSGGQKQRVSLARAAYQDADIYILDDPLSA 786
Cdd:PRK09536 99 EMGrtphrsrfDTWTETDRAAVERA---------MERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 787 VDAHvgkHIFNKVVGPNGLL-AGKTRIFVTHGIHFLPQ-VDEIVVLGKGTILEKGSYRDLL 845
Cdd:PRK09536 170 LDIN---HQVRTLELVRRLVdDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1313-1507 |
2.06e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILE--SAGGQIIIDGIDVASIGLHDLRER--------LTIIPQDPIL 1382
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTERAgiaiihqeLALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1383 ---FSGSlrmNLDPFNKYSDEEVW-RALELahLRsfvsglQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDE 1458
Cdd:PRK13549 101 eniFLGN---EITPGGIMDYDAMYlRAQKL--LA------QLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1459 ATAAV-DLETDSLIqtTIRKEFSQ--CTVITIAHRLHTIMD-SDKIMVLDNGK 1507
Cdd:PRK13549 170 PTASLtESETAVLL--DIIRDLKAhgIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1304-1540 |
2.31e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1304 RYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIiidgidvasiglhdLRER-LTIIPQDPIL 1382
Cdd:PTZ00243 667 FFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAERsIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1383 FSGSLRMNLDPFNKYSDEEVWRALELAHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAA 1462
Cdd:PTZ00243 733 MNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1463 VDLETDSLI-QTTIRKEFSQCTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPEELLsnRGSFYLMAKEAGIENVNHTE 1540
Cdd:PTZ00243 813 LDAHVGERVvEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM--RTSLYATLAAELKENKDSKE 889
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
630-850 |
2.37e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.22 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 630 DKAVKFSEASFTWDPDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSWIQN- 708
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 709 --------------GTIKDNILFGSEYNEKKYQQVLKACAllpdlEILPGGDMAEIGEKG-INLSGGQKQRVSLARAAYQ 773
Cdd:PRK13647 81 vglvfqdpddqvfsSTVWDDVAFGPVNMGLDKDEVERRVE-----EALKAVRMWDFRDKPpYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 774 DADIYILDDPLSAVDAHVGKHIFNKVVGPNGllAGKTRIFVTHGIHFLPQ-VDEIVVLGKGTILEKGSYRDLLDKKGV 850
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHN--QGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1312-1509 |
2.44e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.13 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDL----RERLTIIPQDPILFSG-S 1386
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1387 LRMNLDPFNKYSDEEvwRALELAHLRSFVSglQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLE 1466
Cdd:PRK10535 103 AAQNVEVPAVYAGLE--RKQRLLRAQELLQ--RLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 3219824 1467 TDSLIQTTIRKEFSQC-TVITIAHRLHTIMDSDKIMVLDNGKIV 1509
Cdd:PRK10535 179 SGEEVMAILHQLRDRGhTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
633-847 |
2.90e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPD---LEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-STAYVPQQSWIQN 708
Cdd:PRK13643 2 IKFEKVNYTYQPNspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 709 GTIKDNILFGSEYNEKKYQQVLKACALLPD----------------LEILpgGDMAEIGEKG-INLSGGQKQRVSLARAA 771
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFGPQnfgipkekaekiaaekLEMV--GLADEFWEKSpFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 772 YQDADIYILDDPLSAVDAHVGKHIFNKVVGPNGllAGKTRIFVTHGIHFLPQ-VDEIVVLGKGTILEKGSYRDLLDK 847
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQ--SGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1312-1526 |
3.21e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDV-----ASIglhdLRERLTIIPQDPILFSgs 1386
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtAKI----MREAVAIVPEGRRVFS-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1387 lRM----NLDPFNKYSDEEVWRalelaHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAA 1462
Cdd:PRK11614 94 -RMtveeNLAMGGFFAERDQFQ-----ERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1463 VDLETDSLIQTTIRKEFSQCTVITIAHR--LHTIMDSDKIMVLDNGKIVEYGSPEELLSNRG--SFYL 1526
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDTGDALLANEAvrSAYL 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
650-833 |
3.22e-10 |
|
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: 62.10 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVP---QQSWIQN------GTIKDNIlfgse 720
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNysllpwLTVRENI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 721 ynekkyqqVLKACALLPDLeilPGGDMAEIGEKGINL--------------SGGQKQRVSLARAAYQDADIYILDDPLSA 786
Cdd:TIGR01184 76 --------ALAVDRVLPDL---SKSERRAIVEEHIALvglteaadkrpgqlSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3219824 787 VDAHVGKHIFNKvvgpngLL-----AGKTRIFVTHGI-HFLPQVDEIVVLGKG 833
Cdd:TIGR01184 145 LDALTRGNLQEE------LMqiweeHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1316-1525 |
3.25e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.70 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1316 ITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHdlRERLTIIPQDPILF---------SGS 1386
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFphmtveqniAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1387 LRMNLDPFNKYSDEeVWRALELAHLRSFVSglqlgllsevtEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLE 1466
Cdd:PRK11607 116 LKQDKLPKAEIASR-VNEMLGLVHMQEFAK-----------RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1467 TDSLIQTTIRK--EFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSNRGSFY 1525
Cdd:PRK11607 184 LRDRMQLEVVDilERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1311-1526 |
3.44e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.59 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1311 LVLKGIT-------------CNIKSGEKVGVVGRTGAGKSSLTNcLFRILES-AGGQIIIDGIDVA--SIGLHDlrerLT 1374
Cdd:PRK11432 7 VVLKNITkrfgsntvidnlnLTIKQGTMVTLLGPSGCGKTTVLR-LVAGLEKpTEGQIFIDGEDVThrSIQQRD----IC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1375 IIPQDPILFSG---------SLRMnldpfNKYSDEE----VWRALELAHLRSF----VsglqlgllsevteggDNLSIGQ 1437
Cdd:PRK11432 82 MVFQSYALFPHmslgenvgyGLKM-----LGVPKEErkqrVKEALELVDLAGFedryV---------------DQISGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1438 RQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRkEFSQCTVITIAHRLHTIMD----SDKIMVLDNGKIVEYGS 1513
Cdd:PRK11432 142 QQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR-ELQQQFNITSLYVTHDQSEafavSDTVIVMNKGKIMQIGS 220
|
250
....*....|...
gi 3219824 1514 PEELLSNRGSFYL 1526
Cdd:PRK11432 221 PQELYRQPASRFM 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1313-1520 |
3.66e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.10 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILE-----SAGGQIIIDGIDVAS--IGLHDLRERLTIIPQDPILFSG 1385
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1386 S--------LRMNLDPFNKYSDEEVWRALELAHLRSFVSglqlgllSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLD 1457
Cdd:PRK14239 101 SiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVK-------DRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1458 EATAAVDLETDSLIQTTIRKEFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMN 237
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
650-844 |
3.95e-10 |
|
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: 61.37 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------------STAYVPQQSWIQNG-TIKDNIL 716
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 717 F-----GSEYNEKKYQ--QVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVDA 789
Cdd:cd03263 98 FyarlkGLPKSEIKEEveLLLRVLGLTDKANKRAR-----------TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 790 HVGKHIFNKVvgpNGLLAGKTRIFVTHGIH---FLpqVDEIVVLGKGTILEKGSYRDL 844
Cdd:cd03263 167 ASRRAIWDLI---LEVRKGRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
652-845 |
4.02e-10 |
|
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: 63.58 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST-----------------AYVPQQSwiq-ngTIKD 713
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrriGYVFQEArlfphlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 714 NILFG---SEYNEKKYQ--QVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:COG4148 97 NLLYGrkrAPRAERRISfdEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 789 AHVGKHIfnkvvgpngL-----LAGKTRI---FVTHgihflpQVDEI-------VVLGKGTILEKGSYRDLL 845
Cdd:COG4148 166 LARKAEI---------LpylerLRDELDIpilYVSH------SLDEVarladhvVLLEQGRVVASGPLAEVL 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
630-786 |
4.41e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 630 DKAVKFSEAS----------FTWdPDLEATIQDVNLDIKPGQL-----VAVVGTVGSGKSSLVSAMLGEMENVHGHITIQ 694
Cdd:PRK13409 321 PEPIEFEERPprdeseretlVEY-PDLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 695 GSTAYVPQqsWI---QNGTIKDNI-----LFGSEYnekkYQQvlkacallpdlEILPGGDMAEIGEKGIN-LSGGQKQRV 765
Cdd:PRK13409 400 LKISYKPQ--YIkpdYDGTVEDLLrsitdDLGSSY----YKS-----------EIIKPLQLERLLDKNVKdLSGGELQRV 462
|
170 180
....*....|....*....|.
gi 3219824 766 SLARAAYQDADIYILDDPlSA 786
Cdd:PRK13409 463 AIAACLSRDADLYLLDEP-SA 482
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1312-1523 |
5.18e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.91 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIglHDLRERLTIIPQDPI-LFSGSLRMN 1390
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLV--RDKDGQLKVADKNQLrLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1391 LDPFNKYSDEEVWRALELAHLRsfVSGLQLGLLSE----------VTEGGD-----NLSIGQRQLLCLGRAVLRKSKILV 1455
Cdd:PRK10619 98 FQHFNLWSHMTVLENVMEAPIQ--VLGLSKQEAREravkylakvgIDERAQgkypvHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1456 LDEATAAVDLETDSLIQTTIRKEFSQC-TVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSNRGS 1523
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGkTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
653-846 |
5.53e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 653 VNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG--------STAY------VPQQSWI-QNGTIKDNILF 717
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcarltpAKAHqlgiylVPQEPLLfPNLSVKENILF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 G---SEYNEKKYQQVLKA--CALlpDLEILPGG-DMAEigekginlsggqKQRVSLARAAYQDADIYILDDPLSAVDAHV 791
Cdd:PRK15439 110 GlpkRQASMQKMKQLLAAlgCQL--DLDSSAGSlEVAD------------RQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 792 GKHIFNKVvgpNGLLA-GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLLD 846
Cdd:PRK15439 176 TERLFSRI---RELLAqGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADLST 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
650-846 |
6.50e-10 |
|
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: 62.38 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLG---EMENVHGHITIQGS-----------------TAYVPQ------- 702
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkirgreIQMIFQdpmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 703 -------QswiqngtIKDNILFGSEYNEKKYQQvlKACALLPDLEILPGGDMA-----EigekginLSGGQKQRVSLARA 770
Cdd:COG0444 101 pvmtvgdQ-------IAEPLRIHGGLSKAEARE--RAIELLERVGLPDPERRLdryphE-------LSGGMRQRVMIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 771 AYQDADIYILDDPLSAVDAHVGKHIFNkvvgpngLLA------GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRD 843
Cdd:COG0444 165 LALEPKLLIADEPTTALDVTIQAQILN-------LLKdlqrelGLAILFITHDLGVVAEIaDRVAVMYAGRIVEEGPVEE 237
|
...
gi 3219824 844 LLD 846
Cdd:COG0444 238 LFE 240
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1312-1515 |
6.94e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIidgidvasiglHDLRERLTIIPQ----DPIL-FSGS 1386
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQklylDTTLpLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1387 LRMNLDPFNKYSDeeVWRALE---LAHLRSFvsGLQlgllsevteggdNLSIGQRQLLCLGRAVLRKSKILVLDEATAAV 1463
Cdd:PRK09544 88 RFLRLRPGTKKED--ILPALKrvqAGHLIDA--PMQ------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1464 D----LETDSLIQTtIRKEFSqCTVITIAHRLHTIM-DSDKIMVLdNGKIVEYGSPE 1515
Cdd:PRK09544 152 DvngqVALYDLIDQ-LRRELD-CAVLMVSHDLHLVMaKTDEVLCL-NHHICCSGTPE 205
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
619-786 |
6.96e-10 |
|
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: 63.65 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 619 DTSAIRRVSNFDKAVKFseasftwdPDLEATIQDVNLDIKPGQL-----VAVVGTVGSGKSSLVSAMLGEMENVHGHITI 693
Cdd:COG1245 328 EVHAPRREKEEETLVEY--------PDLTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 694 QGSTAYVPQQ-SWIQNGTIKDNI--LFGSEYNEKKYQQvlkacallpdlEILPGGDMAEIGEKGI-NLSGGQKQRVSLAR 769
Cdd:COG1245 400 DLKISYKPQYiSPDYDGTVEEFLrsANTDDFGSSYYKT-----------EIIKPLGLEKLLDKNVkDLSGGELQRVAIAA 468
|
170
....*....|....*..
gi 3219824 770 AAYQDADIYILDDPlSA 786
Cdd:COG1245 469 CLSRDADLYLLDEP-SA 484
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
643-788 |
6.99e-10 |
|
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: 61.27 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 643 DPDLEATIQDVNLDIKPG-----QLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST-AYVPQQ-SWIQNGTIKDnI 715
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTvSYKPQYiKADYEGTVRD-L 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 716 LFG---SEYNEKKYQQvlkacallpdlEILPGGDMAEIGEKGIN-LSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:cd03237 82 LSSitkDFYTHPYFKT-----------EIAKPLQIEQILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
644-844 |
7.58e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.63 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 644 PDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSWI----------QNG---- 709
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevrktvgivfQNPddql 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 710 ---TIKDNILFG-------SEYNEKKYQQVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYI 779
Cdd:PRK13639 92 fapTVEEDVAFGplnlglsKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 780 LDDPLSAVDAHVGKHIFNKVVGPNGllAGKTRIFVTHGIHFLP-QVDEIVVLGKGTILEKGSYRDL 844
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNK--EGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1312-1517 |
8.10e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.41 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLtnclFRI---LES-AGGQIIIDGIDVAsiGLHDLRERLTIIPQDPILF---- 1383
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIiagLEHqTSGHIRFHGTDVS--RLHARDRKVGFVFQHYALFrhmt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 -----SGSLRM---NLDPFNKYSDEEVWRALELahlrsfvsgLQLGLLSEVTEGgdNLSIGQRQLLCLGRAVLRKSKILV 1455
Cdd:PRK10851 91 vfdniAFGLTVlprRERPNAAAIKAKVTQLLEM---------VQLAHLADRYPA--QLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1456 LDEATAAVDLETDSLIQTTIRK--EFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEEL 1517
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQlhEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1312-1519 |
8.33e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.54 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNL 1391
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1392 DPFNKYSDEEV---WRALELAHLRSFVSGlqLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL--E 1466
Cdd:PRK10253 102 VARGRYPHQPLftrWRKEDEEAVTKAMQA--TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIshQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1467 TDSLiqtTIRKEFSQCTVITIAHRLHTIMDSDK----IMVLDNGKIVEYGSPEELLS 1519
Cdd:PRK10253 180 IDLL---ELLSELNREKGYTLAAVLHDLNQACRyashLIALREGKIVAQGAPKEIVT 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1312-1520 |
8.46e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.01 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILE-----SAGGQIIIDGIDVASIGLH--DLRERLTIIPQDPILF- 1383
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 --------SGSLRMN-LDPFNKYSDEEVWRALELAHLRSFVSglqlgllSEVTEGGDNLSIGQRQLLCLGRAVLRKSKIL 1454
Cdd:PRK14267 99 hltiydnvAIGVKLNgLVKSKKELDERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1455 VLDEATAAVDLETDSLIQTTIRKEFSQCTVITIAHR-LHTIMDSDKIMVLDNGKIVEYGSPEELLSN 1520
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
644-797 |
9.13e-10 |
|
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: 63.23 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 644 PDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSaMLGEMENVHG---HITIQGSTAYVPQQSWIQNGTIKDNILF--- 717
Cdd:TIGR00954 462 PNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYpds 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 718 GSEYNEKKY-QQVLKACALLPDLE-ILP-GGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKH 794
Cdd:TIGR00954 541 SEDMKRRGLsDKDLEQILDNVQLThILErEGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGY 620
|
...
gi 3219824 795 IFN 797
Cdd:TIGR00954 621 MYR 623
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1296-1519 |
9.54e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.72 E-value: 9.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRpeldlvLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAgGQIIIDGIDVASIGLHDL-RERLT 1374
Cdd:PRK03695 1 MQLNDVAVSTR------LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAELaRHRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1375 IIPQDPILFSgslrMnldpfnkysdeEVWRALEL---AHLRSFVSGLQLGLLSEVTEGGD-------NLSIGQRQLLCLG 1444
Cdd:PRK03695 74 LSQQQTPPFA----M-----------PVFQYLTLhqpDKTRTEAVASALNEVAEALGLDDklgrsvnQLSGGEWQRVRLA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1445 RAVLR-------KSKILVLDEATAAVDLETDSLIQTTIRkEFSQ--CTVITIAHRL-HTIMDSDKIMVLDNGKIVEYGSP 1514
Cdd:PRK03695 139 AVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLS-ELCQqgIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRR 217
|
....*
gi 3219824 1515 EELLS 1519
Cdd:PRK03695 218 DEVLT 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1296-1534 |
9.75e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 61.29 E-value: 9.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDlVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTI 1375
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 IPQDP--ILFS---------GSLRMNLDPfnKYSDEEVWRALELAHLRSFVSglqlgllsevtEGGDNLSIGQRQLLCLG 1444
Cdd:PRK13647 84 VFQDPddQVFSstvwddvafGPVNMGLDK--DEVERRVEEALKAVRMWDFRD-----------KPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1445 RAVLRKSKILVLDEATAAVDLETDSLIqTTIRKEFSQ--CTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPeELLSNR 1521
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETL-MEILDRLHNqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLTDE 228
|
250
....*....|...
gi 3219824 1522 GsfylMAKEAGIE 1534
Cdd:PRK13647 229 D----IVEQAGLR 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1311-1520 |
9.83e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.95 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1311 LVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFR---ILES--AGGQIIIDGIDV--ASIGLHDLRERLTIIPQDPILF 1383
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 SGSLRMNLD---PFNKYS---DEEVWRALELAHLRSFVSglqlgllSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLD 1457
Cdd:PRK14243 104 PKSIYDNIAygaRINGYKgdmDELVERSLRQAALWDEVK-------DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1458 EATAAVD----LETDSLIQTTIRkefsQCTVITIAHRLHTIMD-SDKIMVLD---------NGKIVEYGSPEELLSN 1520
Cdd:PRK14243 177 EPCSALDpistLRIEELMHELKE----QYTIIIVTHNMQQAARvSDMTAFFNveltegggrYGYLVEFDRTEKIFNS 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
650-849 |
1.15e-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: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEM--ENVHGHITIQGstayvpqqswiqngtikDNILfgseynekkyq 727
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG-----------------EDIT----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 728 qvlkacALLPDLEILPGGDMA-----EI-GEKGINL--------SGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGK 793
Cdd:cd03217 68 ------DLPPEERARLGIFLAfqyppEIpGVKNADFlryvnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 794 HIFNKVvgpNGLL-AGKTRIFVTHGIHFLPQV--DEIVVLGKGTILEKGSyRDL---LDKKG 849
Cdd:cd03217 142 LVAEVI---NKLReEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGD-KELaleIEKKG 199
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
652-839 |
1.39e-09 |
|
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: 59.51 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGqLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTA------------YVPQQ-SWIQNGTIKDNIlfg 718
Cdd:cd03264 18 GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlkqpqklrrrigYLPQEfGVYPNFTVREFL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 719 seynekKYQQVLK----------ACALLPDLeilpggDMAEIGEKGIN-LSGGQKQRVSLARAAYQDADIYILDDPLSAV 787
Cdd:cd03264 94 ------DYIAWLKgipskevkarVDEVLELV------NLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 788 DAhVGKHIFNKVVGpnGLLAGKTRIFVTH---GIHFLpqVDEIVVLGKGTILEKG 839
Cdd:cd03264 162 DP-EERIRFRNLLS--ELGEDRIVILSTHiveDVESL--CNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
639-853 |
1.57e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.90 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 639 SFTWDPDLEA-TIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGStAYVPQQSW---------IQN 708
Cdd:PRK13650 11 TFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 709 -------GTIKDNILFGSEYNEKKYQQ----VLKACALLpdleilpggDMAEIGEKG-INLSGGQKQRVSLARAAYQDAD 776
Cdd:PRK13650 90 pdnqfvgATVEDDVAFGLENKGIPHEEmkerVNEALELV---------GMQDFKEREpARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 777 IYILDDPLSAVDahvgkhifnkvvgPNGLLA------------GKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDL 844
Cdd:PRK13650 161 IIILDEATSMLD-------------PEGRLEliktikgirddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
....*....
gi 3219824 845 ldkkgvFAR 853
Cdd:PRK13650 228 ------FSR 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
650-788 |
1.59e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.57 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAM-----LGEMENVHGHITIQGSTAYVPQQSWIQ---------------NG 709
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPDVDPVEvrrrigmvfqkpnpfPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 710 TIKDNILFGSEYNEKK------YQQVLKACALLPDLEilpggdmAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDP 783
Cdd:PRK14243 106 SIYDNIAYGARINGYKgdmdelVERSLRQAALWDEVK-------DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
....*
gi 3219824 784 LSAVD 788
Cdd:PRK14243 179 CSALD 183
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1020-1268 |
1.67e-09 |
|
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: 60.94 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWM 1099
Cdd:cd18545 43 ALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1100 MCFFGIAGTLVM----------ICMAT-PVFAIIIIplSILYISVQVFyvatsRQLRRldsvTKSPIYSHFSETVTGLPI 1168
Cdd:cd18545 123 PDLLTLVGIVIImfslnvrlalVTLAVlPLLVLVVF--LLRRRARKAW-----QRVRK----KISNLNAYLHESISGIRV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1169 IRAFEHQQRflawNEKQID-INQKCVFSWITSNRWLAIRLELVGNLVVFCSALLLV-----IYRKTLT-GDVVGFVL--- 1238
Cdd:cd18545 192 IQSFAREDE----NEEIFDeLNRENRKANMRAVRLNALFWPLVELISALGTALVYWyggklVLGGAITvGVLVAFIGyvg 267
|
250 260 270
....*....|....*....|....*....|...
gi 3219824 1239 ---SNALNITQTLNWLVrmtseaeTNIVAVERI 1268
Cdd:cd18545 268 rfwQPIRNLSNFYNQLQ-------SAMASAERI 293
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
650-846 |
1.85e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.97 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST------------AYVPQ-QSWIQNGTIKDNIL 716
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvpsrarharqrvGVVPQfDNLDPDFTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 717 FGSEYNEKKYQQVLKACALLPDLEILPGGDMAEIGEkginLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIF 796
Cdd:PRK13537 103 VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 797 NKVvgpNGLLA-GKTRIFVThgiHFLPQV----DEIVVLGKGTILEKGSYRDLLD 846
Cdd:PRK13537 179 ERL---RSLLArGKTILLTT---HFMEEAerlcDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1311-1509 |
1.98e-09 |
|
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: 59.59 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1311 LVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAG---GQIIIDGIDVASiglHDLRERLTIIPQDPILFSG-- 1385
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGlt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1386 -----------SLRMNLDPFNKYSDEEVWRALELAHLR---SFVSGlqlgllsevteggdnLSIGQRQLLCLGRAVLRKS 1451
Cdd:cd03234 98 vretltytailRLPRKSSDAIRKKRVEDVLLRDLALTRiggNLVKG---------------ISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 1452 KILVLDEATAAVDLET-DSLIQTTIRKEFSQCTVITIAHRLHTIMDS--DKIMVLDNGKIV 1509
Cdd:cd03234 163 KVLILDEPTSGLDSFTaLNLVSTLSQLARRNRIVILTIHQPRSDLFRlfDRILLLSSGEIV 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1312-1464 |
1.98e-09 |
|
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: 59.76 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIID----GIDVASIG---LHDLRER--------LTII 1376
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1377 PQ--------DPIlfsgsLRMNLDPfnkysDEEVWRALE-LAHLrsfvsGLQLGL--LSEVTEGGdnlsiGQRQLLCLGR 1445
Cdd:COG4778 106 PRvsaldvvaEPL-----LERGVDR-----EEARARARElLARL-----NLPERLwdLPPATFSG-----GEQQRVNIAR 165
|
170
....*....|....*....
gi 3219824 1446 AVLRKSKILVLDEATAAVD 1464
Cdd:COG4778 166 GFIADPPLLLLDEPTASLD 184
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1295-1521 |
2.00e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.42 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1295 EIQFNNYQVRYR---PELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIdGIDVASIG-----L 1366
Cdd:PRK13634 2 DITFQKVEHRYQyktPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1367 HDLRERLTIIPQDP--ILFSGSLR-------MNldpFNKYSDEEVWRALELAHLrsfvsglqLGLLSEVTEGGD-NLSIG 1436
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETVEkdicfgpMN---FGVSEEDAKQKAREMIEL--------VGLPEELLARSPfELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1437 QRQLLCLGRAVLRKSKILVLDEATAAVDLETdsliqttiRKE----FSQC------TVITIAHRlhtiMD-----SDKIM 1501
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG--------RKEmmemFYKLhkekglTTVLVTHS----MEdaaryADQIV 217
|
250 260
....*....|....*....|
gi 3219824 1502 VLDNGKIVEYGSPEELLSNR 1521
Cdd:PRK13634 218 VMHKGTVFLQGTPREIFADP 237
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1289-1518 |
2.56e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.80 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1289 DWPRHGEIQFNNYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHD 1368
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1369 LRERLTIIPQDPILFSGSLRMNLDPFNKY------------SDEEVWRALELAHLRSFVSGLQlgllsevteggDNLSIG 1436
Cdd:PRK10575 83 FARKVAYLPQQLPAAEGMTVRELVAIGRYpwhgalgrfgaaDREKVEEAISLVGLKPLAHRLV-----------DSLSGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1437 QRQLLCLGRAVLRKSKILVLDEATAAVDL----ETDSLIQTTIRKEfsQCTVITIahrLHTI-MDS---DKIMVLDNGKI 1508
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQER--GLTVIAV---LHDInMAArycDYLVALRGGEM 226
|
250
....*....|
gi 3219824 1509 VEYGSPEELL 1518
Cdd:PRK10575 227 IAQGTPAELM 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
650-836 |
2.63e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.05 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSL---------------------VSAM----LGEMENVHGHITIQgSTAYVPQQS 704
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLmnilgcldkptsgtyrvagqdVATLdadaLAQLRREHFGFIFQ-RYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 705 WIQNGTIKdNILFGSEYNEKKyqqvLKACALLPDLeilpgGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPL 784
Cdd:PRK10535 103 AAQNVEVP-AVYAGLERKQRL----LRAQELLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3219824 785 SAVDAHVGKHIFNKVVGPNGllAGKTRIFVTHGIHFLPQVDEIVVLGKGTIL 836
Cdd:PRK10535 173 GALDSHSGEEVMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1319-1525 |
2.65e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.51 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1319 NIKSGEKVGVVGRTGAGKSSLTNCLFRILESAG---GQIIIDGIDVASIGLHDLR----ERLTIIPQDPIlfsgslrMNL 1391
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKELNklraEQISMIFQDPM-------TSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1392 DPFNKYSDEevwrALELAHLRSFVSGLQ-----LGLLSEVT--EGGDNL-------SIGQRQLLCLGRAVLRKSKILVLD 1457
Cdd:PRK09473 111 NPYMRVGEQ----LMEVLMLHKGMSKAEafeesVRMLDAVKmpEARKRMkmyphefSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1458 EATAAVDLETDSLIQT---TIRKEFSQcTVITIAHRLHTIMDS-DKIMVLDNGKIVEYGSPEELlsnrgsFY 1525
Cdd:PRK09473 187 EPTTALDVTVQAQIMTllnELKREFNT-AIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDV------FY 251
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1025-1268 |
2.98e-09 |
|
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: 60.14 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1025 ALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFG 1104
Cdd:cd18542 47 GVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1105 IAGTLVMICMATPVFAII---IIPLsILYISVQVF------YVATSRQLRRLDSVTKspiyshfsETVTGLPIIRAF--- 1172
Cdd:cd18542 127 FIGALIIMFSINWKLTLIslaIIPF-IALFSYVFFkkvrpaFEEIREQEGELNTVLQ--------ENLTGVRVVKAFare 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1173 EHQ-QRFLAWNEKQIDINqkcvfswITSNRWLAIR---LELVGNLVVFCSAL---LLVIyRKTLT-GDVVGFVLsnalnI 1244
Cdd:cd18542 198 DYEiEKFDKENEEYRDLN-------IKLAKLLAKYwplMDFLSGLQIVLVLWvggYLVI-NGEITlGELVAFIS-----Y 264
|
250 260
....*....|....*....|....*...
gi 3219824 1245 TQTLNWLVRM----TSEAETNIVAVERI 1268
Cdd:cd18542 265 LWMLIWPVRQlgrlINDMSRASASAERI 292
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
650-845 |
3.13e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.60 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAY----------VPQQSWIQNGTIKDNILFgS 719
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLTMVF-Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 720 EYNEKKYQQVLKACALLPdLEILpGGDMAEIGEKGI------------------NLSGGQKQRVSLARAAYQDADIYILD 781
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAP-IQVL-GLSKQEARERAVkylakvgideraqgkypvHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 782 DPLSAVDAH-VGK--HIFNKVVGpngllAGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLL 845
Cdd:PRK10619 178 EPTSALDPElVGEvlRIMQQLAE-----EGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
651-790 |
3.69e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST------AYVPQQSWI--QNGtIKD------NIL 716
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrqrdEYHQDLLYLghQPG-IKTeltaleNLR 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 717 F----GSEYNEKKYQQVLKACALLpDLEILPGGdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAH 790
Cdd:PRK13538 97 FyqrlHGPGDDEALWEALAQVGLA-GFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1021-1238 |
3.72e-09 |
|
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: 59.81 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1021 GVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDL----LPQTLR 1096
Cdd:cd18546 43 AAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELlqtgLVQLVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1097 SWMMcFFGIAGTLVMI--CMATPVFAIIIiplsILYISVQVFYVATSRQLRRLdSVTKSPIYSHFSETVTGLPIIRAF-- 1172
Cdd:cd18546 123 SLLT-LVGIAVVLLVLdpRLALVALAALP----PLALATRWFRRRSSRAYRRA-RERIAAVNADLQETLAGIRVVQAFrr 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 1173 --EHQQRFLAWNEKQIDINqkcvfswITSNRWLAIR---LELVGNLVVfcSALLLV----IYRKTLT-GDVVGFVL 1238
Cdd:cd18546 197 erRNAERFAELSDDYRDAR-------LRAQRLVAIYfpgVELLGNLAT--AAVLLVgawrVAAGTLTvGVLVAFLL 263
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1313-1511 |
4.22e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDV----------ASIGLhdLRERLTIIPQDPI- 1381
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeAGIGI--IHQELNLIPQLTIa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1382 --LFSGslRMNLDPFNKYSDEEVWRALE--LAHLRSFVSGLQlgLLSEvteggdnLSIGQRQLLCLGRAVLRKSKILVLD 1457
Cdd:PRK10762 98 enIFLG--REFVNRFGRIDWKKMYAEADklLARLNLRFSSDK--LVGE-------LSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1458 EATAAV-DLETDSLIQtTIRKEFSQ-CTVITIAHRLHTIMD-SDKIMVLDNGK-IVEY 1511
Cdd:PRK10762 167 EPTDALtDTETESLFR-VIRELKSQgRGIVYISHRLKEIFEiCDDVTVFRDGQfIAER 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
650-783 |
4.27e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 58.84 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------ST--------AYVPQqswiqnG------ 709
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditglPPhriarlgiGYVPE------Grrifps 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 710 -TIKDNILFGSEY--NEKKYQQVL-KACALLPDLeilpggdmAE-IGEKGINLSGGQKQRVSLARAAYQDADIYILDDP 783
Cdd:COG0410 93 lTVEENLLLGAYArrDRAEVRADLeRVYELFPRL--------KErRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
650-847 |
4.51e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.86 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQ----------GSTAYVPQQSWIQN----------- 708
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKIKNfkelrrrvsmv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 709 ----------GTIKDNILFGS-EYNEKKYQQVLKACALLPDLeilpGGDMAEIGEKGINLSGGQKQRVSLARAAYQDADI 777
Cdd:PRK13631 122 fqfpeyqlfkDTIEKDIMFGPvALGVKKSEAKKLAKFYLNKM----GLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 778 YILDDPLSAVDAHvGKHIFNKVVgPNGLLAGKTRIFVTHGI-HFLPQVDEIVVLGKGTILEKGS-YRDLLDK 847
Cdd:PRK13631 198 LIFDEPTAGLDPK-GEHEMMQLI-LDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTpYEIFTDQ 267
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
650-788 |
7.01e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.31 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAM-----LGEMENVHGHITIQGSTAYVPQQSWIQ----------------N 708
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 709 GTIKDNILFGSEYN---------EKKYQQVLKACALLPDLEilpggdmAEIGEKGINLSGGQKQRVSLARAAYQDADIYI 779
Cdd:PRK14267 100 LTIYDNVAIGVKLNglvkskkelDERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
....*....
gi 3219824 780 LDDPLSAVD 788
Cdd:PRK14267 173 MDEPTANID 181
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1296-1538 |
7.22e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYRPELDLVLKG---ITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIG----LHD 1368
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRAlfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1369 LRERLTIIPQDP--ILFSGSLRMNL--DPFNKYSDEEVWRALELAHLRsfvsglQLGLLSEVTEGGD-NLSIGQRQLLCL 1443
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafGPQNFGIPKEKAEKIAAEKLE------MVGLADEFWEKSPfELSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1444 GRAVLRKSKILVLDEATAAVD----LETDSLIQTTIRkefSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELL 1518
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQ---SGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVF 232
|
250 260
....*....|....*....|
gi 3219824 1519 SNRGsfYLMAKEAGIENVNH 1538
Cdd:PRK13643 233 QEVD--FLKAHELGVPKATH 250
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
642-831 |
8.49e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.80 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 642 WDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------------STAYVPQQSWI-QN 708
Cdd:TIGR01257 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILfHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 709 GTIKDNILFGSEYNEKKYQQV-LKACALLPDLeilpgGDMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAV 787
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEAqLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 3219824 788 DAHVGKHIFNKVVgpnGLLAGKTRIFVTHgihflpQVDEIVVLG 831
Cdd:TIGR01257 1093 DPYSRRSIWDLLL---KYRSGRTIIMSTH------HMDEADLLG 1127
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
650-844 |
9.79e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.18 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSW-IQNgtiKDNILFGSEYNEKKYQQ 728
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRN---KAGMVFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 729 VLKACALLPD-LEILPggdmAEIGE------KGIN-----------LSGGQKQRVSLARAAYQDADIYILDDPLSAVDAH 790
Cdd:PRK13633 103 VEEDVAFGPEnLGIPP----EEIRErvdeslKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3219824 791 VGKHIFNKVVGPNGlLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDL 844
Cdd:PRK13633 179 GRREVVNTIKELNK-KYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
633-845 |
1.13e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.56 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 633 VKFSEASFTWDPDLEATIQ---DVNLDIKPGQLVAVVGTVGSGKSSLVSAM-----------------------LGEMEN 686
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLnalllpdtgtiewifkdeknkkkTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 687 VHGHITIQGST--------------AYVPQQSWIQ--NGTIKDNILFGS-------EYNEKKYQQVLKACALlpDLEILP 743
Cdd:PRK13651 83 VLEKLVIQKTRfkkikkikeirrrvGVVFQFAEYQlfEQTIEKDIIFGPvsmgvskEEAKKRAAKYIELVGL--DESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 744 ggdmaeigEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVGPNglLAGKTRIFVTHGI-HFLP 822
Cdd:PRK13651 161 --------RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN--KQGKTIILVTHDLdNVLE 230
|
250 260
....*....|....*....|...
gi 3219824 823 QVDEIVVLGKGTILEKGSYRDLL 845
Cdd:PRK13651 231 WTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1294-1520 |
1.17e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.10 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1294 GEIQFNNYQVRYRPELDLVLKGI---TCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDV-ASIG---- 1365
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEFKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKkike 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1366 LHDLRERLTIIPQDP--ILFSGSLRMNL--DPFNKYSD-EEVWRAL-ELahlrsfvsgLQLGLLSE--VTEGGDNLSIGQ 1437
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENkQEAYKKVpEL---------LKLVQLPEdyVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1438 RQLLCLGRAVLRKSKILVLDEATAAVDLE-TDSLIQTTIR--KEFSQcTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGS 1513
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKgEEDFINLFERlnKEYKK-RIIMVTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
....*..
gi 3219824 1514 PEELLSN 1520
Cdd:PRK13645 235 PFEIFSN 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
650-830 |
1.24e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS--TAYVPQQSWIQ-----------NGTIKDNIL 716
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdiSTLKPEIYRQQvsycaqtptlfGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 717 FGSEYNEKKYQQVlkacALLPDLEI--LPggdmAEIGEKGIN-LSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHvGK 793
Cdd:PRK10247 103 FPWQIRNQQPDPA----IFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-NK 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 3219824 794 HIFNKVVGPNGLLAGKTRIFVTHGIHFLPQVDEIVVL 830
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1310-1476 |
1.38e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.81 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1310 DLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDvasIGLHDLRERLTII-PQDPILFSGSLR 1388
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLgHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1389 MNLdpfnkysdeEVWRALELAHLRSFVSGL---QLGLLSEVTEGgdNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL 1465
Cdd:PRK13539 92 ENL---------EFWAAFLGGEELDIAAALeavGLAPLAHLPFG--YLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170
....*....|.
gi 3219824 1466 ETDSLIQTTIR 1476
Cdd:PRK13539 161 AAVALFAELIR 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
650-840 |
1.50e-08 |
|
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: 57.06 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS--TAYVPQQSW-------------IQNGTIKDN 714
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdiTGLPPHEIArlgigrtfqiprlFPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 715 ILFGSEYNEKKYQQVLKACALLPDL-----EILpggDMAEIGEKG----INLSGGQKQRVSLARAAYQDADIYILDDP-- 783
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREAreraeELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLDEPaa 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 784 -LSAVDAHVGKHIFNKVVGpngllAGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGS 840
Cdd:cd03219 173 gLNPEETEELAELIRELRE-----RGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGT 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
653-789 |
1.58e-08 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.21 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 653 VNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS----TAYVPQQS--WI--QNG-----TIKDNILFGS 719
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeQRDEPHENilYLghLPGlkpelSALENLHFWA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 720 EYNEKKYQQVLKACAL--LPDLEILPGGdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVDA 789
Cdd:TIGR01189 99 AIHGGAQRTIEDALAAvgLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
652-839 |
1.69e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAM-LGEMENvHGHITIQGST---AYVPQQSWIQNGTIKDNILFgSEYN----- 722
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNHfdfSKTPSDKAIRELRRNVGMVF-QQYNlwphl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 723 ---------EKKYQQVLKACALLPDLEILPGGDMAEIGEK-GINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAhvg 792
Cdd:PRK11124 98 tvqqnlieaPCRVLGLSKDQALARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP--- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 3219824 793 kHIFNKVVGPNGLLA--GKTRIFVTHGIHFLPQVDEIVV-LGKGTILEKG 839
Cdd:PRK11124 175 -EITAQIVSIIRELAetGITQVIVTHEVEVARKTASRVVyMENGHIVEQG 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
651-845 |
1.85e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.17 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLV---------SAmlgemenvhGHITIQG----------------STAYVPQQ-S 704
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIrcinllerpTS---------GSVLVDGvdltalserelraarrKIGMIFQHfN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 705 WIQNGTIKDNILFgseynekkyqqvlkacallPdLEILpGGDMAEIGEK--------GI---------NLSGGQKQRVSL 767
Cdd:COG1135 93 LLSSRTVAENVAL-------------------P-LEIA-GVPKAEIRKRvaellelvGLsdkadaypsQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 768 ARAAYQDADIYILDDPLSAVDAHVGKHIFNkvvgpngLLA------GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGS 840
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILD-------LLKdinrelGLTIVLITHEMDVVRRIcDRVAVLENGRIVEQGP 224
|
....*
gi 3219824 841 YRDLL 845
Cdd:COG1135 225 VLDVF 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1313-1509 |
2.00e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.42 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHD---LRERLTIIPQDPILFsgslrM 1389
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLL-----M 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1390 NLDPFNKYSDEEVWRALELAHLRSFVSGL--QLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDlet 1467
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAAldKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD--- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 3219824 1468 DSLIQTTIR--KEFSQ--CTVITIAHRLHTIMDSD-KIMVLDNGKIV 1509
Cdd:PRK10908 170 DALSEGILRlfEEFNRvgVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
651-846 |
2.01e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.93 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGeMENVHGHITIQG-------STAYVPQQSWIQ------NG------TI 711
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqdldglsRRALRPLRRRMQvvfqdpFGslsprmTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 712 KDNI-----LFGSEYNEKkyQQVLKACALLPDLEiLPGGDMA----EigekginLSGGQKQRVSLARAAYQDADIYILDD 782
Cdd:COG4172 382 GQIIaeglrVHGPGLSAA--ERRARVAEALEEVG-LDPAARHryphE-------FSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 783 PLSAVDAHVGKHIFNkvvgpngLLA------GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLLD 846
Cdd:COG4172 452 PTSALDVSVQAQILD-------LLRdlqrehGLAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
650-788 |
2.13e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.97 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSA---MLGEMENVH--GHITIQGSTAY---------------VPQQSwiqN- 708
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNDLIPGARveGEILLDGEDIYdpdvdvvelrrrvgmVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 709 --GTIKDNILFGSEYNEKKY--------QQVLKACALLPDLEilpggdmAEIGEKGINLSGGQKQRVSLARAAYQDADIY 778
Cdd:COG1117 104 fpKSIYDNVAYGLRLHGIKSkseldeivEESLRKAALWDEVK-------DRLKKSALGLSGGQQQRLCIARALAVEPEVL 176
|
170
....*....|
gi 3219824 779 ILDDPLSAVD 788
Cdd:COG1117 177 LMDEPTSALD 186
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1302-1503 |
2.20e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 56.26 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1302 QVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPI 1381
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1382 LFSGSLRMNLD-PF---NKYSDEEVWRAlELAhlrsfvsglQLGLLSEVTEGGDN-LSIGQRQLLCLGRAVLRKSKILVL 1456
Cdd:PRK10247 92 LFGDTVYDNLIfPWqirNQQPDPAIFLD-DLE---------RFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3219824 1457 DEATAAVD----LETDSLIQTTIRKEfsQCTVITIAHRLHTIMDSDKIMVL 1503
Cdd:PRK10247 162 DEITSALDesnkHNVNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITL 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1316-1508 |
2.60e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.30 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1316 ITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESA-GGQIIIDG--IDVASIgLHDLRERLTIIPQD-------PILFSG 1385
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNP-AQAIRAGIAMVPEDrkrhgivPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1386 SlRMNLDPFNKYSDE-EVWRALELAHLRSFVSGLQLGLLSEVTEGGdNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVD 1464
Cdd:TIGR02633 358 K-NITLSVLKSFCFKmRIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 3219824 1465 L----ETDSLIQTTIRKEFSqctVITIAHRLHTIMD-SDKIMVLDNGKI 1508
Cdd:TIGR02633 436 VgakyEIYKLINQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1296-1519 |
2.84e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.10 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYR---PELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIG----LHD 1368
Cdd:PRK13646 3 IRFDNVSYTYQkgtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1369 LRERLTIIPQDP--ILFSGSL--RMNLDP--FNKYSDEEVWRALELAhlrsfvsgLQLGLLSEVTEGGD-NLSIGQRQLL 1441
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVerEIIFGPknFKMNLDEVKNYAHRLL--------MDLGFSRDVMSQSPfQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1442 CLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRK--EFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELL 1518
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF 234
|
.
gi 3219824 1519 S 1519
Cdd:PRK13646 235 K 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1314-1517 |
2.87e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.73 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1314 KGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGI---DVA----SIGLhdLRERLTIIPQDPILFSGS 1386
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPpaerGVGM--VFQSYALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1387 LRMNLDPFNKYS-DEEVWRALELahlrsfvsgLQLGLLSEvtEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVdl 1465
Cdd:PRK11000 98 FGLKLAGAKKEEiNQRVNQVAEV---------LQLAHLLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL-- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1466 etDSLIQTTIRKEFS------QCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEEL 1517
Cdd:PRK11000 165 --DAALRVQMRIEISrlhkrlGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1060-1268 |
4.59e-08 |
|
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: 56.30 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1060 ILRAPMRFFDTTPTGRIVNRFSgDISTVDDLLPQTLRSWMMCFFGIAGTLV-MICMATPVFAIIIIPLSILYISVQVFYv 1138
Cdd:cd18570 85 LLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIiLFFYNWKLFLITLLIIPLYILIILLFN- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1139 ATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFS---WITSNRWLAIRLELVGNLVV 1215
Cdd:cd18570 163 KPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKlgkLSNLQSSIKGLISLIGSLLI 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1216 FCSALLLVIYRKTLTGDVVGFvlsNAL--NITQTLNWLVRMTSEAETNIVAVERI 1268
Cdd:cd18570 243 LWIGSYLVIKGQLSLGQLIAF---NALlgYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1313-1521 |
5.38e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.79 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRIL---ESAGGQIIIDGIDVASIG--LHDLRE---------------- 1371
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrlARDIRKsrantgyifqqfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1372 RLTIIPQDPILFSGSL---RMNLDPFNKYSDEEVWRALElahlrsfvsglQLGLLSEVTEGGDNLSIGQRQLLCLGRAVL 1448
Cdd:PRK09984 100 RLSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALT-----------RVGMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1449 RKSKILVLDEATAAVDLETDSLIQTTIRkEFSQCTVITIAHRLHTIMDS----DKIMVLDNGKIVEYGSPEELLSNR 1521
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLR-DINQNDGITVVVTLHQVDYAlrycERIVALRQGHVFYDGSSQQFDNER 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
651-833 |
5.44e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.34 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSaML--------GEMEnVHGH-ITIQGSTA-------YVPQQ-SWIQNGTIKD 713
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMK-ILyglyqpdsGEIL-IDGKpVRIRSPRDaialgigMVHQHfMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 714 NILFGSE------YNEKKYQQVLKACALLPDLEILPGgdmAEIGEkginLSGGQKQRVSLARAAYQDADIYILDDPLS-- 785
Cdd:COG3845 100 NIVLGLEptkggrLDRKAARARIRELSERYGLDVDPD---AKVED----LSVGEQQRVEILKALYRGARILILDEPTAvl 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 786 ---AVDAhvgkhifnkvvgpngLLA--------GKTRIFVTHGihfLPQV----DEIVVLGKG 833
Cdd:COG3845 173 tpqEADE---------------LFEilrrlaaeGKSIIFITHK---LREVmaiaDRVTVLRRG 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
578-850 |
6.14e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.29 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 578 SITLFnILRFPLsmLPMVTS--SILQASVSVDRLERY-LGGDDLDTSAIRRVSNFdKAVKFSEASFTWdPDLEATIQDVN 654
Cdd:PRK10522 269 SLTLL-FLRTPL--LSAVGAlpTLLSAQVAFNKLNKLaLAPYKAEFPRPQAFPDW-QTLELRNVTFAY-QDNGFSVGPIN 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 655 LDIKPGQLVAVVGTVGSGKSSLvsAML--GEMENVHGHITIQGST-------AYVPQQSWIqngtIKDNILF----GSEY 721
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTL--AMLltGLYQPQSGEILLDGKPvtaeqpeDYRKLFSAV----FTDFHLFdqllGPEG 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 722 NEKKYQQVLKAcallpdLEILPGGDMAEIGE---KGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVgKHIFNK 798
Cdd:PRK10522 418 KPANPALVEKW------LERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQ 490
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 3219824 799 VVGPNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILE-KGSYRDLLDKKGV 850
Cdd:PRK10522 491 VLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASRDAV 543
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1329-1526 |
6.85e-08 |
|
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: 57.72 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1329 VGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASiGLHDLRERLTIIPQDPILFSgslRMNLDPFNKYSDEEVWRALEL 1408
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFH---HLTVAEHILFYAQLKGRSWEE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1409 AHLRSFVSGLQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRKEFSQCTVITIA 1488
Cdd:TIGR01257 1038 AQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMST 1117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 3219824 1489 HRL-HTIMDSDKIMVLDNGKIVEYGSPEELLSNRGS-FYL 1526
Cdd:TIGR01257 1118 HHMdEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTgFYL 1157
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
650-837 |
7.41e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG------------------------STAYVPQQSW 705
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakhvgfvfqSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 706 IQNGTIKdNILFGSEYNEKKYQ--QVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDP 783
Cdd:PRK10584 106 LENVELP-ALLRGESSRQSRNGakALLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3219824 784 LSAVDAHVGKHIFNKVVGPNGLLAgKTRIFVTHGIHFLPQVDEIVVLGKGTILE 837
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHG-TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
641-835 |
7.62e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.39 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 641 TWDPDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSaMLGEMENV-HGHITIQGS--TAYVPQQSWI----QN----- 708
Cdd:PRK11650 12 SYDGKTQV-IKGIDLDVADGEFIVLVGPSGCGKSTLLR-MVAGLERItSGEIWIGGRvvNELEPADRDIamvfQNyalyp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 709 -GTIKDNILFG--------SEYNEKkyqqVLKACALLpdleilpggdmaEIGE----KGINLSGGQKQRVSLARAAYQDA 775
Cdd:PRK11650 90 hMSVRENMAYGlkirgmpkAEIEER----VAEAARIL------------ELEPlldrKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 776 DIYILDDPLSAVDAHvgkhifnkvvgpngLLA-------------GKTRIFVTHGihflpQV------DEIVVLGKGTI 835
Cdd:PRK11650 154 AVFLFDEPLSNLDAK--------------LRVqmrleiqrlhrrlKTTSLYVTHD-----QVeamtlaDRVVVMNGGVA 213
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1051-1268 |
8.30e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 55.60 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1051 ALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAII---IIPLs 1127
Cdd:cd18564 88 DLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIalaVAPL- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1128 iLYISVQVFY---VATSRQLRRLDSVtkspIYSHFSETVTGLPIIRAF----EHQQRFLAWNEKQIDINQKcvfswitSN 1200
Cdd:cd18564 167 -LLLAARRFSrriKEASREQRRREGA----LASVAQESLSAIRVVQAFgreeHEERRFARENRKSLRAGLR-------AA 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 1201 RwLAIRLELVGNLVVFCsALLLVIY-------RKTLT-GDVVGFV--LSNALNITQTlnwLVRMTSEAETNIVAVERI 1268
Cdd:cd18564 235 R-LQALLSPVVDVLVAV-GTALVLWfgawlvlAGRLTpGDLLVFLayLKNLYKPVRD---LAKLTGRIAKASASAERV 307
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
650-844 |
1.01e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST--------------AYVPQQ-SWIQNGTIKDN 714
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldhklaaqlgiGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 715 ILFGS------------EYNE--KKYQQVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDADIYIL 780
Cdd:PRK09700 101 LYIGRhltkkvcgvniiDWREmrVRAAMMLLRVGLKVDLDEKVA-----------NLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 781 DDPLSAV-DAHVGK--HIFNKVVGpngllAGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDL 844
Cdd:PRK09700 170 DEPTSSLtNKEVDYlfLIMNQLRK-----EGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
650-788 |
1.10e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.51 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITI--------------QGSTAYVPQQSWI-QNGTIKDN 714
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASIfRRLSVYDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 715 ILFGSEYNE--KKYQQVLKACALLPDLEILPGGDmaeigEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:PRK10895 99 LMAVLQIRDdlSAEQREDRANELMEEFHIEHLRD-----SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1306-1517 |
1.10e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1306 RPELDLVlKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQI-------------IIDGIDVASIGLHDLR-E 1371
Cdd:PRK10261 26 QQKIAAV-RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1372 RLTIIPQDPIL-----------FSGSLRMNLDPFNKYSDEEVWRALELAHLRSFVSglqlgLLSEVTEggdNLSIGQRQL 1440
Cdd:PRK10261 105 DMAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQT-----ILSRYPH---QLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1441 LCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIR---KEFSQcTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEE 1516
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqKEMSM-GVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQ 255
|
.
gi 3219824 1517 L 1517
Cdd:PRK10261 256 I 256
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1328-1521 |
1.14e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.63 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1328 VVGRTGAGKSSLTNCLFRILESAGGQIIIDGIdvaSIGLH-------------------DLRERLTIIPQDP--ILFSGS 1386
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDI---YIGDKknnhelitnpyskkiknfkELRRRVSMVFQFPeyQLFKDT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1387 LRMNL--DPFN-KYSDEEvwrALELAHLRSFVSGLQLGLLsEVTEGGdnLSIGQRQLLCLGRAVLRKSKILVLDEATAAV 1463
Cdd:PRK13631 134 IEKDImfGPVAlGVKKSE---AKKLAKFYLNKMGLDDSYL-ERSPFG--LSGGQKRRVAIAGILAIQPEILIFDEPTAGL 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1464 DLETDS-LIQTTIRKEFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLSNR 1521
Cdd:PRK13631 208 DPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
650-845 |
1.26e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 55.10 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTaYVPQQSW---------IQN-------GTIKD 713
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL-LTAENVWnlrrkigmvFQNpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 714 NILFGSEYNEKKYQQVLKACAllpdlEILPGGDMAEIGEKG-INLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAhVG 792
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKRVD-----EALLAVNMLDFKTREpARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP-TG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3219824 793 KHIFNKVVGPNGLLAGKTRIFVTHGIHFLPQVDEIVVLGKGTILEKGSYRDLL 845
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
644-850 |
1.54e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 54.85 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 644 PDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAyvpqqSWIQNGTIK----------- 712
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-----DYSRKGLMKlresvgmvfqd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 713 -DNILF-GSEYNEKKYQQV-LKacalLPDLEILPGGDMAeIGEKGIN---------LSGGQKQRVSLARAAYQDADIYIL 780
Cdd:PRK13636 91 pDNQLFsASVYQDVSFGAVnLK----LPEDEVRKRVDNA-LKRTGIEhlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 781 DDPLSAVDAhVGKHIFNKVVGPNGLLAGKTRIFVTHGIHFLP-QVDEIVVLGKGTILEKGSYRDLLDKKGV 850
Cdd:PRK13636 166 DEPTAGLDP-MGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1313-1509 |
1.85e-07 |
|
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: 55.60 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILE--SAGGQIIIDGIDVASIGLHD--------LRERLTIIPQDPIL 1382
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDteragiviIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1383 ---FSGSlRMNLDPFNKYSDEEVWRALELahLRSfvsgLQLGLLSEVTEGGDnLSIGQRQLLCLGRAVLRKSKILVLDEA 1459
Cdd:TIGR02633 97 eniFLGN-EITLPGGRMAYNAMYLRAKNL--LRE----LQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1460 TAAV-DLETDSLIQttIRKEFSQCTV--ITIAHRLHTIMD-SDKIMVLDNGKIV 1509
Cdd:TIGR02633 169 SSSLtEKETEILLD--IIRDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1052-1268 |
1.94e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 54.44 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1052 LHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFA-IIIIPLSILY 1130
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLAlLVLIPVPLVV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1131 ISVQVF----YVATSRQLRRLDSVTkspiySHFSETVTGLPIIRAF--EH--QQRFLAWNEKQIDINQKCVFSWITSNRW 1202
Cdd:cd18563 158 WGSYFFwkkiRRLFHRQWRRWSRLN-----SVLNDTLPGIRVVKAFgqEKreIKRFDEANQELLDANIRAEKLWATFFPL 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1203 LAIRLELvGNLVVFCSALLLVIyRKTLT-GDVVGFvLSNALNITQTLNWLVRMTSEAETNIVAVERI 1268
Cdd:cd18563 233 LTFLTSL-GTLIVWYFGGRQVL-SGTMTlGTLVAF-LSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
650-788 |
2.01e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS--TAYVPQQSWIqngtikDNILFGSEYNEKKYQ 727
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYL------DTTLPLTVNRFLRLR 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 728 QVLKACALLPDLEILPGGDMAEIGEKgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:PRK09544 94 PGTKKEDILPALKRVQAGHLIDAPMQ--KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1312-1512 |
2.82e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.48 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLfRILESA-GGQIIIDG--------IDVASIGLhdLRERLTIIPQD--- 1379
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEMPrSGTLNIAGnhfdfsktPSDKAIRE--LRRNVGMVFQQynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1380 -PILfsgSLRMNL--DPFN--KYSDEE-VWRALELahlrsfVSGLQLgllsevTEGGD----NLSIGQRQLLCLGRAVLR 1449
Cdd:PRK11124 94 wPHL---TVQQNLieAPCRvlGLSKDQaLARAEKL------LERLRL------KPYADrfplHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1450 KSKILVLDEATAAVDLETDSLIQTTIRkEFSQcTVIT---------IAHRLHTimdsdKIMVLDNGKIVEYG 1512
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIR-ELAE-TGITqvivtheveVARKTAS-----RVVYMENGHIVEQG 223
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1300-1511 |
2.85e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1300 NYQVRYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLfriLESAGGQIIIDGIDVA-----------SIGL-- 1366
Cdd:TIGR00956 766 TYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVL---AERVTTGVITGGDRLVngrpldssfqrSIGYvq 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1367 -HDLR-ERLTIipQDPILFSGSLRMNldpfNKYSDEE----VWRALELAHLRSFVSGLqlgllseVTEGGDNLSIGQRQL 1440
Cdd:TIGR00956 843 qQDLHlPTSTV--RESLRFSAYLRQP----KSVSKSEkmeyVEEVIKLLEMESYADAV-------VGVPGEGLNVEQRKR 909
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1441 LCLGRAVLRKSKILV-LDEATAAVDLETDSLIQTTIRK--EFSQCTVITIAHRLHTIMDS-DKIMVLDNGKIVEY 1511
Cdd:TIGR00956 910 LTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlaDHGQAILCTIHQPSAILFEEfDRLLLLQKGGQTVY 984
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
645-789 |
2.92e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 52.50 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 645 DLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSWI--------QNG-----TI 711
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArgllylghAPGikttlSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 712 KDNILFGSEYNEKkyQQVLKACAL--LPDLEILPGGdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVDA 789
Cdd:cd03231 91 LENLRFWHADHSD--EQVEEALARvgLNGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1020-1199 |
2.94e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 54.09 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWM 1099
Cdd:cd18572 39 VLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1100 MCFFGIAGTLVMICMATP---VFAIIIIPLsILYISvqVFYVATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEH-- 1174
Cdd:cd18572 119 RNLVQLVGGLAFMFSLSWrltLLAFITVPV-IALIT--KVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATee 195
|
170 180 190
....*....|....*....|....*....|..
gi 3219824 1175 --QQRFLAWNEKQIDINQK-----CVFSWITS 1199
Cdd:cd18572 196 reARRYERALDKALKLSVRqalayAGYVAVNT 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
650-788 |
3.59e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.11 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS--TA------------YVPQQSWI-QNGTIKDN 714
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdiTHlpmhkrarlgigYLPQEASIfRKLTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 715 ILFGSEYNEK-KYQQVLKACALLPDLEIlpggdmAEIGE-KGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:COG1137 99 ILAVLELRKLsKKEREERLEELLEEFGI------THLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1312-1520 |
4.15e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 54.69 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKS----SLTNCLFRILESAGGQIIIDGIDVASIGLHDLRE----RLTIIPQDPilf 1383
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEP--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 sgslrMN-LDPF--------------NKYSDEEVW-RALElahlrsfvsglqlgLLSEVteGGDN-----------LSIG 1436
Cdd:COG4172 102 -----MTsLNPLhtigkqiaevlrlhRGLSGAAARaRALE--------------LLERV--GIPDperrldayphqLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1437 QRQ-------LLClgravlrKSKILVLDEATAAVDLeTdslIQTTI-------RKEFsQCTVITIAHRLHTIMD-SDKIM 1501
Cdd:COG4172 161 QRQrvmiamaLAN-------EPDLLIADEPTTALDV-T---VQAQIldllkdlQREL-GMALLLITHDLGVVRRfADRVA 228
|
250
....*....|....*....
gi 3219824 1502 VLDNGKIVEYGSPEELLSN 1520
Cdd:COG4172 229 VMRQGEIVEQGPTAELFAA 247
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1312-1519 |
4.22e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.29 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAG--------GQIIIDGIDVASIGLHDLRERLTIIPQ--DPI 1381
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1382 L-FSGSLRMNLDPF--------NKYSDEEV-WRALELAHLRSFVSglqlgllSEVTeggdNLSIGQRQLLCLGRAV---- 1447
Cdd:PRK13547 96 FaFSAREIVLLGRYpharragaLTHRDGEIaWQALALAGATALVG-------RDVT----TLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1448 -----LRKSKILVLDEATAAVDLETDSLIQTTIR---KEFsQCTVITIAHRLH-TIMDSDKIMVLDNGKIVEYGSPEELL 1518
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRrlaRDW-NLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVL 243
|
.
gi 3219824 1519 S 1519
Cdd:PRK13547 244 T 244
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1296-1507 |
4.29e-07 |
|
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: 50.91 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1296 IQFNNYQVRYrpELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDgidvasiglhdlrerlti 1375
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 ipqdpilfsgslrmnldpfnkysdeevwRALELAHLrsfvsglqlgllsevteggDNLSIGQRQLLCLGRAVLRKSKILV 1455
Cdd:cd03221 61 ----------------------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1456 LDEATAAVDLET-DSLIQTTirKEFsQCTVITIAHRlHTIMDS--DKIMVLDNGK 1507
Cdd:cd03221 94 LDEPTNHLDLESiEALEEAL--KEY-PGTVILVSHD-RYFLDQvaTKIIELEDGK 144
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1312-1476 |
4.49e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 52.11 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRERLTIIPQDPILFSGSLRMNL 1391
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1392 DPFNKY-SDEEVWRALELAHLRSFvsglqlgllsevtegGD----NLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLE 1466
Cdd:cd03231 95 RFWHADhSDEQVEEALARVGLNGF---------------EDrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170
....*....|
gi 3219824 1467 TDSLIQTTIR 1476
Cdd:cd03231 160 GVARFAEAMA 169
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1311-1517 |
5.79e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1311 LVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDLRER-LTIIPQDP-----ILfS 1384
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRlgrglVP-D 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1385 GSLRMNLDpFNKYSDEEVWRA--LELAHLRSFVSGL-------------QLGLLSevteGGdNLsigQRqlLCLGRAVLR 1449
Cdd:COG3845 351 MSVAENLI-LGRYRRPPFSRGgfLDRKAIRAFAEELieefdvrtpgpdtPARSLS----GG-NQ---QK--VILARELSR 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1450 KSKILVLDEATAAVDLETDSLIQTTIRKEFSQ-CTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEEL 1517
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVLLISEDLDEILAlSDRIAVMYEGRIVGEVPAAEA 489
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
657-840 |
6.23e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 54.28 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 657 IKPGQLVAVVGTVGSGKSSLVSAMLGEMEN---VHGHITIQGS----------TAYVPQQS-WIQNGTIKDNILFGSE-- 720
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMpidakemraiSAYVQQDDlFIPTLTVREHLMFQAHlr 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 721 ------YNEKKY--QQVLKACALLP--DLEILPGGDMaeigeKGinLSGGQKQRVSLARAAYQDADIYILDDPLSAVDA- 789
Cdd:TIGR00955 128 mprrvtKKEKRErvDEVLQALGLRKcaNTRIGVPGRV-----KG--LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSf 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 790 ------HVGKHIFNKvvgpngllaGKTRIFVTH--GIHFLPQVDEIVVLGKGTILEKGS 840
Cdd:TIGR00955 201 maysvvQVLKGLAQK---------GKTIICTIHqpSSELFELFDKIILMAEGRVAYLGS 250
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
651-853 |
6.41e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 53.27 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS--TAYVPQQ---------------SWIQNGTIKD 713
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdlTALSEKElrkarrqigmifqhfNLLSSRTVFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 714 NILFgseynekkyqqvlkacallPdLEiLPGGDMAEIGEK--------GI---------NLSGGQKQRVSLARAAYQDAD 776
Cdd:PRK11153 102 NVAL-------------------P-LE-LAGTPKAEIKARvtellelvGLsdkadrypaQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 777 IYILDDPLSAVDAHVGKHIFNKVVGPNGLLaGKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDlldkkgVFAR 853
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINREL-GLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGTVSE------VFSH 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
650-845 |
7.03e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.22 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAM-----LGEMENVHGHITIQGSTAY----------------VPQQswIQN 708
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFkmdvielrrrvqmvfqIPNP--IPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 709 GTIKDNILFGSEYN---------EKKYQQVLKACALLPDLEilpggdmAEIGEKGINLSGGQKQRVSLARAAYQDADIYI 779
Cdd:PRK14247 97 LSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 780 LDDPLSAVDAHVGKHIFNKVVgpnGLLAGKTRIFVThgiHFLPQV----DEIVVLGKGTILEKGSYRDLL 845
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFL---ELKKDMTIVLVT---HFPQQAarisDYVAFLYKGQIVEWGPTREVF 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
652-788 |
7.11e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.34 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIkPGQLV-AVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST-----------------AYVPQQSWI-QNGTIK 712
Cdd:PRK11144 16 TVNLTL-PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLfPHYKVR 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 713 DNILFG-SEYNEKKYQQVLKACALLPDLEILPggdmaeigekgINLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:PRK11144 95 GNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
650-783 |
7.14e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG--------------STAYVPQQSWI-QNGTIKDN 714
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVfSRMTVEEN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 715 ILFGSEYNEKK-YQQ-VLKACALLPDLeilpggdMAEIGEKGINLSGGQKQRVSLARAAYQDADIYILDDP 783
Cdd:PRK11614 101 LAMGGFFAERDqFQErIKWVYELFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
642-846 |
8.41e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.79 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 642 WDP--DLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHI-------TIQGSTAYVPQQSWIQ----- 707
Cdd:PRK15079 28 WQPpkTLKA-VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkdlLGMKDDEWRAVRSDIQmifqd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 708 -------NGTIKDNI----------LFGSEYNEKKYQQVLKAcALLPDLeilpggdmaeigekgIN-----LSGGQKQRV 765
Cdd:PRK15079 107 plaslnpRMTIGEIIaeplrtyhpkLSRQEVKDRVKAMMLKV-GLLPNL---------------INrypheFSGGQCQRI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 766 SLARAAYQDADIYILDDPLSAVDAHVGKHIFNkvvgpngLLA------GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEK 838
Cdd:PRK15079 171 GIARALILEPKLIICDEPVSALDVSIQAQVVN-------LLQqlqremGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVEL 243
|
....*...
gi 3219824 839 GSYRDLLD 846
Cdd:PRK15079 244 GTYDEVYH 251
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
648-841 |
9.69e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 648 ATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLG--EMENVHGHITIQGS--TAYVPQQSwiqngtIKDNILFGSEY-- 721
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdlLELSPEDR------AGEGIFMAFQYpv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 722 ------NEKKYQQVLKACALLPDLEILPGGDMAEIGEKGINL----------------SGGQKQRVSLARAAYQDADIYI 779
Cdd:PRK09580 89 eipgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALlkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 780 LDDPLSAVDAHVGKHIFNkvvGPNGLLAGK-TRIFVTHGIHFLPQV--DEIVVLGKGTILEKGSY 841
Cdd:PRK09580 169 LDESDSGLDIDALKIVAD---GVNSLRDGKrSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSGDF 230
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1055-1124 |
1.50e-06 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 51.75 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1055 QLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQT----LRSWMMCFFGIAG--------TLVMICMATPVFAII 1122
Cdd:cd18573 79 RLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNlsdgLRSLVSGVGGIGMmlyispklTLVMLLVVPPIAVGA 158
|
..
gi 3219824 1123 II 1124
Cdd:cd18573 159 VF 160
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1313-1510 |
1.52e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDV------ASI--GLHDLRERLTIIPQDPI--- 1381
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttAALaaGVAIIYQELHLVPEMTVaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1382 LFSGSLRMNLDPFNKySDEEVWRALELAHLrsfvsGLQLGLLSEVTEggdnLSIGQRQLLCLGRAVLRKSKILVLDEATA 1461
Cdd:PRK11288 100 LYLGQLPHKGGIVNR-RLLNYEAREQLEHL-----GVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1462 AVDL-ETDSLIQtTIRKEFSQCTVIT-IAHRLHTIMD-SDKIMVLDNGKIVE 1510
Cdd:PRK11288 170 SLSArEIEQLFR-VIRELRAEGRVILyVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
650-846 |
1.73e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSWIQngTIKDNI--LFGSEYNEKKYQ 727
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQ--ALRRDIqfIFQDPYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 728 QVLKACALLPDL--EILPGGDMAE--------IGEKGIN-------LSGGQKQRVSLARAAYQDADIYILDDPLSAVDAH 790
Cdd:PRK10261 418 QTVGDSIMEPLRvhGLLPGKAAAArvawllerVGLLPEHawrypheFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 791 VGKHIFNKVVGPNGLLaGKTRIFVTHGIHFLPQVD-EIVVLGKGTILEKGSYRDLLD 846
Cdd:PRK10261 498 IRGQIINLLLDLQRDF-GIAYLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAVFE 553
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
1004-1256 |
2.31e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 51.36 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1004 DNLNGTNNSSSHRDMRIGVFGaLGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFsGD 1083
Cdd:cd18555 30 DNVIVPGNLNLLNVLGIGILI-LFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1084 ISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAIIIIPLSILYISVQVFYVATSRQLRRLDSVTKSPIYSHFSETV 1163
Cdd:cd18555 108 NVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1164 TGLPIIRAFEHQQRFLA-WNE---KQIDINQK--CVFSWITSnrwLAIRLELVGNLVVFCSALLLVIyRKTLT-GDVVGF 1236
Cdd:cd18555 188 YGIETIKSLGSEKNIYKkWENlfkKQLKAFKKkeRLSNILNS---ISSSIQFIAPLLILWIGAYLVI-NGELTlGELIAF 263
|
250 260
....*....|....*....|....*.
gi 3219824 1237 ------VLSNALNITQTLNWLVRMTS 1256
Cdd:cd18555 264 sslagsFLTPIVSLINSYNQFILLKS 289
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
656-849 |
2.52e-06 |
|
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: 49.49 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 656 DIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST-AYVPQQswiqngtikdnilfgseynekkyqqvlkaca 734
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITpVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 735 llpdleilpggdmaeigekgINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIfNKVVGPNGLLAGKTRIFV 814
Cdd:cd03222 70 --------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA-ARAIRRLSEEGKKTALVV 128
|
170 180 190
....*....|....*....|....*....|....*
gi 3219824 815 THGIHFLPQVDEIVVLGKGtilEKGSYRDLLDKKG 849
Cdd:cd03222 129 EHDLAVLDYLSDRIHVFEG---EPGVYGIASQPKG 160
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1021-1237 |
2.58e-06 |
|
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: 50.86 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1021 GVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMM 1100
Cdd:cd18548 43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1101 CFFGIAGTLVMICMATPVFAIIIIpLSILYISVQVFYVAT------SRQLRRLDSVTKSpiyshFSETVTGLPIIRAF-- 1172
Cdd:cd18548 123 APIMLIGAIIMAFRINPKLALILL-VAIPILALVVFLIMKkaiplfKKVQKKLDRLNRV-----VRENLTGIRVIRAFnr 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1173 -EHQ-QRFLAWNEKQIDINqkcvfswITSNRWLAIRLELVgNLVVFCSALL-------LVIYRKTLTGDVVGFV 1237
Cdd:cd18548 197 eDYEeERFDKANDDLTDTS-------LKAGRLMALLNPLM-MLIMNLAIVAilwfgghLINAGSLQVGDLVAFI 262
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1020-1191 |
2.86e-06 |
|
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: 50.87 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLrswM 1099
Cdd:cd18541 43 ALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGI---L 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1100 MCFFGI-AGTLVMICMAT--PVFAII-IIPLSILYISVQVFyvatSRQLRRL-DSVTKSpiYSHFS----ETVTGLPIIR 1170
Cdd:cd18541 120 YLVDALfLGVLVLVMMFTisPKLTLIaLLPLPLLALLVYRL----GKKIHKRfRKVQEA--FSDLSdrvqESFSGIRVIK 193
|
170 180
....*....|....*....|....*
gi 3219824 1171 AF----EHQQRFLAWNEKQIDINQK 1191
Cdd:cd18541 194 AFvqeeAEIERFDKLNEEYVEKNLR 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
657-843 |
3.23e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.80 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 657 IKPGQLVAVVGTVGSGKSSLVSAMLGEME--NVHGHITIQGS---------TAYVPQQSWI-QNGTIKDNILFGS----E 720
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNRkptkqilkrTGFVTQDDILyPHLTVRETLVFCSllrlP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 721 YNEKKYQQVLKACALLPDLEILPGGDMAeIGEKGI-NLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKV 799
Cdd:PLN03211 171 KSLTKQEKILVAESVISELGLTKCENTI-IGNSFIrGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 3219824 800 VGpnglLAGKTRIFVThGIH-----FLPQVDEIVVLGKGTILEKGSYRD 843
Cdd:PLN03211 250 GS----LAQKGKTIVT-SMHqpssrVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
650-834 |
3.53e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEmenvHGHITIQGSTAYVPQQSWIQNGTIKDNILFGSEYnekkyqqv 729
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGY-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 730 lkacallpdleiLPggdmaeIGEKGINLSGGQKQRVSLARAAYQDAD--IYILDDPLSAVDAHVGKHIFNKVvgpNGLLA 807
Cdd:cd03238 79 ------------LT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI---KGLID 137
|
170 180
....*....|....*....|....*...
gi 3219824 808 -GKTRIFVTHGIHFLPQVDEIVVLGKGT 834
Cdd:cd03238 138 lGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1320-1508 |
4.11e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1320 IKSGEKVGVVGRTGAGKSSLTNCLFRILESA-GGQIIIDGIDV----------ASIGL--HDlRERLTIIPQDPILFSGS 1386
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVkirnpqqaiaQGIAMvpED-RKRDGIVPVMGVGKNIT 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1387 LrMNLDPFNKYS--DEevwrALELAHLRSFVSGLQLGLLSEVTEGGdNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVD 1464
Cdd:PRK13549 364 L-AALDRFTGGSriDD----AAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 3219824 1465 L----ETDSLIQTTIRKEFSqctVITIAHRLHTIMD-SDKIMVLDNGKI 1508
Cdd:PRK13549 438 VgakyEIYKLINQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
652-788 |
4.19e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSL--------------VSAMLGEMENVHGHITIQGSTAYVPQqswiqnG-------- 709
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLlsliagarkiqqgrVEVLGGDMADARHRRAVCPRIAYMPQ------Glgknlypt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 710 -TIKDNI-----LFG--SEYNEKKYQQVLKACALLPDLEiLPGGdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILD 781
Cdd:NF033858 93 lSVFENLdffgrLFGqdAAERRRRIDELLRATGLAPFAD-RPAG----------KLSGGMKQKLGLCCALIHDPDLLILD 161
|
....*..
gi 3219824 782 DPLSAVD 788
Cdd:NF033858 162 EPTTGVD 168
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1314-1521 |
4.52e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1314 KGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASiglhdlRERLTIIPQDPILFSGSLRMN--L 1391
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP------RSPLDAVKKGMAYITESRRDNgfF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1392 DPFNKYSDEEVWRALELAHLRSfvsglQLGLLSEVTEGG--------------------DNLSIGQRQLLCLGRAVLRKS 1451
Cdd:PRK09700 354 PNFSIAQNMAISRSLKDGGYKG-----AMGLFHEVDEQRtaenqrellalkchsvnqniTELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1452 KILVLDEATAAVDLETDSLIQTTIRKEFSQC-TVITIAHRLHTIMD-SDKIMVLDNGKIveygspEELLSNR 1521
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGkVILMVSSELPEIITvCDRIAVFCEGRL------TQILTNR 494
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
650-789 |
7.57e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.59 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGemenVHGHITIQGSTAYVPQQ---------------------SWIQN 708
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG----VYPHGTWDGEIYWSGSPlkasnirdteragiviihqelTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 709 GTIKDNILFGSE---------YNEkkyqQVLKACALLPDLEILPGGDMAEIGEKGinlsGGQKQRVSLARAAYQDADIYI 779
Cdd:TIGR02633 93 LSVAENIFLGNEitlpggrmaYNA----MYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLI 164
|
170
....*....|
gi 3219824 780 LDDPLSAVDA 789
Cdd:TIGR02633 165 LDEPSSSLTE 174
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
639-853 |
7.65e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.42 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 639 SFTWDPDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS-------------TAYVPQQS- 704
Cdd:PRK13652 10 CYSYSGSKEA-LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 705 -WIQNGTIKDNILFG-------SEYNEKKYQQVLKACALLPDLEILPGgdmaeigekgiNLSGGQKQRVSLARAAYQDAD 776
Cdd:PRK13652 89 dQIFSPTVEQDIAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 777 IYILDDPLSAVDAHVGKHIFNKVvgpNGLLA--GKTRIFVTHGIHFLPQV-DEIVVLGKGTILEKGSYRDLLDKKGVFAR 853
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFL---NDLPEtyGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
645-844 |
8.23e-06 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 48.52 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 645 DLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSaMLGEM-------ENVHGH------ITIQGSTAYVPQQSWIQNG-T 710
Cdd:cd03265 12 DFEA-VRGVSFRVRRGEIFGLLGPNGAGKTTTIK-MLTTLlkptsgrATVAGHdvvrepREVRRRIGIVFQDLSVDDElT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 711 IKDNI-LFGSEYNEKKYQQVLKAcallpdLEILPGGDMAEIGEKGI-NLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:cd03265 90 GWENLyIHARLYGVPGAERRERI------DELLDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 789 ----AHVGKHIfNKVVGPNGllagkTRIFVThgIHFLPQV----DEIVVLGKGTILEKGSYRDL 844
Cdd:cd03265 164 pqtrAHVWEYI-EKLKEEFG-----MTILLT--THYMEEAeqlcDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
652-796 |
9.33e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-STAYVPQQSWIQNG--------------TIKDNIL 716
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkEIDFKSSKEALENGismvhqelnlvlqrSVMDNMW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 717 FGsEY-------NEKKYQQVLKACALLPDLEILPggdmaeiGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDA 789
Cdd:PRK10982 96 LG-RYptkgmfvDQDKMYRDTKAIFDELDIDIDP-------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
....*..
gi 3219824 790 HVGKHIF 796
Cdd:PRK10982 168 KEVNHLF 174
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1313-1509 |
9.99e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVA--------SIGLHDLRERLTIIPQDPILFS 1384
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskealENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1385 GSL------RMNLDPFNKYSDEEVWRAlelahlrsfvsglQLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDE 1458
Cdd:PRK10982 94 MWLgryptkGMFVDQDKMYRDTKAIFD-------------ELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1459 ATAAVDLETDSLIQTTIRK-EFSQCTVITIAHRLHTIMD-SDKIMVLDNGKIV 1509
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKlKERGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
1028-1225 |
1.02e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 49.00 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1028 LAQGICLLISTLWSIYACR-----NASKALHGQLLTNI----LRAPMRFFDTTPTGRIVNRFSGdISTVDDLLPQTLRSW 1098
Cdd:cd18567 44 LAIGFGLLLLLQALLSALRswlvlYLSTSLNLQWTSNLfrhlLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFVEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1099 MMCFFGIAGTLVMICMATPVFAIIIIPLSILYISVQVFYVatsRQLRRL--DSVTKSPIY-SHFSETVTGLPIIRAFEHQ 1175
Cdd:cd18567 123 LLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALY---PPLRRAteEQIVASAKEqSHFLETIRGIQTIKLFGRE 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3219824 1176 -QRFLAWNEKQID-INqkcvfSWITSNRWLAIRleLVGNLVVFCSALLLVIY 1225
Cdd:cd18567 200 aEREARWLNLLVDaIN-----ADIRLQRLQILF--SAANGLLFGLENILVIY 244
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
1020-1268 |
1.20e-05 |
|
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: 49.01 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLrSWM 1099
Cdd:cd18589 39 ITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENL-SLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1100 McFFGIAGTLVMICMAT-----PVFAIIIIPLSILYIS-VQVFYVATSRQLRrlDSVTKSPIYShfSETVTGLPIIRAFE 1173
Cdd:cd18589 118 M-WYLARGLFLFIFMLWlspklALLTALGLPLLLLVPKfVGKFQQSLAVQVQ--KSLARANQVA--VETFSAMKTVRSFA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1174 HQ----QRFLAWNEKQIDINQK-----CVFSWITSNRWLAIRlelVGNLVVFCSallLVIYRKTLTGDVVGFVLSNaLNI 1244
Cdd:cd18589 193 NEegeaQRYRQRLQKTYRLNKKeaaayAVSMWTSSFSGLALK---VGILYYGGQ---LVTAGTVSSGDLVTFVLYE-LQF 265
|
250 260
....*....|....*....|....
gi 3219824 1245 TQTLNWLVRMTSEAETNIVAVERI 1268
Cdd:cd18589 266 TSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
652-786 |
1.22e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGemenVHGHITIQGSTAYVPQQswIQNGTIKDNilfgseynEKK-----Y 726
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSG----VYPHGTYEGEIIFEGEE--LQASNIRDT--------ERAgiaiiH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 727 QQVlkacALLPDL----------EILPGGDM-------------AEIG------EKGINLSGGQKQRVSLARAAYQDADI 777
Cdd:PRK13549 89 QEL----ALVKELsvleniflgnEITPGGIMdydamylraqkllAQLKldinpaTPVGNLGLGQQQLVEIAKALNKQARL 164
|
....*....
gi 3219824 778 YILDDPLSA 786
Cdd:PRK13549 165 LILDEPTAS 173
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
321-608 |
1.29e-05 |
|
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: 48.93 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 321 SFILKLIHDLLVFLNPQLLKLLI--GFVKSSNSYVWfgyICAILMFAVTLIQSFC--LQSYFqhCFVLGMCVRTTVMSSI 396
Cdd:cd18548 4 APLFKLLEVLLELLLPTLMADIIdeGIANGDLSYIL---RTGLLMLLLALLGLIAgiLAGYF--AAKASQGFGRDLRKDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 397 YKKALTLSNLARKQYTIGETVNLMSVDSQKLMDATNYM-QLVWSSVIQITLSIFFLWR---ELGPSILAGVGVMVLLIPV 472
Cdd:cd18548 79 FEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLlRMLVRAPIMLIGAIIMAFRinpKLALILLVAIPILALVVFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 473 NGVLATKI-RNIQvqnmKNKDKRLKIMNEILSGIKILKYFAWEP----SFQEQVQGIRKKELKNLLRFGQLQSLLIFILQ 547
Cdd:cd18548 159 IMKKAIPLfKKVQ----KKLDRLNRVVRENLTGIRVIRAFNREDyeeeRFDKANDDLTDTSLKAGRLMALLNPLMMLIMN 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 548 ITpiLVSVVTFSVYvLVDSANVLNAE-KAFTSItLFNILrFPLSMLPMVTSSILQASVSVDR 608
Cdd:cd18548 235 LA--IVAILWFGGH-LINAGSLQVGDlVAFINY-LMQIL-MSLMMLSMVFVMLPRASASAKR 291
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
619-840 |
1.45e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.70 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 619 DTSAIRRVSNFDKAVKFSEASFTWDPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLgEMENVHGHITIQGST- 697
Cdd:PRK15134 271 PASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGEIWFDGQPl 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 698 ------AYVPQQSWIQ------NG------TIKDNILFGSEYNEK------KYQQVLKAcallpdleilpggdMAEIG-- 751
Cdd:PRK15134 350 hnlnrrQLLPVRHRIQvvfqdpNSslnprlNVLQIIEEGLRVHQPtlsaaqREQQVIAV--------------MEEVGld 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 752 -----EKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVGpnglLAGKTR---IFVTHGIHFLPQ 823
Cdd:PRK15134 416 petrhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS----LQQKHQlayLFISHDLHVVRA 491
|
250
....*....|....*...
gi 3219824 824 V-DEIVVLGKGTILEKGS 840
Cdd:PRK15134 492 LcHQVIVLRQGEVVEQGD 509
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1312-1467 |
1.56e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.03 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDgIDVASIGlhdlrERLTIIPQDPILFSGSLRMNL 1391
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQFG-----REASLIDAIGRKGDFKDAVEL 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 1392 DPFNKYSDEEVWRalelahlRSFvsglqlgllsevteggDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLET 1467
Cdd:COG2401 119 LNAVGLSDAVLWL-------RRF----------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1023-1129 |
1.58e-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: 48.62 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1023 FGALGLAQGICLLIST-LWSIYACRNASKaLHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDL----LPQTLRS 1097
Cdd:cd18577 53 FVYLGIGSFVLSYIQTaCWTITGERQARR-IRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGigekLGLLIQS 131
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 3219824 1098 WMMCFFGIA-----G---TLVMICMaTPVFAIIIIPLSIL 1129
Cdd:cd18577 132 LSTFIAGFIiafiySwklTLVLLAT-LPLIAIVGGIMGKL 170
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
643-783 |
1.62e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 643 DPDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGST--------------AYVPQ----QS 704
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDitglsprerrrlgvAYIPEdrlgRG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 705 WIQNGTIKDNILFGSeYNEKKYQQ--VLK-------ACALLPDLEILPGGDMAEIGekgiNLSGGQKQRVSLARAAYQDA 775
Cdd:COG3845 347 LVPDMSVAENLILGR-YRRPPFSRggFLDrkairafAEELIEEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDP 421
|
....*...
gi 3219824 776 DIYILDDP 783
Cdd:COG3845 422 KLLIAAQP 429
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
650-855 |
1.64e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVP-------QQSWIQNGTIKdNILFGSEYN 722
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAissglngQLTGIENIELK-GLMMGLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 723 EKKyqqvlkacallpdlEILPGG-DMAEIGeKGIN-----LSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIF 796
Cdd:PRK13545 119 KIK--------------EIIPEIiEFADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 797 NKVvgpNGLLA-GKTRIFVTHGihfLPQVDEIVV----LGKGTILEKGSYRDLLDKKGVFARNW 855
Cdd:PRK13545 184 DKM---NEFKEqGKTIFFISHS---LSQVKSFCTkalwLHYGQVKEYGDIKEVVDHYDEFLKKY 241
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1316-1508 |
1.82e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1316 ITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHD-LRERLTIIPQDP----ILFSGSLRMN 1390
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRqssgLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1391 LDPFNkYSDEEVW--RALELAHLRSFVSglQLGL-LSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLET 1467
Cdd:PRK15439 362 VCALT-HNRRGFWikPARENAVLERYRR--ALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 3219824 1468 DSLIQTTIRKEFSQCT-VITIAHRLHTIMD-SDKIMVLDNGKI 1508
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1020-1127 |
2.05e-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: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWM 1099
Cdd:cd18551 39 LALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLV 118
|
90 100 110
....*....|....*....|....*....|....*....
gi 3219824 1100 MCFFGIAGTLVM-----------ICMATPVFAIIIIPLS 1127
Cdd:cd18551 119 TGVLTVVGAVVLmflldwvltlvTLAVVPLAFLIILPLG 157
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1309-1516 |
2.27e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1309 LDLVLKGITcniksgekvGVVGRTGAGKSSLTNCLFRILESAGGQIIIDG---IDVAS-IGLHDLRERLTIIPQDPILF- 1383
Cdd:PRK11144 19 LTLPAQGIT---------AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQDARLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1384 ----SGSLRMNLDPFNKysdeevwralelAHLRSFVSGLQLG-LLSEVTEggdNLSIGQRQLLCLGRAVLRKSKILVLDE 1458
Cdd:PRK11144 90 hykvRGNLRYGMAKSMV------------AQFDKIVALLGIEpLLDRYPG---SLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3219824 1459 ATAAVDL----ETDSLIQTtIRKEFsQCTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEE 1516
Cdd:PRK11144 155 PLASLDLprkrELLPYLER-LAREI-NIPILYVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1304-1519 |
4.77e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1304 RYRPELDLVLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESA-----GGQIIIDGIDVASIGLHDLR----ERLT 1374
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRgvrgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1375 IIPQDPILfsgslrmNLDPFNKYsDEEVWRALEL-------AHLRSFVSGL-QLGLLSEVTEGGD---NLSIGQRQLLCL 1443
Cdd:PRK15134 96 MIFQEPMV-------SLNPLHTL-EKQLYEVLSLhrgmrreAARGEILNCLdRVGIRQAAKRLTDyphQLSGGERQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1444 GRAVLRKSKILVLDEATAAVDLETDSLIQTTIRkEFSQ---CTVITIAHRLHTIMD-SDKIMVLDNGKIVEYGSPEELLS 1519
Cdd:PRK15134 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLR-ELQQelnMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
652-844 |
5.65e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 47.03 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG-------STAYVPQQSWIQ----------NG--TIK 712
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqditglsGRELRPLRRRMQmvfqdpyaslNPrmTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 713 DNILFGSEYNEkkyqqvlkacallpdleILPGGDMAEIGEK-----GIN----------LSGGQKQRVSLARAAYQDADI 777
Cdd:COG4608 116 DIIAEPLRIHG-----------------LASKAERRERVAEllelvGLRpehadrypheFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 778 YILDDPLSAVDAHVGKHIFNkvvgpngLLA------GKTRIFVTHGIHFLPQV-DEIVV--LGKgtILEKGSYRDL 844
Cdd:COG4608 179 IVCDEPVSALDVSIQAQVLN-------LLEdlqdelGLTYLFISHDLSVVRHIsDRVAVmyLGK--IVEIAPRDEL 245
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1315-1504 |
5.75e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.95 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1315 GITCNIKSGEKVGVVGRTGAGKSSltncLFRIL----ESAGGQIIIDGIDvasigLHDLRERLtiipQDPILFSG----- 1385
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTS----LLRILaglaRPDAGEVLWQGEP-----IRRQRDEY----HQDLLYLGhqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1386 --------SLRMNLDPFNKYSDEEVWRALELAHLRSFvsglqlgllSEVTEGgdNLSIGQRQLLCLGRAVLRKSKILVLD 1457
Cdd:PRK13538 86 kteltaleNLRFYQRLHGPGDDEALWEALAQVGLAGF---------EDVPVR--QLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 3219824 1458 EATAAVDLETDSLIQTTIRKEFSQ--CTVITIAHRLHtiMDSDKIMVLD 1504
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQggMVILTTHQDLP--VASDKVRKLR 201
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1004-1172 |
6.37e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 46.71 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1004 DNLNGTNNSSSHRDMRIGVFGALgLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGD 1083
Cdd:cd18576 24 DAALGGGDTASLNQIALLLLGLF-LLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSND 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1084 ISTVDD----LLPQTLRSwmmCFFGIAGTLVMICMATPVFAIIIIPLSILYISVQVFyvatSRQLRRL-----DSVTKSp 1154
Cdd:cd18576 103 VTQIQDtlttTLAEFLRQ---ILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLF----GRRIRKLskkvqDELAEA- 174
|
170
....*....|....*...
gi 3219824 1155 iYSHFSETVTGLPIIRAF 1172
Cdd:cd18576 175 -NTIVEETLQGIRVVKAF 191
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
650-789 |
6.49e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 45.70 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSL--VSAMLGEMENVHGHITIQG---------STAYVPQQS-WIQNGTIKDNILF 717
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLldVLAGRKTAGVITGEILINGrpldknfqrSTGYVEQQDvHSPNLTVREALRF 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3219824 718 GseynekkyqqvlkacALLpdleilpggdmaeigeKGINLSggQKQRVSLARAAYQDADIYILDDPLSAVDA 789
Cdd:cd03232 103 S---------------ALL----------------RGLSVE--QRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
1010-1147 |
7.01e-05 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 46.77 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1010 NNSSSHRDMRIGVFGALGL--AQGI--CLLISTLWSI---YACRnaskaLHGQLLTNILRAPMRFFDTTPTGRIVNRFSG 1082
Cdd:cd18574 33 TNGDFIEDLKKPALKLLGLylLQSLltFAYISLLSVVgerVAAR-----LRNDLFSSLLRQDIAFFDTHRTGELVNRLTA 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1083 DI----STVDDLLPQTLRSwMMCFFGIAGTLVMICMATPVFAIIIIPLSILyisVQVFYvatSRQLRRL 1147
Cdd:cd18574 108 DVqefkSSFKQCVSQGLRS-VTQTVGCVVSLYLISPKLTLLLLVIVPVVVL---VGTLY---GSFLRKL 169
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1055-1268 |
7.35e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 46.32 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1055 QLLTNILRAPMRFFDTTPTGRIVNRFSGDI----STVDDLLPQTLRSwmmcFFGIAGTLV-MICMATP--VFAIIIIPLS 1127
Cdd:cd18550 77 QLYAHLQRMSLAFFTRTRTGEIQSRLNNDVggaqSVVTGTLTSVVSN----VVTLVATLVaMLALDWRlaLLSLVLLPLF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1128 IL---YISvQVFYVATSRQLRRLDSVTkspiySHFSET--VTGLPIIRAF----EHQQRFLAWNEKQIDINQKCVfswiT 1198
Cdd:cd18550 153 VLptrRVG-RRRRKLTREQQEKLAELN-----SIMQETlsVSGALLVKLFgredDEAARFARRSRELRDLGVRQA----L 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219824 1199 SNRWLAIRLELVGNL---VVFCSALLLVIyRKTLT-GDVVGFVlsnAL--NITQTLNWLVRMTSEAETNIVAVERI 1268
Cdd:cd18550 223 AGRWFFAALGLFTAIgpaLVYWVGGLLVI-GGGLTiGTLVAFT---ALlgRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1060-1238 |
8.95e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 46.38 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1060 ILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAII-IIPLSILYISVqVFYV 1138
Cdd:cd18778 83 LQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLtLIPIPFLALGA-WLYS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1139 ATSRQLRRLDSVTKSPIYSHFSETVTGLPIIRAFEHQQ----RFLAWNEKQIDINQKCVFSWitsnrwlairlELVGNLV 1214
Cdd:cd18778 162 KKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEeeakRFEALSRRYRKAQLRAMKLW-----------AIFHPLM 230
|
170 180 190
....*....|....*....|....*....|....
gi 3219824 1215 VFCSAL--LLVIY---RKTL-----TGDVVGFVL 1238
Cdd:cd18778 231 EFLTSLgtVLVLGfggRLVLageltIGDLVAFLL 264
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
658-788 |
1.04e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.82 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 658 KPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHitiqgstaYVPQQSWiqngtikDNIL--F-GSE---YNEKKYQQVLK 731
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDW-------DEILdeFrGSElqnYFTKLLEGDVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 732 ACALLPDLEILPG---GDMAEI----GEKGI-------------------NLSGGQKQRVSLARAAYQDADIYILDDPLS 785
Cdd:cd03236 89 VIVKPQYVDLIPKavkGKVGELlkkkDERGKldelvdqlelrhvldrnidQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
...
gi 3219824 786 AVD 788
Cdd:cd03236 169 YLD 171
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
1056-1238 |
1.15e-04 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis 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: 349993 [Multi-domain] Cd Length: 295 Bit Score: 45.90 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1056 LLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMICMATPVFAIII---IPLSILYIs 1132
Cdd:cd18549 81 LFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVfalLPLMIIFT- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1133 vqVFY----VATSRQLRRldsvTKSPIYSHFSETVTGLPIIRAF----EHQQRFLAWNEKQIDINQKCVF--SWITSNRW 1202
Cdd:cd18549 160 --IYFnkkmKKAFRRVRE----KIGEINAQLEDSLSGIRVVKAFaneeYEIEKFDEGNDRFLESKKKAYKamAYFFSGMN 233
|
170 180 190
....*....|....*....|....*....|....*.
gi 3219824 1203 LAIRLelvGNLVVFCSALLLVIYRKTLTGDVVGFVL 1238
Cdd:cd18549 234 FFTNL---LNLVVLVAGGYFIIKGEITLGDLVAFLL 266
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1320-1504 |
1.46e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.32 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1320 IKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIiidgidvasiglhDLRERLTIIPQ----DpilFSGSLRMNLDPFN 1395
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQyispD---YDGTVEEFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1396 K------YSDEEVWRALELAHLrsfvsglqlgLLSEVteggDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDS 1469
Cdd:COG1245 427 TddfgssYYKTEIIKPLGLEKL----------LDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 3219824 1470 LIQTTIRK--EFSQCTVITIAHRLHTI-MDSDKIMVLD 1504
Cdd:COG1245 493 AVAKAIRRfaENRGKTAMVVDHDIYLIdYISDRLMVFE 530
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
658-788 |
1.61e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.32 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 658 KPGQLVAVVGTVGSGKSSLVSAMLGEMenvhghitiqgstayVPQQSWIQNGTIKDNIL--F-GSE--------YNEK-- 724
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGEL---------------KPNLGDYDEEPSWDEVLkrFrGTElqdyfkklANGEik 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 725 ---KYQQVlkacALLPDL------EILPG----GDMAEIGEK-GI---------NLSGGQKQRVSLARAAYQDADIYILD 781
Cdd:COG1245 162 vahKPQYV----DLIPKVfkgtvrELLEKvderGKLDELAEKlGLenildrdisELSGGELQRVAIAAALLRDADFYFFD 237
|
....*..
gi 3219824 782 DPLSAVD 788
Cdd:COG1245 238 EPSSYLD 244
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1312-1513 |
1.77e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSL----TNCLFRILESAGGQIIIDGI-----------DVASIGLHDLR-ERLTI 1375
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLlktiASNTDGFHIGVEGVITYDGItpeeikkhyrgDVVYNAETDVHfPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1376 ipQDPILFSGSLRMnldPFNKYS--DEEVWRalelAHLRSFVSGLqLGL-LSEVTEGGDNL----SIGQRQLLCLGRAVL 1448
Cdd:TIGR00956 156 --GETLDFAARCKT---PQNRPDgvSREEYA----KHIADVYMAT-YGLsHTRNTKVGNDFvrgvSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 1449 RKSKILVLDEATAAVD----LETDSLIQTTIRkeFSQCTV-ITIAHRLHTIMDS-DKIMVLDNGKIVEYGS 1513
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDsataLEFIRALKTSAN--ILDTTPlVAIYQCSQDAYELfDKVIVLYEGYQIYFGP 294
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1322-1506 |
1.81e-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: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1322 SGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIdgidvasiglhdlrerltiipqdpilfsgslrMNLDPFNKYSDEE 1401
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------IDGEDILEEVLDQ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1402 VWRALELAHLRSFVSGLQLGLLsevteggdnlsigqrqllcLGRAVLRKSKILVLDEATAAVDLETDSLIQ-------TT 1474
Cdd:smart00382 49 LLLIIVGGKKASGSGELRLRLA-------------------LALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLL 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 3219824 1475 IRKEFSQCTVITIAHRLHTIMD------SDKIMVLDNG 1506
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPallrrrFDRRIVLLLI 147
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
1020-1268 |
1.87e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 45.17 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALGLAQGICLListLWSIYACRNASK---ALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVddllpqtlR 1096
Cdd:cd18543 42 VLLLLALGVAEAVLSF---LRRYLAGRLSLGvehDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV--------Q 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1097 SWMMcfFG--IAGTLVMICMATPVFAIIIIPLSILY-ISVQVFYVATSRQLRRLDSVTKSP------IYSHFSETVTGLP 1167
Cdd:cd18543 111 RFLA--FGpfLLGNLLTLVVGLVVMLVLSPPLALVAlASLPPLVLVARRFRRRYFPASRRAqdqagdLATVVEESVTGIR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1168 IIRAFEHQQRFLAWNEKQIDInqkcVFS------WITSNRWLAI----RLELVGNLVVfcsALLLVIyRKTLT-GDVVGF 1236
Cdd:cd18543 189 VVKAFGRERRELDRFEAAARR----LRAtrlraaRLRARFWPLLealpELGLAAVLAL---GGWLVA-NGSLTlGTLVAF 260
|
250 260 270
....*....|....*....|....*....|....
gi 3219824 1237 V-LSNALN-ITQTLNWLVRMTSEAETnivAVERI 1268
Cdd:cd18543 261 SaYLTMLVwPVRMLGWLLAMAQRARA---AAERV 291
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1026-1237 |
2.23e-04 |
|
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: 45.10 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1026 LGLAQGICLLISTLWSI--------YACRNASKALH---GQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQT 1094
Cdd:cd18554 44 LFTIIGIMFFIFLILRPpveyyrqyFAQWIANKILYdirKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1095 L-RSWM---MCFFGIAGTLVMICMATPVfAIIIIPLSIlyISVQVFYvATSRQLRRLDSVTKSPIYSHFSETVTGLPIIR 1170
Cdd:cd18554 124 LmNIWLdmiTIIIAICIMLVLNPKLTFV-SLVIFPFYI--LAVKYFF-GRLRKLTKERSQALAEVQGFLHERIQGMSVIK 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1171 AFEHQQRflawNEKQID-INQKCVFSWITSNRWLAIRLELVGN-------LVVFCSALLLVIYRKTLtGDVVGFV 1237
Cdd:cd18554 200 SFALEKH----EQKQFDkRNGHFLTRALKHTRWNAKTFSAVNTitdlaplLVIGFAAYLVIEGNLTV-GTLVAFV 269
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
651-695 |
2.40e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.53 E-value: 2.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 3219824 651 QDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQG 695
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM 67
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1313-1515 |
2.52e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.87 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIglhdLRERL-TIIPQD-------PILFS 1384
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNLvAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1385 GSLRMnldpfNKYSdEEVWRALELAHLRSFVSGL--QLGLLSEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAA 1462
Cdd:PRK15056 99 DVVMM-----GRYG-HMGWLRRAKKRDRQIVTAAlaRVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1463 VDLETDSLIQTTIRKEFSQ-CTVITIAHRLHTIMDSDKIMVLDNGKIVEYGSPE 1515
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1313-1518 |
2.63e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1313 LKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDVASIGLHDL-----------RERLTIIPQDPI 1381
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAinhgfalvteeRRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1382 LFSgSLRMNLDPFnkysdEEVWRALELAHLRS----FVSGLQLGLLSEVTEGGdNLSIGQRQLLCLGRAVLRKSKILVLD 1457
Cdd:PRK10982 344 GFN-SLISNIRNY-----KNKVGLLDNSRMKSdtqwVIDSMRVKTPGHRTQIG-SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3219824 1458 EATAAVDL----ETDSLIQTTIRKEFSqctVITIAHRLHTIMD-SDKIMVLDNGK---IVEYG--SPEELL 1518
Cdd:PRK10982 417 EPTRGIDVgakfEIYQLIAELAKKDKG---IIIISSEMPELLGiTDRILVMSNGLvagIVDTKttTQNEIL 484
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
317-609 |
2.77e-04 |
|
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: 44.74 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 317 VILKSFILKLIHDLLVFLNPQLLKLLIGFVKSSNSYVWFGYIcAILMFAVTLIQSF--CLQSYFqhCFVLGMCVRTTVMS 394
Cdd:cd18570 3 LLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNII-SIGLILLYLFQSLlsYIRSYL--LLKLSQKLDIRLIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 395 SIYKKALTL-----SNlaRKqytIGEtvnLMSvdsqKLMDATNYMQLVWSSVIQITLSIFflwrelgpSILAGVGVM--- 466
Cdd:cd18570 80 GYFKHLLKLplsffET--RK---TGE---IIS----RFNDANKIREAISSTTISLFLDLL--------MVIISGIILffy 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 467 --------VLLIPVNGVLA----TKIRNIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFQEQVQGIRKKELKNLLR 534
Cdd:cd18570 140 nwklflitLLIIPLYILIIllfnKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFK 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219824 535 FGQLQSLLIFILQITPILVSVVTF---SVYVLvdsANVLNAEKAFTSITLFNILRFPLSMLPMVTSSILQASVSVDRL 609
Cdd:cd18570 220 LGKLSNLQSSIKGLISLIGSLLILwigSYLVI---KGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
1060-1268 |
3.37e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. 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. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 44.47 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1060 ILRAPMRFFDTTPTGRIVNRFsGDISTVDDLL-PQTLRSWMMCFFGIAGTLVMICMATP--VFAIIIIPLSILyisvqvF 1136
Cdd:cd18568 85 LLSLPLSFFASRKVGDIITRF-QENQKIRRFLtRSALTTILDLLMVFIYLGLMFYYNLQltLIVLAFIPLYVL------L 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1137 YVATSRQLRRLDS---VTKSPIYSHFSETVTGLPIIRAFEHQQRFLAWNEKQIDINQKCVFSWITsnrwLAIRLELVGNL 1213
Cdd:cd18568 158 TLLSSPKLKRNSReifQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQK----LSIVLQLISSL 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3219824 1214 --------VVFCSAlLLVIYRKTLTGDVVGFvlsNAL--NITQTLNWLVRMTSEAETNIVAVERI 1268
Cdd:cd18568 234 inhlgtiaVLWYGA-YLVISGQLTIGQLVAF---NMLfgSVINPLLALVGLWDELQETRISVERL 294
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1059-1178 |
4.49e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 44.01 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1059 NILRAPMRFFDTTPTGRIVNRFSGDISTVDDL----LPQTLRSWMMcffgIAGTLVMICMATP---VFAIIIIPLSILYI 1131
Cdd:cd18575 78 HLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVvgssLSIALRNLLL----LIGGLVMLFITSPkltLLVLLVIPLVVLPI 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 3219824 1132 svqvfyVATSRQLRRLDSVTKSPI---YSHFSETVTGLPIIRAFEHQ----QRF 1178
Cdd:cd18575 154 ------ILFGRRVRRLSRASQDRLadlSAFAEETLSAIKTVQAFTREdaerQRF 201
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1312-1519 |
4.90e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1312 VLKGITCNIKSGEKVGVVGRTGAGKSSLTNCLFRILESAG--GQIIIDGIDVASiglhDLRERLTIIPQDPIL------- 1382
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDILyphltvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1383 ----FSGSLRMNldpfNKYSDEEVWRALElahlrSFVSGLQLGLLSEVTEGGD---NLSIGQRQLLCLGRAVLRKSKILV 1455
Cdd:PLN03211 159 etlvFCSLLRLP----KSLTKQEKILVAE-----SVISELGLTKCENTIIGNSfirGISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1456 LDEATAAVDLETD-SLIQTTIRKEFSQCTVITIAH----RLHTIMDSdkIMVLDNGKIVEYGSPEELLS 1519
Cdd:PLN03211 230 LDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHqpssRVYQMFDS--VLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
756-788 |
4.99e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 4.99e-04
10 20 30
....*....|....*....|....*....|...
gi 3219824 756 NLSGGQKQRVSLARAAYQDADIYILDDPLSAVD 788
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
652-846 |
5.33e-04 |
|
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: 44.29 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 652 DVNLDIKPGQLVAVVGTVGSGKSslVSAM--LGEMEnvHGHITIQGStayvpqqswiqngtikdnILFGSeynekkyQQV 729
Cdd:COG4172 28 GVSFDIAAGETLALVGESGSGKS--VTALsiLRLLP--DPAAHPSGS------------------ILFDG-------QDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 730 LKacalLPDLEI--LPGGDMA------------------EIGE-----KGIN---------------------------- 756
Cdd:COG4172 79 LG----LSERELrrIRGNRIAmifqepmtslnplhtigkQIAEvlrlhRGLSgaaararalellervgipdperrldayp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 757 --LSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNkvvgpngLLAGKTR------IFVTH--GI--HFlpqV 824
Cdd:COG4172 155 hqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILD-------LLKDLQRelgmalLLITHdlGVvrRF---A 224
|
250 260
....*....|....*....|..
gi 3219824 825 DEIVVLGKGTILEKGSYRDLLD 846
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFA 246
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
650-876 |
5.67e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGSTAYVPQQSWIqNGTIK--DNILFGSEYNEKKYQ 727
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGQLTgiENIEFKMLCMGFKRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 728 QVLKacaLLPdlEILPGGDMAE-IGEKGINLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKHIFNKVVGPNGll 806
Cdd:PRK13546 119 EIKA---MTP--KIIEFSELGEfIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKE-- 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219824 807 AGKTRIFVTHGIHflpQVDE----IVVLGKGTILEKGSYRDLLDKKGVFArnwKTFMKHSGPEGEATVNNDSEA 876
Cdd:PRK13546 192 QNKTIFFVSHNLG---QVRQfctkIAWIEGGKLKDYGELDDVLPKYEAFL---NDFKKKSKAEQKEFRNKLDES 259
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1056-1112 |
6.59e-04 |
|
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: 43.45 E-value: 6.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 3219824 1056 LLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLPQTLRSWMMCFFGIAGTLVMI 1112
Cdd:cd18784 75 LFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFM 131
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1431-1510 |
8.97e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1431 DNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDlETDS-----LIqttirKEFSQ--CTVITIAHRLHTIMD-SDKIMV 1502
Cdd:NF040905 138 TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALN-EEDSaalldLL-----LELKAqgITSIIISHKLNEIRRvADSITV 211
|
....*...
gi 3219824 1503 LDNGKIVE 1510
Cdd:NF040905 212 LRDGRTIE 219
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
651-816 |
9.91e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 651 QDVNLDikPGQLVAVVGTVGSGKSSLVSAM----LGEMENVHGHITIQgSTAYVPQQSWIQNGTIkdnilfgseynekky 726
Cdd:cd03227 14 NDVTFG--EGSLTIITGPNGSGKSTILDAIglalGGAQSATRRRSGVK-AGCIVAAVSAELIFTR--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 727 qqvlkacallpdleilpggdmaeigekgINLSGGQKQRVSLA----RAAYQDADIYILDDPLSAVDAHVGKHIFNKVvgp 802
Cdd:cd03227 76 ----------------------------LQLSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDPRDGQALAEAI--- 124
|
170
....*....|....*
gi 3219824 803 NGLLAGKTR-IFVTH 816
Cdd:cd03227 125 LEHLVKGAQvIVITH 139
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1326-1345 |
1.32e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 42.83 E-value: 1.32e-03
10 20
....*....|....*....|
gi 3219824 1326 VGVVGRTGAGKSSLTNCLFR 1345
Cdd:COG3596 42 IALVGKTGAGKSSLINALFG 61
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
650-799 |
1.38e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.86 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 650 IQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHI------------TIQGSTAYVPQQSWIQ-NGTIKDNIL 716
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqsikkdlcTYQKQLCFVGHRSGINpYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 717 FGSEYNEKKYqQVLKACAL--LPDLEILPGGdmaeigekgiNLSGGQKQRVSLARAAYQDADIYILDDPLSAVDAHVGKH 794
Cdd:PRK13540 97 YDIHFSPGAV-GITELCRLfsLEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
....*
gi 3219824 795 IFNKV 799
Cdd:PRK13540 166 IITKI 170
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1325-1383 |
2.76e-03 |
|
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: 39.14 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1325 KVGVVGRTGAGKSSLTNCL------------------FRILESAGGQI-IID---GIDVASIGLHDLRERLTIIPQDPIL 1382
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALtgakaivsdypgttrdpnEGRLELKGKQIiLVDtpgLIEGASEGEGLGRAFLAIIEADLIL 80
|
.
gi 3219824 1383 F 1383
Cdd:pfam01926 81 F 81
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
620-786 |
3.21e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.91 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 620 TSAIRRVSNFDKavkfseaSFtwdPDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLVSAMLGEMENVHGHITIQGS--T 697
Cdd:PRK10762 1 MQALLQLKGIDK-------AF---PGVKA-LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 698 AYVPQQS-------------WIQNGTIKDNILFGSEYN--------EKKYQQvlkACALLPDLEILPGGDMAeIGEkgin 756
Cdd:PRK10762 70 FNGPKSSqeagigiihqelnLIPQLTIAENIFLGREFVnrfgridwKKMYAE---ADKLLARLNLRFSSDKL-VGE---- 141
|
170 180 190
....*....|....*....|....*....|
gi 3219824 757 LSGGQKQRVSLARAAYQDADIYILDDPLSA 786
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
1020-1177 |
3.26e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 41.24 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALGLAQGICLLISTLWSIYACRNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDL----LPQtl 1095
Cdd:cd18584 40 LLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDGYfaryLPQ-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1096 rswmmcffgiagtLVMICMATPVFAIIIIPLS-----ILYIS---VQVFYV--------ATSRQLRRLDSVTkspiySHF 1159
Cdd:cd18584 118 -------------LVLAAIVPLLILVAVFPLDwvsalILLVTaplIPLFMIligkaaqaASRRQWAALSRLS-----GHF 179
|
170 180
....*....|....*....|
gi 3219824 1160 SETVTGLPIIRAF--EHQQR 1177
Cdd:cd18584 180 LDRLRGLPTLKLFgrARAQA 199
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1020-1165 |
4.13e-03 |
|
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: 40.93 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219824 1020 IGVFGALGLAQGIclliSTLWSIYAC----RNASKALHGQLLTNILRAPMRFFDTTPTGRIVNRFSGDISTVDDLLpqtl 1095
Cdd:cd18540 45 ILLYLGLILIQAL----SVFLFIRLAgkieMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEII---- 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3219824 1096 rSWMM-----CFFGIAGTLVMICMATPVFAIIII----PLSILYISVQVFYVATSRQLRRLDSVtkspIYSHFSETVTG 1165
Cdd:cd18540 117 -SWGLvdlvwGITYMIGILIVMLILNWKLALIVLavvpVLAVVSIYFQKKILKAYRKVRKINSR----ITGAFNEGITG 190
|
|
| |
