|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
193-1449 |
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: 831.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 193 LSDPLLTKNPRKESarlaTAGFFSILSFSWMNPLLSLGFKKPLSPEDIPSVVPEDEAQLAYKKFSQAW------------ 260
Cdd:TIGR00957 192 FSETNHDPNPCPES----SASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWkkeckktrkqpv 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 261 ------------------------DTLLGdESSTKERN-LVFRAVVKVYFKENIFIAVFAFLRTFAVVSLPLMLYVFVDY 315
Cdd:TIGR00957 268 savygkkdpskpkgssqldaneevEALIV-KSPHKPRKpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRF 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 316 ANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYKKQLKLSSLGRKRHSSGEIVNYIAVDAY 395
Cdd:TIGR00957 347 VNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 396 RMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKMLQNCQTQFMIAQDKRLRSTSEILNSM 475
Cdd:TIGR00957 427 RFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGI 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 476 KVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVF-LGCALLKSAPLNASTIFTVLATLRVM 554
Cdd:TIGR00957 507 KVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFaVYVTVDENNILDAEKAFVSLALFNIL 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 555 SEPVKIIPDAISAIIQGNVSFQRLNNFLLDDELKMDEIERSGL-DASGTAVDIQVGNFGWePETKIPTLRNIHLEIKHGQ 633
Cdd:TIGR00957 587 RFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIkPGEGNSITVHNATFTW-ARDLPPTLNGITFSIPEGA 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 634 KVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNG 713
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEI 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 714 FGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCV--EDSLKEKTVILVTHQVEFL 791
Cdd:TIGR00957 746 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYL 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 792 SEVDQILVMEEGTITQSGKYEELLMMGTAFQQLVNAHndavtvlplASNESLGDLRKEGKDREIRNMTVVEKIEEEIEKT 871
Cdd:TIGR00957 826 PQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTY---------APDEQQGHLEDSWTALVSGEGKEAKLIENGMLVT 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 872 DIPGVQ------------------------------------LTQEEEKESGYVGMKPFLDYIGvSRGWCLLWSSVLGQV 915
Cdd:TIGR00957 897 DVVGKQlqrqlsasssdsgdqsrhhgssaelqkaeakeetwkLMEADKAQTGQVELSVYWDYMK-AIGLFITFLSIFLFV 975
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 916 GFVVFQAASTYWLAFAIGIPKITNT-----MLIGVYSIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLF 990
Cdd:TIGR00957 976 CNHVSALASNYWLSLWTDDPMVNGTqnntsLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSF 1055
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 991 FDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQDYYLASARELIRI 1070
Cdd:TIGR00957 1056 FERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRL 1135
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1071 NGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQN-VTLFtcALLLILIP 1149
Cdd:TIGR00957 1136 ESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNcIVLF--AALFAVIS 1213
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1150 KGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYMNIPEEPPAIIDDKRPPSSWPSNGTIHLQELKIR 1229
Cdd:TIGR00957 1214 RHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLR 1293
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1230 YRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFR 1309
Cdd:TIGR00957 1294 YREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFS 1373
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1310 GCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASID 1389
Cdd:TIGR00957 1374 GSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1390 SATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYF 1449
Cdd:TIGR00957 1454 LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-1453 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 811.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 33 IAFVNLLFLCIFYLFLIASCVSTH-FIVRGRKKGWIFVAVAICCAITSFIFLGVGLNSL-IHGGNDVTEISWVACFVEGI 110
Cdd:PLN03130 41 ISHLVLLGLCLYRIWLIKKDHKVQrFCLRSKWYNYFLALLAAYCTAEPLFRLVMGISVLnLDGQTSLPPFEIVSLIVEAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 111 IWVSLAVSLLVNGSKWVNILVsvWWVSFALLDLVAKSGILLQ---------GNGIRILDILTLPMSLLLLLCSWMNLRS- 180
Cdd:PLN03130 121 TWCSMLVMIGVETKIYIREFR--WYVRFAVIYVLVGDAVMLNlvlsvkeyySSFVLYLYISEVAAQVLFGILLLVYFPNl 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 181 -----SSAAAQDCSVTGLSDPLLTKN---PRKEsarlatAGFFSILSFSWMNPLLSLGFKKPLSPEDIPSVVPEDEAQLA 252
Cdd:PLN03130 199 dpypgYTPIGSESVDDYEYEELPGGEqicPERH------ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 253 YKKFSQAWDtllgdESSTKERNLVFRAVVKVYFKENIFIAVFAFLRTFAVVSLPLMLyvfvdyaNSDHRDLRNG-----F 327
Cdd:PLN03130 273 YRSFQKCWD-----EELKKPKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLL-------NLLLESMQNGepawiG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 328 FNLACLVMLKLVESLTMRHWYFAS-RRSGMRIRSALMVAAYKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHS 406
Cdd:PLN03130 341 YIYAFSIFVGVVLGVLCEAQYFQNvMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 407 GWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDE 486
Cdd:PLN03130 421 LWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENS 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 487 FKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVFlGCALLKSAPLNASTIFTVLATLRVMSEPVKIIPDAIS 566
Cdd:PLN03130 501 FQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSF-GVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLIT 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 567 AIIQGNVSFQRLNNFLLDDELKMdeIERSGLDASGTAVDIQVGNFGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKS 646
Cdd:PLN03130 580 QAVNANVSLKRLEELLLAEERVL--LPNPPLEPGLPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKT 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 647 SLLHAVLGEIPKVS-GTVKVFGSIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQR 725
Cdd:PLN03130 658 SLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGER 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 726 GINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTI 805
Cdd:PLN03130 738 GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 806 TQSGKYEELLMMGTAFQQLV-NAHNDAVTVlplASNESLGDLRKEGKDREIRNMTVVEKIEEEIEKTDIPGVQLTQEEEK 884
Cdd:PLN03130 818 KEEGTYEELSNNGPLFQKLMeNAGKMEEYV---EENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEER 894
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 885 ESGYVGMKPFLDYIGVSRGWCLLWSSVLGQVGFVVFQAASTYWLAFAI--GIPKITNTML-IGVYSIIS------TLSAG 955
Cdd:PLN03130 895 ETGVVSWKVLERYKNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTdqGTPKTHGPLFyNLIYALLSfgqvlvTLLNS 974
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 956 FVYaraITTAhlgLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDV-PFAFIFVVAPAVELTAALLI 1034
Cdd:PLN03130 975 YWL---IMSS---LYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVaVFVNMFLGQIFQLLSTFVLI 1048
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1035 ---MTYVTWQVIIIALLALaatkVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDA 1111
Cdd:PLN03130 1049 givSTISLWAIMPLLVLFY----GAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDN 1124
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1112 DAVLFFLSNAAMEWVILRIETLQNVTLFTCALLLILI------PKGYiAPgLVGLSLSYALTLTQTQVFLTRWYCTLSNS 1185
Cdd:PLN03130 1125 NIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQngraenQAAF-AS-TMGLLLSYALNITSLLTAVLRLASLAENS 1202
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1186 IISVERIKQYMNIPEEPPAIIDDKRPPSSWPSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLI 1265
Cdd:PLN03130 1203 LNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSML 1282
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1266 SALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPN 1345
Cdd:PLN03130 1283 NALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSL 1362
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1346 KLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMV 1425
Cdd:PLN03130 1363 GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRI 1442
|
1450 1460
....*....|....*....|....*....
gi 1063712898 1426 MVLSFGDLVEYNEPSKLMETD-SYFSKLV 1453
Cdd:PLN03130 1443 LVLDAGRVVEFDTPENLLSNEgSAFSKMV 1471
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
38-1453 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 775.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 38 LLFLCIFYLFLIASCVS-THFIVRGRKKGWIFVAVAICCAITSF--IFLGVGLNSLiHGGNDVTEISWVACFVEGIIWVS 114
Cdd:PLN03232 46 LLGLCFYRIWIILDNAKaQIYVLRKKYYNCVLGILACYCVVEPVlrLVMGISLFDM-DEETDLPPFEVASLMVEAFAWFS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 115 LAVSLLVNGSKWVNILVsvWWVSFALLDLVAKSGILLQgngiRILDILTLPMSLLLLLCswMNLRSSSA----------- 183
Cdd:PLN03232 125 MLVLIGLETKQYVKEFR--WYVRFGVVYVLVADAVLLD----LVLPLKNSINRTALYLC--ISSRCCQAlfgilllvyip 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 184 AAQDCSVTGLSDPLLTKNPRKESARLAT-------AGFFSILSFSWMNPLLSLGFKKPLSPEDIPSVVPEDEAQLAYKKF 256
Cdd:PLN03232 197 ELDPYPGYHILNNESLDNVEYDALRGGEnicperyASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 257 SQAWDtllgdESSTKERNLVFRAVVKVYFKENIFIAVFAFLRTFAVVSLPLMLYVFVdyansdhRDLRNG-----FFNLA 331
Cdd:PLN03232 277 QRCWT-----EESRRPKPWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLL-------QSMQEGdpawvGYVYA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 332 CLVMLKLVESLTMRHWYFAS-RRSGMRIRSALMVAAYKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSL 410
Cdd:PLN03232 345 FLIFFGVTFGVLCESQYFQNvGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 411 SLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKK 490
Cdd:PLN03232 425 PFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESR 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 491 IESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVFlGCALLKSAPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQ 570
Cdd:PLN03232 505 IQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSF-GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVN 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 571 GNVSFQRLNNFLLDDELKMdeIERSGLDASGTAVDIQVGNFGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLH 650
Cdd:PLN03232 584 ANVSLQRIEELLLSEERIL--AQNPPLQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLIS 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 651 AVLGEIPKVSGT-VKVFGSIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINL 729
Cdd:PLN03232 662 AMLGELSHAETSsVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNI 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 730 SGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSG 809
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEG 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 810 KYEELLMMGTAFQQL------------VNAHNDAV-----TVLPLASNESLGDLRKEGKDREIrnmtvvekieeeiektd 872
Cdd:PLN03232 822 TFAELSKSGSLFKKLmenagkmdatqeVNTNDENIlklgpTVTIDVSERNLGSTKQGKRGRSV----------------- 884
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 873 ipgvqLTQEEEKESGYVGMKPFLDYIGVSRGwclLWSSVLGQVGFV---VFQAASTYWLAFAIGIPKITN---TMLIGVY 946
Cdd:PLN03232 885 -----LVKQEERETGIISWNVLMRYNKAVGG---LWVVMILLVCYLtteVLRVSSSTWLSIWTDQSTPKSyspGFYIVVY 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 947 SIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVP----------- 1015
Cdd:PLN03232 957 ALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVAnlmnmfmnqlw 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1016 -----FAFIFVVApAVELTA--ALLIMTYVTWQviiiallalaatkvvqdYYLASARELIRINGTTKAPVMNYAAETSLG 1088
Cdd:PLN03232 1037 qllstFALIGTVS-TISLWAimPLLILFYAAYL-----------------YYQSTSREVRRLDSVTRSPIYAQFGEALNG 1098
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1089 VVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQNVTLFTCALLLIL----IPKGYIAPGLVGLSLSY 1164
Cdd:PLN03232 1099 LSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLrngnAENQAGFASTMGLLLSY 1178
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1165 ALTLTQTQVFLTRWYCTLSNSIISVERIKQYMNIPEEPPAIIDDKRPPSSWPSNGTIHLQELKIRYRPNAPLVLKGISCT 1244
Cdd:PLN03232 1179 TLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFF 1258
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1245 FREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDPLGVYSD 1324
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHND 1338
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1325 DEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEF 1404
Cdd:PLN03232 1339 ADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEF 1418
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1405 ADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETD-SYFSKLV 1453
Cdd:PLN03232 1419 KSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDtSAFFRMV 1468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
294-1453 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 587.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 294 FAFLRTFAVVSLPLMLYVFVDYANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYKKQLKL 373
Cdd:PTZ00243 252 FKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCGLQYRSALNALIFEKCFTI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 374 S--SLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKMLQ 451
Cdd:PTZ00243 332 SskSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQM 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 452 NCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVFLGC 531
Cdd:PTZ00243 412 AARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVFTVY 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 532 ALLKSApLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRLNNFLLDDEL------KMDEIERSGLDASGTA-- 603
Cdd:PTZ00243 492 YLLGHE-LTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNAtcstvqDMEEYWREQREHSTACql 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 604 ------VDIQV------------------------------------------------------------GNFGWEPET 617
Cdd:PTZ00243 571 aavlenVDVTAfvpvklprapkvktsllsralrmlcceqcrptkrhpspsvvvedtdygspssasrhivegGTGGGHEAT 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPT---------------------LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTS 676
Cdd:PTZ00243 651 PTSErsaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQA 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 677 WIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPF 756
Cdd:PTZ00243 731 WIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 757 SAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEElLMMGTAFQQL------------ 824
Cdd:PTZ00243 811 SALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLaaelkenkdske 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 825 --VNAHNDAVTVLP-----LASNESLGDLRKEGKDreirnmtvvekieeeIEKTDIPGVQLTQEEEKESGYVGMKPFLDY 897
Cdd:PTZ00243 890 gdADAEVAEVDAAPggavdHEPPVAKQEGNAEGGD---------------GAALDAAAGRLMTREEKASGSVPWSTYVAY 954
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 898 IGVSRGWClLWSSVLgqVGFVV---FQAASTYWLA-FAIGIPKITNTMLIGVYSIISTLSAGFVYARAITTAHLGLKASK 973
Cdd:PTZ00243 955 LRFCGGLH-AAGFVL--ATFAVtelVTVSSGVWLSmWSTRSFKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSR 1031
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 974 AFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAAT 1053
Cdd:PTZ00243 1032 NMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLY 1111
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1054 KVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETL 1133
Cdd:PTZ00243 1112 YRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFL 1191
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1134 QNVTLFTCALLLI---LIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM-NIPEEP------- 1202
Cdd:PTZ00243 1192 SNIVVTVIALIGVigtMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDmpeldee 1271
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1203 ----------------PAIIDDKRPPSSWPSN---GTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKST 1263
Cdd:PTZ00243 1272 vdalerrtgmaadvtgTVVIEPASPTSAAPHPvqaGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKST 1351
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1264 LISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNL 1343
Cdd:PTZ00243 1352 LLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASE 1431
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1344 PNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVL-DEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDS 1422
Cdd:PTZ00243 1432 SEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQY 1511
|
1290 1300 1310
....*....|....*....|....*....|..
gi 1063712898 1423 DMVMVLSFGDLVEYNEPSKL-METDSYFSKLV 1453
Cdd:PTZ00243 1512 DKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
209-1466 |
9.84e-151 |
|
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: 497.51 E-value: 9.84e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 209 LATAGFFSILSFSWMNPLLSLGFKKPLSPEDIPSVVPEDEAQLAYKKFSQAWDTLLgdeSSTKERNLVFRAVVKVYFKEN 288
Cdd:TIGR01271 6 VEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDREL---ASAKKNPKLLNALRRCFFWRF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 289 IFIAVFAFLRTFAVVSLPLMLYVFVDYANSDHRDLRNGFFNLAC-LVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAY 367
Cdd:TIGR01271 83 VFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALgLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 368 KKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFA 447
Cdd:TIGR01271 163 KKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 448 KMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVV 527
Cdd:TIGR01271 243 QKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 528 FLGCALLKSAPLNasTIFTVLATLRVMSEPV-KIIPDAISAIIQGNVSFQRLNNFLLDDELKM-------DEIERSGLDA 599
Cdd:TIGR01271 323 VVPYALIKGIILR--RIFTTISYCIVLRMTVtRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTleynlttTEVEMVNVTA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 600 S-------------------GTA---VDIQVGNFGWEpetKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIP 657
Cdd:TIGR01271 401 SwdegigelfekikqnnkarKQPngdDGLFFSNFSLY---VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 658 KVSGTVKVFGSIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRI 737
Cdd:TIGR01271 478 PSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARI 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 738 QLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEEL--- 814
Cdd:TIGR01271 558 SLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELqak 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 815 ------LMMGT---------------------------------------AFQQ-------------LVNAHN------- 829
Cdd:TIGR01271 638 rpdfssLLLGLeafdnfsaerrnsiltetlrrvsidgdstvfsgpetikqSFKQpppefaekrkqsiILNPIAsarkfsf 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 830 --------------DAV---------------------------------------TVLPLASNESLGDLRKEGKDREIR 856
Cdd:TIGR01271 718 vqmgpqkaqattieDAVrepserkfslvpedeqgeeslprgnqyhhglqhqaqrrqSVLQLMTHSNRGENRREQLQTSFR 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 857 NMTVVEKIEEEIEKTDIPGVQLTQE-------------------EEKESGYV--GMKPFLDYIGVSRG--WCLLWSSVLg 913
Cdd:TIGR01271 798 KKSSITQQNELASELDIYSRRLSKDsvyeiseeineedlkecfaDERENVFEttTWNTYLRYITTNRNlvFVLIFCLVI- 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 914 qvgFVVFQAASTYWLAFAIGIPKITNTM---------LIGVYSIIST------------------LSAGFVyaRAITTAH 966
Cdd:TIGR01271 877 ---FLAEVAASLLGLWLITDNPSAPNYVdqqhanassPDVQKPVIITptsayyifyiyvgtadsvLALGFF--RGLPLVH 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 967 LGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAF-------------IFVVA---PAVELTA 1030
Cdd:TIGR01271 952 TLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLfdfiqltlivlgaIFVVSvlqPYIFIAA 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1031 ALLIMTYVtwqviiiallalaatkVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTA---ERFFKNYLN 1107
Cdd:TIGR01271 1032 IPVAVIFI----------------MLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQsyfETLFHKALN 1095
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1108 LVDADavlFFLSNAAMEWVILRIETLqnVTLFTCALLLILIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSII 1187
Cdd:TIGR01271 1096 LHTAN---WFLYLSTLRWFQMRIDII--FVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMR 1170
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1188 SVERIKQYMNIPEEPPA--------------IIDDKRPPSSWPSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGV 1253
Cdd:TIGR01271 1171 SVSRVFKFIDLPQEEPRpsggggkyqlstvlVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGL 1250
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1254 VGRTGSGKSTLISALFRLVEpASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEK 1333
Cdd:TIGR01271 1251 LGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEE 1329
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1334 CQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVA 1413
Cdd:TIGR01271 1330 VGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSE 1409
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 1414 HRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLV-----AEYWASCRGNSSQ 1466
Cdd:TIGR01271 1410 HRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMsaadrLKLFPLHRRNSSK 1467
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1219-1439 |
2.11e-125 |
|
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: 388.78 E-value: 2.11e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1219 GTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1298
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKI 1378
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 1379 LVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEP 1439
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
604-804 |
9.38e-108 |
|
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: 339.83 E-value: 9.38e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 604 VDIQVGNFGWEPE--TKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQSG 681
Cdd:cd03250 1 ISVEDASFTWDSGeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063712898 762 HTAGVLFHKCVEDSLKE-KTVILVTHQVEFLSEVDQILVMEEGT 804
Cdd:cd03250 161 HVGRHIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1215-1439 |
2.43e-94 |
|
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: 302.79 E-value: 2.43e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1215 WPSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDL 1294
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1295 RMKLSIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALekcqlkttisnlpnkldsSVSDEGENWSVGQRQLFCLGRVLLK 1374
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1375 RNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEP 1439
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
891-1454 |
2.02e-88 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 300.16 E-value: 2.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 891 MKPFLDYIGVSRGWCLLwsSVLGQVGFVVFQAASTYWLAFAI--GIPKITNT---MLIGVYSIISTLSAGFVYARAITTA 965
Cdd:COG1132 9 LRRLLRYLRPYRGLLIL--ALLLLLLSALLELLLPLLLGRIIdaLLAGGDLSallLLLLLLLGLALLRALLSYLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 966 HLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQ---- 1041
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRlali 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1042 ----VIIIALLALAATKVVQDYYLASARELIRINGttkapvmnYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFF 1117
Cdd:COG1132 167 vllvLPLLLLVLRLFGRRLRKLFRRVQEALAELNG--------RLQESLSGIRVVKAFGREERELERFREANEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1118 LSNAAMEWVILRIETLQNV-TLFTCALLLILIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1196
Cdd:COG1132 239 RAARLSALFFPLMELLGNLgLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1197 nipEEPPAIIDDKRPPSSWPSNGTIHLQELKIRYRPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPAS 1276
Cdd:COG1132 319 ---DEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1277 GCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDpLGV--YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDE 1354
Cdd:COG1132 395 GRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR-YGRpdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1355 GENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLV 1434
Cdd:COG1132 474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
570 580
....*....|....*....|
gi 1063712898 1435 EYNEPSKLMETDSYFSKLVA 1454
Cdd:COG1132 554 EQGTHEELLARGGLYARLYR 573
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
915-1455 |
2.06e-83 |
|
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: 289.81 E-value: 2.06e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 915 VGFVVFQAASTYWLAFAIGIpkitntmligvySIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDST 994
Cdd:COG2274 183 IDRVLPNQDLSTLWVLAIGL------------LLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 995 PVGRILTRASSDLNVLD----------YDVPFAFIFVV-----APAVELTAALLIMTYVTWqviiiallalaaTKVVQDY 1059
Cdd:COG2274 251 SVGDLASRFRDVESIREfltgslltalLDLLFVLIFLIvlffySPPLALVVLLLIPLYVLL------------GLLFQPR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1060 YLASARELIRINGTtkapVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVdADAV-----LFFLSNAAMEWVILrIETLQ 1134
Cdd:COG2274 319 LRRLSREESEASAK----RQSLLVETLRGIETIKALGAESRFRRRWENLL-AKYLnarfkLRRLSNLLSTLSGL-LQQLA 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1135 NVTLFTCALLLILipKGYIAPG-------LVGLSLSYALTLTQtqvFLTRWYctlsNSIISVERIKQYMNIPEEPPAIID 1207
Cdd:COG2274 393 TVALLWLGAYLVI--DGQLTLGqliafniLSGRFLAPVAQLIG---LLQRFQ----DAKIALERLDDILDLPPEREEGRS 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1208 DKRPPsswPSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIS 1287
Cdd:COG2274 464 KLSLP---RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1288 KIGLKDLRMKLSIIPQEPTLFRGCIRTNL---DPLgvYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQ 1364
Cdd:COG2274 541 QIDPASLRRQIGVVLQDVFLFSGTIRENItlgDPD--ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQ 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1365 LFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLME 1444
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
570
....*....|.
gi 1063712898 1445 TDSYFSKLVAE 1455
Cdd:COG2274 699 RKGLYAELVQQ 709
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1219-1453 |
1.35e-77 |
|
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: 257.53 E-value: 1.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1219 GTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1298
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKI 1378
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 1379 LVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLM-ETDSYFSKLV 1453
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
290-578 |
3.38e-74 |
|
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: 248.94 E-value: 3.38e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 290 FIAVFAFLRTFAVVSLPLMLYVFVDYANSDHR-DLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYK 368
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDePLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 369 KQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAK 448
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 449 MLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVF 528
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 529 LGCALLKSaPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 578
Cdd:cd18579 241 ATYVLLGN-PLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
903-1196 |
3.15e-69 |
|
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: 234.71 E-value: 3.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 903 GWCLLWSSVLGQVGFVVFQAASTYWLAFAIGIPKITNTMLIGVYSIISTL-SAGFVYARAITTAHLGLKASKAFFSGFTN 981
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLaSVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 982 AVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQDYYL 1061
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1062 ASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQNVTLFTC 1141
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1142 ALLLILIPkGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1196
Cdd:cd18580 241 ALLAVLLR-SSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
277-828 |
8.91e-69 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 243.15 E-value: 8.91e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 277 FRAVVKVYFKENIFIAVFAFLRTFAVVSLPLMLYVFVDYAnSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGM 356
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDAL-LAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 357 RIRSALMVAAYKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWW-FHSGWSLSLQLLLSTAVLF------GVVGAGA 429
Cdd:COG1132 91 RVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLFvidwrlALIVLLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 430 FPGLILLLLCgllnlpFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEF-TWLAKAQLT 508
Cdd:COG1132 171 LPLLLLVLRL------FGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRrANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 509 KAFGSFLYWMSPTIVSSVVFLGCALLKSAPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRLNNfLLDDELK 588
Cdd:COG1132 245 ALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE-LLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 589 MDEIERsGLDASGTAVDIQVGN--FGWEPETkiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVF 666
Cdd:COG1132 324 IPDPPG-AVPLPPVRGEIEFENvsFSYPGDR--PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 667 G-------------SIAYVSQTSWIQSGTIRDNILYGKPMESR-RYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGG 732
Cdd:COG1132 401 GvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPDATDeEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 733 QKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKcVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYE 812
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570
....*....|....*.
gi 1063712898 813 ELLMMGTAFQQLVNAH 828
Cdd:COG1132 560 ELLARGGLYARLYRLQ 575
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1088-1446 |
2.87e-61 |
|
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: 220.78 E-value: 2.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1088 GVVTIRAFGTAERffknYLNLVDADA---------VL--FFLSNAAMEW----------VILRIETLQ-NVTLFTCALLL 1145
Cdd:COG4988 206 GLTTLKLFGRAKA----EAERIAEASedfrkrtmkVLrvAFLSSAVLEFfaslsialvaVYIGFRLLGgSLTLFAALFVL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1146 ILIPKGYiAPgLVGLSLSYALTLtqtqvfltrwyctlsNSIISVERIkqyMNIPEEPPAIIDDKRPPSSWPSNGTIHLQE 1225
Cdd:COG4988 282 LLAPEFF-LP-LRDLGSFYHARA---------------NGIAAAEKI---FALLDAPEPAAPAGTAPLPAAGPPSIELED 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1226 LKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEP 1305
Cdd:COG4988 342 VSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNP 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1306 TLFRGCIRTNLDpLG--VYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDE 1383
Cdd:COG4988 421 YLFAGTIRENLR-LGrpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDE 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1384 ATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETD 1446
Cdd:COG4988 500 PTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1219-1444 |
4.73e-60 |
|
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: 205.92 E-value: 4.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1219 GTIHLQELKIRYRPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1298
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEK-CQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNK 1377
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKeAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1378 ILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLME 1444
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
620-814 |
2.65e-57 |
|
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: 200.08 E-value: 2.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQSGTIRDNILYGKPMESRRYN 699
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 700 AAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEK 779
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANK 210
|
170 180 190
....*....|....*....|....*....|....*
gi 1063712898 780 TVILVTHQVEFLSEVDQILVMEEGTITQSGKYEEL 814
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
604-804 |
2.00e-55 |
|
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: 192.16 E-value: 2.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 604 VDIQVGNFGWEPEtkIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTV-----------------KVF 666
Cdd:cd03290 1 VQVTNGYFSWGSG--LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 667 GSIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYAD 746
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 747 ADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKE--KTVILVTHQVEFLSEVDQILVMEEGT 804
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1221-1428 |
3.06e-55 |
|
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: 189.90 E-value: 3.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1300
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLFRGCIRTNLdplgvysddeiwkalekcqlkttisnlpnkldssvsdegenWSVGQRQLFCLGRVLLKRNKILV 1380
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063712898 1381 LDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVL 1428
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVL 167
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
997-1454 |
2.56e-54 |
|
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: 200.38 E-value: 2.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 997 GRILTRASSDLNVLDYdvpfAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQ-------DYYLA--SAREL 1067
Cdd:COG4987 112 GDLLNRLVADVDALDN----LYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAglllpllAARLGrrAGRRL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1068 IRINGTTKApvmnYAAETSLGVVTIRAFGTAERFF-------KNYLNLVDADAVLFFLSNAAMEWVilrietlqnVTLFT 1140
Cdd:COG4987 188 AAARAALRA----RLTDLLQGAAELAAYGALDRALarldaaeARLAAAQRRLARLSALAQALLQLA---------AGLAV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1141 CALLLILIP---KGYIAP------GLVGLSLSYALT-LTQTQVFLTRwyctlsnSIISVERIKQymnIPEEPPAIIDDKR 1210
Cdd:COG4987 255 VAVLWLAAPlvaAGALSGpllallVLAALALFEALApLPAAAQHLGR-------VRAAARRLNE---LLDAPPAVTEPAE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1211 PPSSwPSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG 1290
Cdd:COG4987 325 PAPA-PGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1291 LKDLRMKLSIIPQEPTLFRGCIRTNL---DPLGvySDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFC 1367
Cdd:COG4987 404 EDDLRRRIAVVPQRPHLFDTTLRENLrlaRPDA--TDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLA 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1368 LGRVLLKRNKILVLDEATASIDSAT-DAIIQRiIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETD 1446
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATeQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
....*...
gi 1063712898 1447 SYFSKLVA 1454
Cdd:COG4987 561 GRYRQLYQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1230-1452 |
3.20e-54 |
|
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: 189.36 E-value: 3.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1230 YRPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFR 1309
Cdd:cd03253 10 YDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1310 GCIRTNLDplgvY-----SDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEA 1384
Cdd:cd03253 89 DTIGYNIR----YgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 1385 TASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKL 1452
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
907-1452 |
2.57e-53 |
|
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: 197.63 E-value: 2.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 907 LWSSVLGQVGFVVFQAASTYWLAFaigIPKITNTMLIGVY-SIISTLSAGFV-------YARAITTAHLGlKASKAFFSG 978
Cdd:TIGR02203 13 KAGLVLAGVAMILVAATESTLAAL---LKPLLDDGFGGRDrSVLWWVPLVVIglavlrgICSFVSTYLLS-WVSNKVVRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 979 FTNAVF----KAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATK 1054
Cdd:TIGR02203 89 IRVRMFekllGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1055 VVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFG----TAERF-FKNYLNLVDA----------DAVLFFLS 1119
Cdd:TIGR02203 169 ILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGgqayETRRFdAVSNRNRRLAmkmtsagsisSPITQLIA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1120 NAAMEWVIlrietlqnvtlftcALLLILIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYMNIP 1199
Cdd:TIGR02203 249 SLALAVVL--------------FIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1200 EEPPaiiDDKRPPSSwpSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI 1279
Cdd:TIGR02203 315 PEKD---TGTRAIER--ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1280 LIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNL--DPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGEN 1357
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIayGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1358 WSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYN 1437
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
|
570
....*....|....*
gi 1063712898 1438 EPSKLMETDSYFSKL 1452
Cdd:TIGR02203 550 THNELLARNGLYAQL 564
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1219-1454 |
1.12e-52 |
|
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: 186.60 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1219 GTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEpASGCILIDGIDISKIGLKDLRMKL 1298
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKI 1378
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 1379 LVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLVA 1454
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAIS 235
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
904-1196 |
1.38e-52 |
|
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: 186.90 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 904 WCLLWSSVLGQVGFVVFQaasTYWLAF-------AIGIPKITNTML--IGVYSIISTLSAGFVYARAITTAHLGLKASKA 974
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQ---SWWLGIwasayetSSALPPSEVSVLyyLGIYALISLLSVLLGTLRYLLFFFGSLRASRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 975 FFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATK 1054
Cdd:cd18604 78 LHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1055 VVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQ 1134
Cdd:cd18604 158 YIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLG 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 1135 NVTLFTCALLLILIPKgyIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1196
Cdd:cd18604 238 ALFSFATAALLVYGPG--IDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
907-1196 |
3.61e-52 |
|
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: 185.76 E-value: 3.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 907 LWSSVLGQVGFVVFQAASTYWLAF-------AIGIPKITNTMLIGVYSIISTLSAGFVYARAITTAHLGLKASKAFFSGF 979
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEwsddpalNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 980 TNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQDY 1059
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1060 YLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQNVTLF 1139
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1140 TCALLLIlIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1196
Cdd:cd18603 241 FAALFAV-LSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1221-1453 |
5.79e-52 |
|
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: 183.12 E-value: 5.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRY--RPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1298
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPTLFRGCIRTNLDpLGVYS--DDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRN 1376
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIR-YGKPDatDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1377 KILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLV 1453
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
563-815 |
1.63e-51 |
|
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: 191.90 E-value: 1.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 563 DAISAiiqgnvsFQRLNNFLLDDELKMDEIERSGLDASGTAVDIQVGNFGWEPETkiPTLRNIHLEIKHGQKVAVCGPVG 642
Cdd:COG4988 303 NGIAA-------AEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 643 AGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDNILYGKPMESR-RYNAAIKACALD 708
Cdd:COG4988 374 AGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRPDASDeELEAALEAAGLD 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 709 KDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKcVEDSLKEKTVILVTHQV 788
Cdd:COG4988 454 EFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRL 532
|
250 260
....*....|....*....|....*..
gi 1063712898 789 EFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:COG4988 533 ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
536-824 |
3.39e-51 |
|
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: 191.13 E-value: 3.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 536 SAPLNASTIFTVLAtlrvMSEPVKIIPDAISAIIQGNVSFQRLNNfLLDDELKMDEIERSGLDASGTAVDIQVGNFGWeP 615
Cdd:COG4987 271 SGPLLALLVLAALA----LFEALAPLPAAAQHLGRVRAAARRLNE-LLDAPPAVTEPAEPAPAPGGPSLELEDVSFRY-P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 616 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGT 682
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTT 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 683 IRDNILYGKPMES-RRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:COG4987 425 LRENLRLARPDATdEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDA 504
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 762 HTAGVLFHKcVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQL 824
Cdd:COG4987 505 ATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1221-1452 |
3.41e-51 |
|
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: 180.50 E-value: 3.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1300
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLFRGCIRTNLdplgVY-----SDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKR 1375
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1376 NKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKL 1452
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
292-578 |
6.93e-51 |
|
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: 181.90 E-value: 6.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 292 AVFAFLRTFAVVSLPLMLYVFVDYANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYKKQL 371
Cdd:cd18595 3 ALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 372 KLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKMLQ 451
Cdd:cd18595 83 RLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 452 NCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVFLGC 531
Cdd:cd18595 163 KLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1063712898 532 ALLKSAP-LNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 578
Cdd:cd18595 243 VLSDPDNvLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
277-826 |
2.25e-50 |
|
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: 191.59 E-value: 2.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 277 FRAVVKVYFKENIFIAVFAFLRTFAVVSLPLMLYVFVDYAnsdhrdLRNGFFNL-----ACLVMLKLVESL--TMRHWYF 349
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRV------LPNQDLSTlwvlaIGLLLALLFEGLlrLLRSYLL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 350 --ASRRSGMRIRSALMvaayKKQLKLSSLGRKRHSSGEIVNYIAvDAYRMGEFLwwfhSGWSLSLQLLLSTAVLFGVV-- 425
Cdd:COG2274 221 lrLGQRIDLRLSSRFF----RHLLRLPLSFFESRSVGDLASRFR-DVESIREFL----TGSLLTALLDLLFVLIFLIVlf 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 426 ---------GAGAFPGLILLLLCgllnlpFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIEScrd 496
Cdd:COG2274 292 fyspplalvVLLLIPLYVLLGLL------FQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWEN--- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 497 deftwLAKAQLTKAFGSFLYWMSPTIVSS---------VVFLGCALLKSAPLN-----ASTIFTVLATLRVMSepvkiIP 562
Cdd:COG2274 363 -----LLAKYLNARFKLRRLSNLLSTLSGllqqlatvaLLWLGAYLVIDGQLTlgqliAFNILSGRFLAPVAQ-----LI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 563 DAISAIIQGNVSFQRLNNFL-LDDElkmDEIERSGLDASGTAVDIQVGN--FGWEPETKiPTLRNIHLEIKHGQKVAVCG 639
Cdd:COG2274 433 GLLQRFQDAKIALERLDDILdLPPE---REEGRSKLSLPRLKGDIELENvsFRYPGDSP-PVLDNISLTIKPGERVAIVG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 640 PVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDNILYGKPMESR-RYNAAIKAC 705
Cdd:COG2274 509 RSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPDATDeEIIEAARLA 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 706 ALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAgvlfhKCVEDSLKE----KTV 781
Cdd:COG2274 589 GLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE-----AIILENLRRllkgRTV 663
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1063712898 782 ILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQLVN 826
Cdd:COG2274 664 IIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
981-1435 |
3.77e-50 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 188.39 E-value: 3.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 981 NAVFKAPMLFFDSTPVGRILTRASSDLNVLDyDVpfaFIFVVAP---AVELTAALLI-MTYVTWQVIIIALLALAATKVV 1056
Cdd:PRK10790 106 DAALRQPLSAFDTQPVGQLISRVTNDTEVIR-DL---YVTVVATvlrSAALIGAMLVaMFSLDWRMALVAIMIFPAVLVV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1057 QDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNylnlvdadavlffLSNAAMEWVILRIETLQ-- 1134
Cdd:PRK10790 182 MVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGER-------------MGEASRSHYMARMQTLRld 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1135 ------NVTLFT----CALLLILipkGYIAPGLVGLSLSYALT-----LTQTQVFLTRWYCTLSNSIISVERIKQYMNIP 1199
Cdd:PRK10790 249 gfllrpLLSLFSalilCGLLMLF---GFSASGTIEVGVLYAFIsylgrLNEPLIELTTQQSMLQQAVVAGERVFELMDGP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1200 EEPPAiiDDKRPPSSwpsnGTIHLQELKIRYRPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI 1279
Cdd:PRK10790 326 RQQYG--NDDRPLQS----GRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1280 LIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLdPLGV-YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENW 1358
Cdd:PRK10790 399 RLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANV-TLGRdISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNL 477
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1359 SVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVE 1435
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
904-1196 |
9.67e-50 |
|
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: 178.88 E-value: 9.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 904 WCLLWSSVLGQVGfvvfQAASTYWLAFAI--------GIPKITNTMLIGVYSIISTLSAGFVYARAITTAHLGLKASKAF 975
Cdd:cd18605 2 ILILLSLILMQAS----RNLIDFWLSYWVshsnnsffNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 976 FSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKV 1055
Cdd:cd18605 78 HNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1056 VQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQN 1135
Cdd:cd18605 158 IQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1136 VTLFTCAL--LLILIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1196
Cdd:cd18605 238 LIVTFVALtaVVQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
873-1453 |
3.64e-48 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 184.93 E-value: 3.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 873 IPGVQLTQEEEKESGY-VGMKPFLDYIGVSRGW-----CLLWSSVLGQVGFVVFQAASTYWLAFAIGIPKITNTM-LIGV 945
Cdd:TIGR00958 130 SAGASEKEAEQGQSETaDLLFRLLGLSGRDWPWlisafVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIfFMCL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 946 YSIISTLSAGFvyaRA----ITTAHLGLKASKAFFSgftnAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFV 1021
Cdd:TIGR00958 210 LSIASSVSAGL---RGgsfnYTMARINLRIREDLFR----SLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1022 VAPAVELTAALLIMTYVTWQVIIIALLAL----AATKVVQDYYLASARELIriNGTTKApvmNYAAETSLGVV-TIRAFG 1096
Cdd:TIGR00958 283 LRNLVMLLGLLGFMLWLSPRLTMVTLINLplvfLAEKVFGKRYQLLSEELQ--EAVAKA---NQVAEEALSGMrTVRSFA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1097 TAERFFKNY---------LNLVDADAVLFFLsnaameWVILRIETLQNVTLFTCALLLILipKGYIAPGLVGLSLSYALT 1167
Cdd:TIGR00958 358 AEEGEASRFkealeetlqLNKRKALAYAGYL------WTTSVLGMLIQVLVLYYGGQLVL--TGKVSSGNLVSFLLYQEQ 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1168 LTQTQVFLTRWYCTLSNSIISVERIKQYMNipeeppaiiddkRPPSSWPS--------NGTIHLQELKIRY--RPNAPlV 1237
Cdd:TIGR00958 430 LGEAVRVLSYVYSGMMQAVGASEKVFEYLD------------RKPNIPLTgtlaplnlEGLIEFQDVSFSYpnRPDVP-V 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLD 1317
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1318 -PLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATasidSATDAII 1396
Cdd:TIGR00958 577 yGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT----SALDAEC 652
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1397 QRIIRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLV 1453
Cdd:TIGR00958 653 EQLLQEsrSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
911-1196 |
1.49e-46 |
|
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: 169.19 E-value: 1.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 911 VLGQVGFVVFQAASTYWLAFAIG-IPKITNTMLIGVYSIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPML 989
Cdd:cd18606 5 LLLLILSQFAQVFTNLWLSFWTEdFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 990 FFDSTPVGRILTRASSDLNVLDYDVP----------------FAFIFVVAPAVELTAALLIMTYVtwqviiiallalaat 1053
Cdd:cd18606 85 FFDTTPLGRILNRFSKDTDVLDNELPdslrmflytlssiigtFILIIIYLPWFAIALPPLLVLYY--------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1054 kVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETL 1133
Cdd:cd18606 150 -FIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1134 QNVTLFTCALLLIlIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1196
Cdd:cd18606 229 GSLLVLIVALLCV-TRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1200-1435 |
9.21e-46 |
|
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: 175.78 E-value: 9.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1200 EEPPAIIDDKRPPSSWPSNGTIHLQELKIRYRPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI 1279
Cdd:COG5265 337 DQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1280 LIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLdplgVY-----SDDEIWKALEKCQLKTTISNLPNKLDSSVSDE 1354
Cdd:COG5265 416 LIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGER 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1355 GENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLV 1434
Cdd:COG5265 492 GLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIV 571
|
.
gi 1063712898 1435 E 1435
Cdd:COG5265 572 E 572
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
610-803 |
3.97e-44 |
|
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: 157.93 E-value: 3.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 610 NFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTS 676
Cdd:cd03228 7 SFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 677 WIQSGTIRDNILygkpmesrrynaaikacaldkdmngfghgdlteigqrginlSGGQKQRIQLARAVYADADVYLLDDPF 756
Cdd:cd03228 86 FLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063712898 757 SAVDAHTAgVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEG 803
Cdd:cd03228 125 SALDPETE-ALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1221-1454 |
7.33e-44 |
|
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: 159.57 E-value: 7.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1300
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLFRGCIRTNL---DPlgVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNK 1377
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1378 ILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLVA 1454
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
290-578 |
9.98e-44 |
|
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: 161.89 E-value: 9.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 290 FIAVFAFLRTFAVVSLPLMLYVFVDY-ANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYK 368
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYlEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 369 KQLKL-------------------SSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGA 429
Cdd:cd18596 81 KALRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 430 FPGLILLLLCGLLNLPFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTK 509
Cdd:cd18596 161 LVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLD 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 510 AFGSFLYWMSPTIVSSVVFLGCALLKSAPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 578
Cdd:cd18596 241 LLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
615-809 |
2.07e-43 |
|
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: 157.75 E-value: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 615 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSG 681
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNILYGKPM-ESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 760
Cdd:cd03245 93 TLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063712898 761 AHTAGVLFHKcVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSG 809
Cdd:cd03245 173 MNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1219-1434 |
6.60e-43 |
|
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: 156.21 E-value: 6.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1219 GTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1298
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPTLFRGCIRTNLDPLGVYSDDE-IWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNK 1377
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDErILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 1378 ILVLDEATASIDSATDA-IIQRiIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLV 1434
Cdd:cd03245 161 ILLLDEPTSAMDMNSEErLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
610-815 |
2.08e-41 |
|
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: 152.38 E-value: 2.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 610 NFGWEPetKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTS 676
Cdd:cd03254 9 NFSYDE--KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 677 WIQSGTIRDNILYGKPMESR-RYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:cd03254 87 FLFSGTIMENIRLGRPNATDeEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 756 FSAVDAHTAgVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:cd03254 167 TSNIDTETE-KLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1088-1454 |
5.23e-41 |
|
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: 162.43 E-value: 5.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1088 GVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQnvtLFTCALLLILIPKGYIAPGL-VGLSLSYAL 1166
Cdd:TIGR03797 323 GISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLP---VLTSAALFAAAISLLGGAGLsLGSFLAFNT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1167 TLTQTQVFLTRwyctLSNSIISV-------ERIKQymnIPEEPPAIIDDKRPPSswPSNGTIHLQELKIRYRPNAPLVLK 1239
Cdd:TIGR03797 400 AFGSFSGAVTQ----LSNTLISIlaviplwERAKP---ILEALPEVDEAKTDPG--KLSGAIEVDRVTFRYRPDGPLILD 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1240 GISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDPL 1319
Cdd:TIGR03797 471 DVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGG 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1320 GVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATasidSATDAIIQRI 1399
Cdd:TIGR03797 551 APLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEAT----SALDNRTQAI 626
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1400 IREEFA--DCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLVA 1454
Cdd:TIGR03797 627 VSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
604-824 |
1.01e-40 |
|
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: 150.46 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 604 VDIQVGNFGWePETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAvlgeIPKV----SGTVKVFG------------ 667
Cdd:cd03251 1 VEFKNVTFRY-PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNL----IPRFydvdSGRILIDGhdvrdytlaslr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 668 -SIAYVSQTSWIQSGTIRDNILYGKPMESRR--YNAAIKACALDKDMNgFGHGDLTEIGQRGINLSGGQKQRIQLARAVY 744
Cdd:cd03251 76 rQIGLVSQDVFLFNDTVAENIAYGRPGATREevEEAARAANAHEFIME-LPEGYDTVIGERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 745 ADADVYLLDDPFSAVDAHTagvlfHKCVEDSL----KEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTA 820
Cdd:cd03251 155 KDPPILILDEATSALDTES-----ERLVQAALerlmKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGV 229
|
....
gi 1063712898 821 FQQL 824
Cdd:cd03251 230 YAKL 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
624-832 |
1.37e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 159.63 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 624 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPkVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDNILYG 690
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 691 KP-MESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAgvlfh 769
Cdd:PRK11174 447 NPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE----- 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 770 KCVEDSLKE----KTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQLVNAHNDAV 832
Cdd:PRK11174 522 QLVMQALNAasrrQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEEI 588
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
611-824 |
5.09e-40 |
|
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: 148.53 E-value: 5.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 611 FGWEPETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSW 677
Cdd:cd03253 8 FAYDPGRPV--LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 678 IQSGTIRDNILYGKP--MESRRYNAAIKACALDKDMNgFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:cd03253 86 LFNDTIGYNIRYGRPdaTDEEVIEAAKAAQIHDKIMR-FPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 756 FSAVDAHTAGVLFhKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQL 824
Cdd:cd03253 165 TSALDTHTEREIQ-AALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
911-1196 |
2.93e-39 |
|
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: 148.91 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 911 VLGQVGFVVFQAASTYWLA-------------FAIGIPKITN---TMLIGVYSIISTLSAGFVYARAITTAHLGLKASKA 974
Cdd:cd18602 5 LALALLKQGLRVATDFWLAdwteanhdvasvvFNITSSSLEDdevSYYISVYAGLSLGAVILSLVTNLAGELAGLRAARR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 975 FFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATK 1054
Cdd:cd18602 85 LHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1055 VVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQ 1134
Cdd:cd18602 165 FLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLG 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1135 NVTLFTCALLLILIPK-GYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1196
Cdd:cd18602 245 AVIVFLAALSSLTAALaGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1200-1428 |
6.06e-39 |
|
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: 153.60 E-value: 6.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1200 EEPPAIIDDKRPpSSWPSNGTIHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI 1279
Cdd:TIGR02857 302 DAAPRPLAGKAP-VTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1280 LIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNL---DPLGvySDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGE 1356
Cdd:TIGR02857 380 AVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--SDAEIREALERAGLDEFVAALPQGLDTPIGEGGA 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 1357 NWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVL 1428
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
290-578 |
1.63e-38 |
|
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: 146.06 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 290 FIAVFAFLRTFAVVSLPLMLYVFVD-----YANSDHRDLRNGF-FNLACLVMLkLVESLTMRHWYFASRRSGMRIRSALM 363
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINfvedaYLGGPPPSIGYGIgYAIGLFLLQ-LLSSLLLNHFFYRSMLTGAQVRAALT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 364 VAAYKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLN 443
Cdd:cd18597 80 KAIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 444 LPFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTK----AFGSFLywms 519
Cdd:cd18597 160 GFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRsiltAVAFSL---- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 520 PTIVSSVVFLGCALLKSaPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 578
Cdd:cd18597 236 PVLASMLSFITYYATGH-TLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
620-800 |
5.06e-38 |
|
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: 150.90 E-value: 5.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDN 686
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILYGKP----MESRRynaAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 762
Cdd:TIGR02857 416 IRLARPdasdAEIRE---ALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063712898 763 TAgVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVM 800
Cdd:TIGR02857 493 TE-AEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
903-1196 |
7.58e-38 |
|
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: 145.01 E-value: 7.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 903 GWCLLWSSVLGQVGFVVFQAASTYWLAF----------------AIGIPKITNTMLIGVYSIISTLSAGFVY----ARAI 962
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYwlkqgsgnttnnvdnsTVDSGNISDNPDLNFYQLVYGGSILVILllslIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 963 TTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQV 1042
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1043 IIIALLALAATKVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAA 1122
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 1123 MEWVILRIETLQNVTLFTCALLLILIpKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1196
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLL-KGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1200-1453 |
1.10e-37 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 150.88 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1200 EEPPAIIDDKRppsswpSNGTIHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI 1279
Cdd:PRK13657 320 RDPPGAIDLGR------VKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1280 LIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDpLGV--YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGEN 1357
Cdd:PRK13657 393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR-VGRpdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQ 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1358 WSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYN 1437
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
250
....*....|....*.
gi 1063712898 1438 EPSKLMETDSYFSKLV 1453
Cdd:PRK13657 552 SFDELVARGGRFAALL 567
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
620-815 |
1.11e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--------SIAYVSQTSWIQSG---TIRDNI- 687
Cdd:COG1121 20 PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQRAEVDWDfpiTVRDVVl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 --LYGKPMESRRYNAAIKAC---ALDK-DMNGFGHgdlTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:COG1121 100 mgRYGRRGLFRRPSRADREAvdeALERvGLEDLAD---RPIGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 762 HTAGVLFhkcveDSLKE-----KTVILVTHQVEFLSE-VDQILVMEEGTITqSGKYEELL 815
Cdd:COG1121 173 ATEEALY-----ELLRElrregKTILVVTHDLGAVREyFDRVLLLNRGLVA-HGPPEEVL 226
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
290-579 |
4.52e-36 |
|
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: 138.92 E-value: 4.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 290 FIAVFAFLRTFAVVSLPLMLYVFVDYANSDHR-DLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYK 368
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVAYFVPDSTvTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 369 KQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAK 448
Cdd:cd18594 81 KTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 449 MLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVF 528
Cdd:cd18594 161 LFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 529 LGCALLKSApLNASTIFTVLATLRVMSEPVKI-IPDAISAIIQGNVSFQRLN 579
Cdd:cd18594 241 VPYVLTGNT-LTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRIQ 291
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
570-815 |
9.27e-36 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 144.86 E-value: 9.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 570 QGNVSFQRLNNfLLDDELKMDEIERSGLDASGT-AVDIQVGNFgwePETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSL 648
Cdd:PRK10789 282 RGSAAYSRIRA-MLAEAPVVKDGSEPVPEGRGElDVNIRQFTY---PQTDHPALENVNFTLKPGQMLGICGPTGSGKSTL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 649 LHAVLGEIPKVSGTVKVF-------------GSIAYVSQTSWIQSGTIRDNILYGKPMESRRY--NAAIKACALDkDMNG 713
Cdd:PRK10789 358 LSLIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSDTVANNIALGRPDATQQEieHVARLASVHD-DILR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 714 FGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSlKEKTVILVTHQVEFLSE 793
Cdd:PRK10789 437 LPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSALTE 515
|
250 260
....*....|....*....|..
gi 1063712898 794 VDQILVMEEGTITQSGKYEELL 815
Cdd:PRK10789 516 ASEILVMQHGHIAQRGNHDQLA 537
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
615-827 |
9.98e-36 |
|
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: 136.13 E-value: 9.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 615 PETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQTSWIQSG 681
Cdd:cd03249 14 PDVPI--LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNILYGKP---MESRRynAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSA 758
Cdd:cd03249 92 TIAENIRYGKPdatDEEVE--EAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 759 VDAHTAGVLfHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQLVNA 827
Cdd:cd03249 170 LDAESEKLV-QEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1219-1433 |
2.10e-35 |
|
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: 134.91 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1219 GTIHLQELKIRYrPNAP--LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM 1296
Cdd:cd03248 10 GIVKFQNVTFAY-PTRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1297 KLSIIPQEPTLFRGCIRTNLD-PLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKR 1375
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 1376 NKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDL 1433
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
615-815 |
3.23e-35 |
|
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: 142.87 E-value: 3.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 615 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKV------------FG-SIAYVSQTSWIQSG 681
Cdd:TIGR01842 327 PGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLdgadlkqwdretFGkHIGYLPQDVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNIL-YGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 760
Cdd:TIGR01842 407 TVAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 761 AHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:TIGR01842 487 EEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1088-1415 |
5.80e-35 |
|
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: 141.73 E-value: 5.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1088 GVVTIRAFGTAERFFKNYlnlVDADAVLFFLSNAAMEWVILRietlQNVTLFTCAL---LLILIPKGYIAPGLVGLSLSY 1164
Cdd:TIGR02868 202 GAAELVASGALPAALAQV---EEADRELTRAERRAAAATALG----AALTLLAAGLavlGALWAGGPAVADGRLAPVTLA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1165 ALTLTQTQVF-----LTRWYCTLSNSIISVERIKQYMNiPEEPPAIIDDKRPPSSWPSNGTIHLQELKIRYrPNAPLVLK 1239
Cdd:TIGR02868 275 VLVLLPLAAFeafaaLPAAAQQLTRVRAAAERIVEVLD-AAGPVAEGSAPAAGAVGLGKPTLELRDLSAGY-PGAPPVLD 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1240 GISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDpL 1319
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLR-L 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1320 GV--YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQ 1397
Cdd:TIGR02868 432 ARpdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL 511
|
330
....*....|....*...
gi 1063712898 1398 RIIREEFADCTVITVAHR 1415
Cdd:TIGR02868 512 EDLLAALSGRTVVLITHH 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1190-1455 |
1.33e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 141.52 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1190 ERIKQYMNIPEEPPAiidDKRPPSSWPSNGTIHLQELKIrYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALF 1269
Cdd:PRK11174 322 ESLVTFLETPLAHPQ---QGEKELASNDPVTIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1270 RLVePASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNL---DPLgvYSDDEIWKALEKCQLKTTISNLPNK 1346
Cdd:PRK11174 398 GFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPD--ASDEQLQQALENAWVSEFLPLLPQG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1347 LDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVM 1426
Cdd:PRK11174 475 LDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIW 554
|
250 260
....*....|....*....|....*....
gi 1063712898 1427 VLSFGDLVEYNEPSKLMETDSYFSKLVAE 1455
Cdd:PRK11174 555 VMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
620-809 |
2.21e-34 |
|
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: 131.50 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--------SIAYVSQTSWIQSG---TIRDNI- 687
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRSIDRDfpiSVRDVVl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 --LYGKPMESRRYNAAIKAC---ALDKdmngfghGDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:cd03235 93 mgLYGHKGLFRRLSKADKAKvdeALER-------VGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063712898 762 HTAGVLFHKCVEDSLKEKTVILVTHQVEFLSE-VDQILVMeEGTITQSG 809
Cdd:cd03235 166 KTQEDIYELLRELRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1228-1414 |
2.27e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.48 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1228 IRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTL 1307
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1308 FRGCIRTNLD-PLG----VYSDDEIWKALEKCQLKTTIsnlpnkLDSSVsdegENWSVGQRQLFCLGRVLLKRNKILVLD 1382
Cdd:COG4619 86 WGGTVRDNLPfPFQlrerKFDRERALELLERLGLPPDI------LDKPV----ERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190
....*....|....*....|....*....|....
gi 1063712898 1383 EATASIDSATDAIIQRIIREEFADC--TVITVAH 1414
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEgrAVLWVSH 189
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
934-1195 |
4.38e-34 |
|
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: 133.99 E-value: 4.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 934 IPKITNTMLIGVYSIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYD 1013
Cdd:cd18601 53 IEDLDRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1014 VPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIR 1093
Cdd:cd18601 133 LPLTFLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1094 AFGTAERF---FKNYLNLvDADAVLFFLsnAAMEWVILRIETLqnVTLFTCALLLI-LIPKGYIAPGLVGLSLSYALTLT 1169
Cdd:cd18601 213 AYSAQERFqeeFDAHQDL-HSEAWFLFL--ATSRWLAVRLDAL--CALFVTVVAFGsLFLAESLDAGLVGLSLSYALTLM 287
|
250 260
....*....|....*....|....*.
gi 1063712898 1170 QTQVFLTRWYCTLSNSIISVERIKQY 1195
Cdd:cd18601 288 GTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
610-825 |
5.24e-34 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 139.45 E-value: 5.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 610 NFGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTS 676
Cdd:TIGR02204 344 NFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlrqldpaelraRMALVPQDP 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 677 WIQSGTIRDNILYGKPMESRR--YNAAIKACAlDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDD 754
Cdd:TIGR02204 424 VLFAASVMENIRYGRPDATDEevEAAARAAHA-HEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDE 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 755 PFSAVDAHTAgVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQLV 825
Cdd:TIGR02204 503 ATSALDAESE-QLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLA 572
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
293-578 |
1.37e-33 |
|
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: 131.91 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 293 VFAFLRTFAVV---SLPLMLYVFVDYANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYKK 369
Cdd:cd18598 1 PLGLLKLLADVlgfAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 370 QLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKM 449
Cdd:cd18598 81 ALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 450 LQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVFL 529
Cdd:cd18598 161 IGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1063712898 530 GCALLKSaPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 578
Cdd:cd18598 241 TYVLMGN-TLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
306-578 |
2.14e-33 |
|
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: 131.97 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 306 PLMLYVFVDYANSDHRD------------------LRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAY 367
Cdd:cd18591 17 PLCISGIVDYVEENTYSssnstdklsvsyvtveefFSNGYVLAVILFLALLLQATFSQASYHIVIREGIRLKTALQAMIY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 368 KKQLKLSS--LGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLP 445
Cdd:cd18591 97 EKALRLSSwnLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIGAALILVMTPLQYL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 446 FAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSS 525
Cdd:cd18591 177 IARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLMTFLTQASPILVTL 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 526 VVFLGCALLKSAPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 578
Cdd:cd18591 257 VTFGLYPYLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
470-827 |
2.52e-33 |
|
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: 139.10 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 470 EILNSMKVIKLQSWEDEFKKKIescrDDEF-TWLAKA---QLTKAFGSFLYWMSPTIVSSVV-FLGCALLKSAPLNASTI 544
Cdd:TIGR01193 339 EDLNGIETIKSLTSEAERYSKI----DSEFgDYLNKSfkyQKADQGQQAIKAVTKLILNVVIlWTGAYLVMRGKLTLGQL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 545 FTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRLNNFLLDDelkmDEIERSGLDASGTAV--DIQVGNFGWEPETKIPTL 622
Cdd:TIGR01193 415 ITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVD----SEFINKKKRTELNNLngDIVINDVSYSYGYGSNIL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 623 RNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDNILY 689
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhtlrqFINYLPQEPYIFSGSILENLLL 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 690 G-KP-MESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAgvl 767
Cdd:TIGR01193 571 GaKEnVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE--- 647
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 768 fHKCVED--SLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQLVNA 827
Cdd:TIGR01193 648 -KKIVNNllNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1216-1452 |
4.86e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 136.69 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1216 PSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLR 1295
Cdd:PRK11176 337 RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1296 MKLSIIPQEPTLFRGCIRTNL--DPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLL 1373
Cdd:PRK11176 417 NQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1374 KRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKL 1452
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1238-1386 |
1.32e-32 |
|
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: 124.30 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRG-CIRTNL 1316
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1317 -------DPLGVYSDDEIWKALEKCqlkttisNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATA 1386
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
615-815 |
3.81e-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: 3.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 615 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKV------------FG-SIAYVSQTSWIQSG 681
Cdd:COG4618 341 PGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlsqwdreeLGrHIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNI-LYGKPMESRRYNAAIKACAldKDM-----NGFGhgdlTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:COG4618 421 TIAENIaRFGDADPEKVVAAAKLAGV--HEMilrlpDGYD----TRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 756 FSAVDAhtAGvlfhkcvEDSLKE---------KTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:COG4618 495 NSNLDD--EG-------EAALAAairalkargATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1221-1428 |
9.29e-32 |
|
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: 122.71 E-value: 9.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1300
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLFRGCIRTNLdplgvysddeiwkalekcqlkttisnlpnkldssvsdegenWSVGQRQLFCLGRVLLKRNKILV 1380
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1381 LDEATASIDSATDAIIQRIIRE-EFADCTVITVAHRvPTVIDS-DMVMVL 1428
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHR-PETLASaDRILVL 168
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
622-805 |
3.61e-31 |
|
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: 122.58 E-value: 3.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--------SIAYVSQTS----WIqsgTIRDNILY 689
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQQDallpWL---TVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 690 G------KPMESRRY-NAAIKACALDkdmnGFGHgdlteigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 762
Cdd:cd03293 97 GlelqgvPKAEARERaEELLELVGLS----GFEN-------AYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 763 TAGVLfHKCVEDSLKE--KTVILVTHQVE---FLSevDQILVMEE--GTI 805
Cdd:cd03293 166 TREQL-QEELLDIWREtgKTVLLVTHDIDeavFLA--DRVVVLSArpGRI 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
605-809 |
6.50e-31 |
|
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: 121.83 E-value: 6.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 605 DIQVGNFG--WEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SI 669
Cdd:cd03244 2 DIEFKNVSlrYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 670 AYVSQTSWIQSGTIRDNI-LYGKPMESRRYNaAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADAD 748
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 749 VYLLDDPFSAVDAHTAGVLfHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSG 809
Cdd:cd03244 160 ILVLDEATASVDPETDALI-QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1221-1442 |
9.52e-31 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 121.52 E-value: 9.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVE-----PASGCILIDGIDISKIGLKD-- 1293
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1294 LRMKLSIIPQEPTLFRGCIRTNLDpLGV----YSDDEIWKALEKCQLKTTisnlpnKLDSSVSDE--GENWSVGQRQLFC 1367
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA-YGLrlhgIKLKEELDERVEEALRKA------ALWDEVKDRlhALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1368 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAH------RVptvidSDMVMVLSFGDLVEYNEPSK 1441
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 1063712898 1442 L 1442
Cdd:cd03260 227 I 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
622-805 |
9.94e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 122.51 E-value: 9.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--------SIAYVSQTS----WIqsgTIRDNILY 689
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQEPallpWL---TVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 690 G-----KPMESRRYNA--AIKACALDKDMNGFGHgdlteigqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 762
Cdd:COG1116 104 GlelrgVPKAERRERAreLLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 763 TAGVLfHKCVEDSLKE--KTVILVTHQVE---FLSevDQILVMEE--GTI 805
Cdd:COG1116 173 TRERL-QDELLRLWQEtgKTVLFVTHDVDeavFLA--DRVVVLSArpGRI 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
622-825 |
2.16e-30 |
|
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: 121.05 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDNIL 688
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 689 YGKP-MESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVL 767
Cdd:cd03252 98 LADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 768 FHKcVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQLV 825
Cdd:cd03252 178 MRN-MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
604-805 |
8.21e-30 |
|
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: 118.73 E-value: 8.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 604 VDIQVGNFGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IA 670
Cdd:cd03248 12 VKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 671 YVSQTSWIQSGTIRDNILYG---KPMESRRyNAAIKACAlDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADA 747
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGlqsCSFECVK-EAAQKAHA-HSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 748 DVYLLDDPFSAVDAHTAGVLfHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTI 805
Cdd:cd03248 170 QVLILDEATSALDAESEQQV-QQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1182-1452 |
8.85e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 126.48 E-value: 8.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1182 LSNSIISVERIKQymnIPEEPPAIIDDKRPPSSwPSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGK 1261
Cdd:PRK11160 304 LGQVIASARRINE---ITEQKPEVTFPTTSTAA-ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1262 STLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNL---DPLGvySDDEIWKALEKCQLKT 1338
Cdd:PRK11160 380 STLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLEK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1339 TISNlPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVpT 1418
Cdd:PRK11160 458 LLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRL-T 535
|
250 260 270
....*....|....*....|....*....|....*
gi 1063712898 1419 VIDS-DMVMVLSFGDLVEYNEPSKLMETDSYFSKL 1452
Cdd:PRK11160 536 GLEQfDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
606-805 |
1.57e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.61 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 606 IQVGNFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYV 672
Cdd:COG4619 1 LELEGLSFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 673 SQTSWIQSGTIRDNILYGKPMESRRYNAAikacALDKDMN--GFGHGDLTeigQRGINLSGGQKQRIQLARAVYADADVY 750
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRERKFDRE----RALELLErlGLPPDILD---KPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 751 LLDDPFSAVDAHTAGvLFHKCVEDSLKEK--TVILVTHQVEFLSEV-DQILVMEEGTI 805
Cdd:COG4619 153 LLDEPTSALDPENTR-RVEELLREYLAEEgrAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1218-1432 |
3.01e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 127.45 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1218 NGTIHLQELKIRY--RPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRL------------------------ 1271
Cdd:PTZ00265 1163 KGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1272 ------------------------------VEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDpLGV 1321
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGK 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1322 --YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRI 1399
Cdd:PTZ00265 1321 edATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270
....*....|....*....|....*....|....*
gi 1063712898 1400 IRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGD 1432
Cdd:PTZ00265 1401 IVDikDKADKTIITIAHRIASIKRSDKIVVFNNPD 1435
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
615-805 |
7.10e-29 |
|
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: 114.24 E-value: 7.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 615 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQTSWIQSG 681
Cdd:cd03246 11 PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNILygkpmesrrynaaikacaldkdmngfghgdlteigqrginlSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:cd03246 91 SIAENIL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063712898 762 HTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTI 805
Cdd:cd03246 130 EGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
618-804 |
7.80e-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: 113.49 E-value: 7.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSiayvsQTSWIQSGTIRDNILYgkpmesrr 697
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRIGY-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 698 ynaaikacaldkdmngfghgdlteIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLK 777
Cdd:cd00267 78 ------------------------VPQ----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE 129
|
170 180
....*....|....*....|....*...
gi 1063712898 778 EKTVILVTHQVEFLSEV-DQILVMEEGT 804
Cdd:cd00267 130 GRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1200-1444 |
9.11e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 122.70 E-value: 9.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1200 EEPPAIIDDKRPPSSWPSNGT--IHLQELKIRY---RPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEP 1274
Cdd:COG1123 238 AAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1275 ASGCILIDGIDISKIG---LKDLRMKLSIIPQEPT--LF-RGCIRTNL-DPL---GVYSDDEIWK----ALEKCQLKTTI 1340
Cdd:COG1123 318 TSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYssLNpRMTVGDIIaEPLrlhGLLSRAERRErvaeLLERVGLPPDL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1341 SN-LPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE---EFaDCTVITVAHRV 1416
Cdd:COG1123 398 ADrYPHEL-----------SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqrEL-GLTYLFISHDL 465
|
250 260
....*....|....*....|....*....
gi 1063712898 1417 PTVID-SDMVMVLSFGDLVEYNEPSKLME 1444
Cdd:COG1123 466 AVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1221-1445 |
9.86e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 116.44 E-value: 9.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRP--NAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1298
Cdd:COG1124 2 LEVRNLSVSYGQggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPtlfrgciRTNLDP--------------LGV-YSDDEIWKALEKCQLKTTI-SNLPNKLdssvsdegenwSVGQ 1362
Cdd:COG1124 82 QMVFQDP-------YASLHPrhtvdrilaeplriHGLpDREERIAELLEQVGLPPSFlDRYPHQL-----------SGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1363 RQLFCLGRVLLKRNKILVLDEATASIDSATDAII----QRIIREEfaDCTVITVAHRVPtVID--SDMVMVLSFGDLVEY 1436
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEIlnllKDLREER--GLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEE 220
|
....*....
gi 1063712898 1437 NEPSKLMET 1445
Cdd:COG1124 221 LTVADLLAG 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1228-1431 |
1.13e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 113.11 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1228 IRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQeptL 1307
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1308 frgcirtnldplgvysddeiwkalekcqlkttisnlpnkldssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATAS 1387
Cdd:cd00267 82 ---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063712898 1388 IDSATDAIIQRIIREEFAD-CTVITVAHRVPTVID-SDMVMVLSFG 1431
Cdd:cd00267 111 LDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
610-809 |
1.42e-28 |
|
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: 113.56 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 610 NFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS------------IAYVSQTSW 677
Cdd:cd03247 7 SFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 678 IQSGTIRDNIlygkpmesrrynaaikacaldkdmngfghgdlteigqrGINLSGGQKQRIQLARAVYADADVYLLDDPFS 757
Cdd:cd03247 86 LFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 758 AVDAHTAGVLFhKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSG 809
Cdd:cd03247 128 GLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
290-578 |
1.79e-28 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 116.93 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 290 FIAVFAFLrTFAVVSLPLMLYVFVDYANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYKK 369
Cdd:cd18559 2 FLLIKLVL-CNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 370 QLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKM 449
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 450 LQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVFL 529
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 530 GCALLKS-APLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 578
Cdd:cd18559 241 AYVSRHSlAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
291-578 |
2.18e-28 |
|
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: 116.51 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 291 IAVFAFLRTFAVVSLPLMLYVFVDYANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYKKQ 370
Cdd:cd18592 3 ILLLLISLIFGFIGPTILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 371 LKLSSLGRKrhSSGEIVNYIAVDAYRMGE---FLWWFHSGWSLSLQLLLSTAVLFG---VVGAGAFPglillllcglLNL 444
Cdd:cd18592 83 LRLRSLGDK--SVGELINIFSNDGQRLFDaavFGPLVIGGPVVLILGIVYSTYLLGpwaLLGMLVFL----------LFY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 445 PFAKMLQNCQTQF----MIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSP 520
Cdd:cd18592 151 PLQAFIAKLTGKFrrkaIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVP 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 521 TIVSSVVFLGCALLKSApLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 578
Cdd:cd18592 231 VIASVVTFLAHVALGND-LTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
615-804 |
2.31e-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: 114.10 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 615 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQ--TSWIQ 679
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLVFQnpDDQFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 680 SGTIRDNILYG-------KPMESRRYNAAIKACaldkdmngfghgDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYL 751
Cdd:cd03225 90 GPTVEEEVAFGlenlglpEEEIEERVEEALELV------------GLEGLRDRSPfTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 752 LDDPFSAVDAHTAGVLFHKcVEDsLKE--KTVILVTHQVEFLSEV-DQILVMEEGT 804
Cdd:cd03225 158 LDEPTAGLDPAGRRELLEL-LKK-LKAegKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
618-809 |
2.33e-28 |
|
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: 114.15 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------SIAYVSQT----SWIqsgT 682
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDyalfPHL---T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 683 IRDNILYG-------KPMESRRYNAAIKACALDKDMNGFGHGdlteigqrginLSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:cd03259 89 VAENIAFGlklrgvpKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 756 FSAVDAHTAGVLFHKcVEDSLKE--KTVILVTH-QVEFLSEVDQILVMEEGTITQSG 809
Cdd:cd03259 158 LSALDAKLREELREE-LKELQRElgITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
598-824 |
2.48e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 121.86 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 598 DASGTAVDIQVGN--FGWePETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------- 667
Cdd:PRK11160 331 TAAADQVSLTLNNvsFTY-PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyse 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 668 -----SIAYVSQTSWIQSGTIRDNILYGKPMES-RRYNAAIKACALDKDMNGfGHGDLTEIGQRGINLSGGQKQRIQLAR 741
Cdd:PRK11160 410 aalrqAISVVSQRVHLFSATLRDNLLLAAPNASdEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 742 AVYADADVYLLDDPFSAVDAHTA----GVLFHKCvedslKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMM 817
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETErqilELLAEHA-----QNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
....*..
gi 1063712898 818 GTAFQQL 824
Cdd:PRK11160 564 QGRYYQL 570
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
547-787 |
3.15e-28 |
|
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: 121.31 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 547 VLATLRVMsEPVKIIPDAISAIIQGNVSFQRLNNfLLDDELKMDEIErsgLDASGTAVDIQVG------NFGWEPETkiP 620
Cdd:TIGR02868 277 VLLPLAAF-EAFAALPAAAQQLTRVRAAAERIVE-VLDAAGPVAEGS---APAAGAVGLGKPTlelrdlSAGYPGAP--P 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 621 TLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQTSWIQSGTIRDNI 687
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 LYGKPMES-RRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGV 766
Cdd:TIGR02868 430 RLARPDATdEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
250 260
....*....|....*....|.
gi 1063712898 767 LFHKcVEDSLKEKTVILVTHQ 787
Cdd:TIGR02868 510 LLED-LLAALSGRTVVLITHH 529
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
622-757 |
3.35e-28 |
|
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: 111.59 E-value: 3.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSG-TIRDNI 687
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 688 LYGKPMEsrRYNAAIKACALDKDMNGFGHGDL--TEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFS 757
Cdd:pfam00005 81 RLGLLLK--GLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
611-816 |
4.40e-28 |
|
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: 113.97 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 611 FGWEPETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSW 677
Cdd:COG1122 8 FSYPGGTPA--LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 678 IQ--SGTIRDNILYGkPMESRRYNAAIKAC---ALDKdmngFGhgdLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYL 751
Cdd:COG1122 86 DQlfAPTVEEDVAFG-PENLGLPREEIRERveeALEL----VG---LEHLADRPPhELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 752 LDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELLM 816
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFS 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
539-824 |
4.90e-28 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 121.28 E-value: 4.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 539 LNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRLnnF-LLDDELKMDEIERSGLDASGtavDIQVGN--FGWeP 615
Cdd:PRK11176 279 LTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTL--FaILDLEQEKDEGKRVIERAKG---DIEFRNvtFTY-P 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 616 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGT 682
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQNVHLFNDT 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 683 IRDNILYGKPMESRRY---NAAIKACALDKdMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAV 759
Cdd:PRK11176 433 IANNIAYARTEQYSREqieEAARMAYAMDF-INKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 760 DAHTAGVLfHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQL 824
Cdd:PRK11176 512 DTESERAI-QAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
618-825 |
6.35e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 121.75 E-value: 6.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIR 684
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 DNILYG---KPMESRRyNAAIKACALDKDMnGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:TIGR00958 573 ENIAYGltdTPDEEIM-AAAKAANAHDFIM-EFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 762 HTAGVLFHkcvEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQLV 825
Cdd:TIGR00958 651 ECEQLLQE---SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
622-826 |
6.72e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 113.62 E-value: 6.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------------SIAYVSQTSWIQSG-TIRDNI- 687
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 ----LYGKPMESR--RYNAAIKACALDKDMNgfghgdlteigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:COG1131 96 ffarLYGLPRKEAreRIDELLELFGLTDAAD-----------RKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 762 HTAGVLFHKCVEDSLKEKTVILVTHQvefLSEV----DQILVMEEGTITQSGKYEELL--MMGTAFQQLVN 826
Cdd:COG1131 165 EARRELWELLRELAAEGKTVLLSTHY---LEEAerlcDRVAIIDKGRIVADGTPDELKarLLEDVFLELTG 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
622-809 |
7.12e-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: 111.76 E-value: 7.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQtswiqsgtirdnil 688
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 689 ygkpmesrrynaAIKACaldkdmngfghgDLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVD-AHTAGV 766
Cdd:cd03214 81 ------------ALELL------------GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDiAHQIEL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 767 LfhkcveDSLKE------KTVILVTHQVEFLSEV-DQILVMEEGTITQSG 809
Cdd:cd03214 137 L------ELLRRlarergKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
611-824 |
1.05e-27 |
|
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: 120.31 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 611 FGWEPETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWIQS-G------- 681
Cdd:COG5265 365 FGYDPERPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqDIRDVTQASLRAAiGivpqdtv 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 ----TIRDNILYGKPMESRR-YNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPF 756
Cdd:COG5265 443 lfndTIAYNIAYGRPDASEEeVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 757 SAVDAHTagvlfHKCVEDSLKE----KTVILVTHQvefLSEV---DQILVMEEGTITQSGKYEELLMMGTAFQQL 824
Cdd:COG5265 523 SALDSRT-----ERAIQAALREvargRTTLVIAHR---LSTIvdaDEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
610-824 |
1.08e-27 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 121.00 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 610 NFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTS 676
Cdd:TIGR01846 462 RFRYAPDSP-EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGvdlaiadpawlrrQMGVVLQEN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 677 WIQSGTIRDNILYGKP---MESRRYnAAIKACALDKdMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLD 753
Cdd:TIGR01846 541 VLFSRSIRDNIALCNPgapFEHVIH-AAKLAGAHDF-ISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFD 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 754 DPFSAVDAHTAGVLFHKCVEDSlKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQL 824
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1221-1435 |
1.44e-27 |
|
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: 110.87 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGlKDLRMKLSI 1300
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLFRGCIRTNLdplgvysddeiwkalekcqlkttisnlpnkldssvsdeGENWSVGQRQLFCLGRVLLKRNKILV 1380
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1381 LDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVE 1435
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1221-1444 |
2.08e-27 |
|
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: 112.04 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1300
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPT--LFRGCIR-------TNldpLGVySDDEIWKALEKCqLKTTisNLPNKLDSSVSDegenWSVGQRQLFCLGRV 1371
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpEN---LGL-PREEIRERVEEA-LELV--GLEHLADRPPHE----LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1372 LLKRNKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLME 1444
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFS 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
593-827 |
3.20e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 118.91 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 593 ERSGL-DASGTAVDIQVGNFGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKS---SLLHAVLGeiPKvSGTVKVFG- 667
Cdd:PRK13657 321 DPPGAiDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKStliNLLQRVFD--PQ-SGRILIDGt 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 668 ------------SIAYVSQTSWIQSGTIRDNILYGKP--MESRRYNAAIKACALD---KDMNGFGhgdlTEIGQRGINLS 730
Cdd:PRK13657 398 dirtvtraslrrNIAVVFQDAGLFNRSIEDNIRVGRPdaTDEEMRAAAERAQAHDfieRKPDGYD----TVVGERGRQLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 731 GGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLfHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGK 810
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
250
....*....|....*..
gi 1063712898 811 YEELLMMGTAFQQLVNA 827
Cdd:PRK13657 553 FDELVARGGRFAALLRA 569
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1183-1438 |
4.01e-27 |
|
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: 117.83 E-value: 4.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1183 SNSIISVERIKQYMNipEEPPaiiddKRPPSSWPS-NGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGK 1261
Cdd:TIGR01842 285 SGARQAYKRLNELLA--NYPS-----RDPAMPLPEpEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGK 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1262 STLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDPLGVYSDDE-IWKALEKCQLKTTI 1340
Cdd:TIGR01842 358 STLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEkIIEAAKLAGVHELI 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1341 SNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATD-AIIQRIIREEFADCTVITVAHRVPTV 1419
Cdd:TIGR01842 438 LRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEqALANAIKALKARGITVVVITHRPSLL 517
|
250
....*....|....*....
gi 1063712898 1420 IDSDMVMVLSFGDLVEYNE 1438
Cdd:TIGR01842 518 GCVDKILVLQDGRIARFGE 536
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1226-1437 |
7.90e-27 |
|
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: 110.29 E-value: 7.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1226 LKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG---LKDLRMKLSI 1300
Cdd:cd03257 7 LSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPtlfrgciRTNLDPL--------------GVYSDDE-----IWKALEKCQLKTTISN-LPNKLdssvsdegenwSV 1360
Cdd:cd03257 87 VFQDP-------MSSLNPRmtigeqiaeplrihGKLSKKEarkeaVLLLLVGVGLPEEVLNrYPHEL-----------SG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1361 GQRQLFCLGRVLLKRNKILVLDEATASIDSATDA-IIQRI--IREEFaDCTVITVAHRVPTV-IDSDMVMVLSFGDLVEY 1436
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAqILDLLkkLQEEL-GLTLLFITHDLGVVaKIADRVAVMYAGKIVEE 227
|
.
gi 1063712898 1437 N 1437
Cdd:cd03257 228 G 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1217-1455 |
1.16e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.24 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1217 SNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM 1296
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1297 KLSIIPQEP-TLFrgcirtnldpLGVYSDDEIWKALE-KC----QLKTTISNLPNK--LDSSVSDEGENWSVGQRQLFCL 1368
Cdd:PRK13632 84 KIGIIFQNPdNQF----------IGATVEDDIAFGLEnKKvppkKMKDIIDDLAKKvgMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1369 GRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPS------ 1440
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKeilnnk 233
|
250
....*....|....*...
gi 1063712898 1441 ---KLMETDSYFSKLVAE 1455
Cdd:PRK13632 234 eilEKAKIDSPFIYKLSK 251
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
622-815 |
2.42e-26 |
|
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: 109.75 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSG-TIRDNI 687
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEPPAPFGlTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 LYG-KP------MESRRYNAAIKAcALDK-DMNGFGHGDLTEigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAV 759
Cdd:COG1120 97 ALGrYPhlglfgRPSAEDREAVEE-ALERtGLEHLADRPVDE-------LSGGERQRVLIARALAQEPPLLLLDEPTSHL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 760 D-AHTAGVLfhkcveDSLKE------KTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:COG1120 169 DlAHQLEVL------ELLRRlarergRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
290-578 |
3.40e-26 |
|
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: 110.39 E-value: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 290 FIAVFAFLRTFAVVSLPLMLYVFVDY--ANSDHRDLRNGFFNLACLVMLKLVESLTmRHWYF-ASRRSGMRIRSALMVAA 366
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYfeGNGSSISLTEAYLYAGGVSLCSFLFIIT-HHPYFfGMQRIGMRLRVACSSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 367 YKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPF 446
Cdd:cd18593 80 YRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 447 AKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSV 526
Cdd:cd18593 160 GKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 527 VFLGCALLkSAPLNASTIFTVLAtlrvMSEPVKII-----PDAISAIIQGNVSFQRL 578
Cdd:cd18593 240 TFLAYILL-GNILTAERVFVTMA----LYNAVRLTmtlffPFAIQFGSELSVSIRRI 291
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
616-805 |
5.57e-26 |
|
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: 107.58 E-value: 5.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 616 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHaVLGEIPKV-SGTVKVFG-----------------SIAYVSQT-S 676
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGtdisklsekelaafrrrHIGFVFQSfN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 677 WIQSGTIRDNI-----LYGKPMESRRYNA--AIKACALDKDMNGFGHgdlteigqrgiNLSGGQKQRIQLARAVYADADV 749
Cdd:cd03255 93 LLPDLTALENVelpllLAGVPKKERRERAeeLLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 750 YLLDDPFSAVDAHTAGV---LFHKCVEDslKEKTVILVTHQVEFLSEVDQILVMEEGTI 805
Cdd:cd03255 162 ILADEPTGNLDSETGKEvmeLLRELNKE--AGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
618-815 |
5.94e-26 |
|
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: 108.02 E-value: 5.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------------SIAYVSQTSWIQSG-TIR 684
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRlTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 DNILY---GKPMESRRYNAAIKAcaLDKDMngfghgDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 760
Cdd:COG4555 93 ENIRYfaeLYGLFDEELKKRIEE--LIELL------GLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 761 AHTAGvLFHKCVEdSLKE--KTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:COG4555 165 VMARR-LLREILR-ALKKegKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELR 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1221-1444 |
9.32e-26 |
|
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: 107.64 E-value: 9.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRmKLSI 1300
Cdd:COG4555 2 IEVENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLF-RGCIRTNLDPLGvysddEIWKaLEKCQLKTTISN------LPNKLDSSVSDegenWSVGQRQLFCLGRVLL 1373
Cdd:COG4555 79 LPDERGLYdRLTVRENIRYFA-----ELYG-LFDEELKKRIEEliellgLEEFLDRRVGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1374 KRNKILVLDEATASIdsatDAIIQRIIREEFADC-----TVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLME 1444
Cdd:COG4555 149 HDPKVLLLDEPTNGL----DVMARRLLREILRALkkegkTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1221-1444 |
9.43e-26 |
|
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: 113.46 E-value: 9.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPA---SGCILIDGIDISKIGLKDLRMK 1297
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1298 LSIIPQEPTlfrgcirTNLDPLGV------------YSDDEIWK----ALEKCQLKTTISNLPNKLdssvsdegenwSVG 1361
Cdd:COG1123 85 IGMVFQDPM-------TQLNPVTVgdqiaealenlgLSRAEARArvleLLEAVGLERRLDRYPHQL-----------SGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1362 QRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNE 1438
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGP 226
|
....*.
gi 1063712898 1439 PSKLME 1444
Cdd:COG1123 227 PEEILA 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1221-1414 |
5.49e-25 |
|
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: 105.90 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1300
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTL-F---------RGciRTN-LDPLGVYSDDE---IWKALEKCQlkttISNLPNKLDSSVSDegenwsvGQRQLF 1366
Cdd:COG1120 80 VPQEPPApFgltvrelvaLG--RYPhLGLFGRPSAEDreaVEEALERTG----LEHLADRPVDELSG-------GERQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 1367 CLGRVLLKRNKILVLDEATASID----SATDAIIQRIIREEfaDCTVITVAH 1414
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARER--GRTVVMVLH 196
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
622-802 |
8.98e-25 |
|
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: 103.71 E-value: 8.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS------IAYVSQTSWI--QSG-----TIRDNI- 687
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdarEDYRRRLAYLghADGlkpelTVRENLr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 ----LYGKPMESRRYNAAIKACALDkdmngfGHGDLtEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAht 763
Cdd:COG4133 98 fwaaLYGLRADREAIDEALEAVGLA------GLADL-PVRQ----LSAGQKRRVALARLLLSPAPLWLLDEPFTALDA-- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063712898 764 AGV-LFHKCVEDSLKE-KTVILVTHQvEFLSEVDQILVMEE 802
Cdd:COG4133 165 AGVaLLAELIAAHLARgGAVLLTTHQ-PLELAAARVLDLGD 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
622-805 |
9.13e-25 |
|
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: 102.48 E-value: 9.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGsiayvsQTSWIQSGTIRDNILYgKPMESRrynaa 701
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRIGY-LPEEPS----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 702 ikacaLDKDMNGFGHgdlteigqrgINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTV 781
Cdd:cd03230 84 -----LYENLTVREN----------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTI 148
|
170 180
....*....|....*....|....*
gi 1063712898 782 ILVTHQVEFLSEV-DQILVMEEGTI 805
Cdd:cd03230 149 LLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
622-804 |
1.35e-24 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 102.27 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG---------------SIAYVSQTSWIQSG-TIRD 685
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 686 NILYGkpmesrrynaaikacaldkdmngfghgdlteigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAG 765
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063712898 766 VlfhkcVEDSLKE------KTVILVTHQVEFLSEV-DQILVMEEGT 804
Cdd:cd03229 138 E-----VRALLKSlqaqlgITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
622-815 |
1.89e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 106.38 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTV----KVFGS--------IAYVSQ--------Tswiqs 680
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPD-SGRIvlngRDLFTnlpprerrVGFVFQhyalfphmT----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 681 gtIRDNILYGkpMESRRYN-AAIKACA---LDK-DMNGFGHgdlteigQRGINLSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:COG1118 92 --VAENIAFG--LRVRPPSkAEIRARVeelLELvQLEGLAD-------RYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 756 FSAVDAHTAGVLfhkcvEDSLKE------KTVILVTHQVEflsEV----DQILVMEEGTITQSGKYEELL 815
Cdd:COG1118 161 FGALDAKVRKEL-----RRWLRRlhdelgGTTVFVTHDQE---EAlelaDRVVVMNQGRIEQVGTPDEVY 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1188-1421 |
1.99e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.90 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1188 SVERI---KQYMNIPEEPPAIIDDKRPPSSwpsnGTIHLQELKIRyRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTL 1264
Cdd:COG4178 331 TVDRLagfEEALEAADALPEAASRIETSED----GALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1265 ISALFRLVEPASGCILIDGIDiskiglkdlrmKLSIIPQEPTLFRGCIRTNL---DPLGVYSDDEIWKALEKCQLkttiS 1341
Cdd:COG4178 406 LRAIAGLWPYGSGRIARPAGA-----------RVLFLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL----G 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1342 NLPNKLDssvsdEGENW----SVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRvP 1417
Cdd:COG4178 471 HLAERLD-----EEADWdqvlSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-S 544
|
....
gi 1063712898 1418 TVID 1421
Cdd:COG4178 545 TLAA 548
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
610-806 |
3.24e-24 |
|
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: 101.95 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 610 NFGWEPETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKV----------FGSIAYVSQTSWIQ 679
Cdd:cd03226 6 SFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLngkpikakerRKSIGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 680 --SGTIRDNILYGKPMESRRYNAAikACALdKDMNGFGHGDlteigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFS 757
Cdd:cd03226 84 lfTDSVREELLLGLKELDAGNEQA--ETVL-KDLDLYALKE-----RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 758 AVDAHTA---GVLFHKCvedSLKEKTVILVTHQVEFLSEV-DQILVMEEGTIT 806
Cdd:cd03226 156 GLDYKNMervGELIREL---AAQGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1223-1431 |
4.14e-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: 101.77 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1223 LQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIP 1302
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1303 QEP-------TLFR----GCIRTNLDPlgvysdDEIWKALEKCqLKTTisNLPNKLDSSVSDegenWSVGQRQLFCLGRV 1371
Cdd:cd03225 82 QNPddqffgpTVEEevafGLENLGLPE------EEIEERVEEA-LELV--GLEGLRDRSPFT----LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1372 LLKRNKILVLDEATASIDSATDAIIQRIIReEFADC--TVITVAHRVPTVID-SDMVMVLSFG 1431
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
616-826 |
5.48e-24 |
|
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: 102.86 E-value: 5.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 616 ETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSG-TVKVFG-------------SIAYVS---QTSWI 678
Cdd:COG1119 15 GKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGerrggedvwelrkRIGLVSpalQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 679 QSGTIRDNIL---YGKPMESRRYNAAIKACALDKdMNGFGhgdLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDD 754
Cdd:COG1119 93 RDETVLDVVLsgfFDSIGLYREPTDEQRERAREL-LELLG---LAHLADRPFGtLSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 755 PFSAVDAHtAGVLFHKCVED--SLKEKTVILVTHQVE-FLSEVDQILVMEEGTITQSGKYEELL---MMGTAFQQLVN 826
Cdd:COG1119 169 PTAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPKEEVLtseNLSEAFGLPVE 245
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1219-1428 |
5.91e-24 |
|
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: 108.30 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1219 GTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1298
Cdd:COG4618 329 GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKI 1378
Cdd:COG4618 409 GYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 1379 LVLDEATASIDSATDAIIQRIIREEFAD-CTVITVAHRvPTVIDS-DMVMVL 1428
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHR-PSLLAAvDKLLVL 539
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
620-800 |
5.97e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.77 E-value: 5.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--SIAYVSQTS---WIQSGTIRDNI---LYGK 691
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSevpDSLPLTVRDLVamgRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 692 PMESRRYNAAIKAcALDKDMNGFGhgdLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHK 770
Cdd:NF040873 86 RGLWRRLTRDDRA-AVDDALERVG---LADLAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAL 161
|
170 180 190
....*....|....*....|....*....|
gi 1063712898 771 CVEDSLKEKTVILVTHQVEFLSEVDQILVM 800
Cdd:NF040873 162 LAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1191-1450 |
7.04e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 108.26 E-value: 7.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1191 RIKQYMnipEEPPAIIDDKRPPSSWPSNGTIHLQELkiRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFR 1270
Cdd:PRK10789 289 RIRAML---AEAPVVKDGSEPVPEGRGELDVNIRQF--TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1271 LVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLdPLGV--YSDDEIWKALEKCQLKTTISNLPNKLD 1348
Cdd:PRK10789 364 HFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI-ALGRpdATQQEIEHVARLASVHDDILRLPQGYD 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1349 SSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVL 1428
Cdd:PRK10789 443 TEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVM 522
|
250 260
....*....|....*....|..
gi 1063712898 1429 SFGDLVEYNEPSKLMETDSYFS 1450
Cdd:PRK10789 523 QHGHIAQRGNHDQLAQQSGWYR 544
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
618-814 |
8.17e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.77 E-value: 8.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG-----------SIAYVSQtSWI--QSGTI 683
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPT-SGEILIGGrdvtdlppkdrNIAMVFQ-SYAlyPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 684 RDNILYgkPMESRRYNAAikacaldkdmngfghgdltEIGQR--------GI---------NLSGGQKQRIQLARAVYAD 746
Cdd:COG3839 93 YENIAF--PLKLRKVPKA-------------------EIDRRvreaaellGLedlldrkpkQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 747 ADVYLLDDPFSAVDAHTAGVL------FHKcvedSLKeKTVILVTH-QVEFLSEVDQILVMEEGTITQSGKYEEL 814
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMraeikrLHR----RLG-TTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1223-1434 |
1.21e-23 |
|
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: 99.43 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1223 LQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIP 1302
Cdd:cd03214 2 VENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1303 QeptlfrgcirtnldplgvysddeiwkALEKCQlkttISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLD 1382
Cdd:cd03214 80 Q--------------------------ALELLG----LAHLADRPFNELSG-------GERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1383 EATASID----SATDAIIQRIIREEfaDCTVITVAHrvptviD-------SDMVMVLSFGDLV 1434
Cdd:cd03214 123 EPTSHLDiahqIELLELLRRLARER--GKTVVMVLH------DlnlaaryADRVILLKDGRIV 177
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
620-814 |
3.21e-23 |
|
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: 100.11 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG-----------SIAYVSQT-SWIQSGTIRDN 686
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERPD-SGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILYG---KPMESRRYNAAIKAcaldKDMNGFGHGDLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 762
Cdd:cd03296 95 VAFGlrvKPRSERPPEAEIRA----KVHELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 763 TAGVL--FHKCVEDSLKEKTViLVTH-QVEFLSEVDQILVMEEGTITQSGKYEEL 814
Cdd:cd03296 171 VRKELrrWLRRLHDELHVTTV-FVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
622-814 |
4.41e-23 |
|
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: 99.50 E-value: 4.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWI----------QSG------TIR 684
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGeDISGLSEAELYrlrrrmgmlfQSGalfdslTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 DNILYgkPM-ESRRYNAA-IKACALDKdmngfghgdLTEIGQRGI------NLSGGQKQRIQLARAVYADADVYLLDDPF 756
Cdd:cd03261 96 ENVAF--PLrEHTRLSEEeIREIVLEK---------LEAVGLRGAedlypaELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 757 SAVDAHTAGVlfhkcVED---SLKEK---TVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEEL 814
Cdd:cd03261 165 AGLDPIASGV-----IDDlirSLKKElglTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
620-815 |
5.85e-23 |
|
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: 99.68 E-value: 5.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQtswiQSG----- 681
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQ----QIGlfphm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNI-----LYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEigqrginLSGGQKQRIQLARAVYADADVYLLDDPF 756
Cdd:cd03295 91 TVEENIalvpkLLKWPKEKIRERADELLALVGLDPAEFADRYPHE-------LSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 757 SAVDAHTagvlfhkcvEDSLKE----------KTVILVTHQV-EFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:cd03295 164 GALDPIT---------RDQLQEefkrlqqelgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
622-814 |
6.61e-23 |
|
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: 98.79 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-----LGEIPKVSGTVKVFGSIAYVSQTSWIQ---------------SG 681
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDVLElrrrvgmvfqkpnpfPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNILYGKP---MESRRYNAAIKACALDKdmngfghGDLT-EIGQR--GINLSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:cd03260 96 SIYDNVAYGLRlhgIKLKEELDERVEEALRK-------AALWdEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 756 FSAVDAHTAGVlfhkcVEDSLKE----KTVILVTH---QVEFLSevDQILVMEEGTITQSGKYEEL 814
Cdd:cd03260 169 TSALDPISTAK-----IEELIAElkkeYTIVIVTHnmqQAARVA--DRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
615-815 |
1.88e-22 |
|
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: 103.06 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 615 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIP---KVSGTVKVFG-------------SIAYVSQTSWI 678
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGrdllelsealrgrRIGMVFQDPMT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 679 Q--SGTIRDNIlygkpMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:COG1123 95 QlnPVTVGDQI-----AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 756 FSAVDAHTAgvlfhKCVEDSLKE------KTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:COG1123 170 TTALDVTTQ-----AEILDLLRElqrergTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
618-809 |
2.22e-22 |
|
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: 97.58 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG----------------SIAYVSQ---TSWI 678
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQdpmSSLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 679 QSGTIRDNILygKPMESRRYN---AAIKACALDKDMngfGHGDLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDD 754
Cdd:cd03257 97 PRMTIGEQIA--EPLRIHGKLskkEARKEAVLLLLV---GVGLPEEVLNRYPHeLSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 755 PFSAVDAHT-AGV--LFHKcvedsLKEK---TVILVTHQVEFLSEV-DQILVMEEGTITQSG 809
Cdd:cd03257 172 PTSALDVSVqAQIldLLKK-----LQEElglTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1234-1428 |
2.89e-22 |
|
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: 96.38 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1234 APLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGidiskiglkdlrmKLSIIPQEPTLFRGCIR 1313
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEPWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1314 TNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSAT- 1392
Cdd:cd03250 84 ENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVg 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063712898 1393 DAIIQRIIREEFADC-TVITVAHRVPTVIDSDMVMVL 1428
Cdd:cd03250 164 RHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVL 200
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
616-806 |
4.81e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 96.27 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 616 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHaVLGEIPKV-SGTVKVFG-----------------SIAYVSQTS- 676
Cdd:COG1136 18 EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdisslserelarlrrrHIGFVFQFFn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 677 WIQSGTIRDNILY-----GKPMESRRynAAIKAcALDKdmngFGhgdLTEIGQRGIN-LSGGQKQRIQLARAVYADADVY 750
Cdd:COG1136 97 LLPELTALENVALplllaGVSRKERR--ERARE-LLER----VG---LGDRLDHRPSqLSGGQQQRVAIARALVNRPKLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 751 LLDDPFSAVDAHTAGV---LFHKCVEDSlkEKTVILVTHQVEFLSEVDQILVMEEGTIT 806
Cdd:COG1136 167 LADEPTGNLDSKTGEEvleLLRELNREL--GTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
622-814 |
5.47e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 99.40 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG-----------SIAYVSQtswiqSG------TI 683
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPD-SGRILLDGrdvtglppekrNVGMVFQ-----DYalfphlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 684 RDNILYGkpMESRRYNAA-IKAC---ALDK-DMNGFGHgdlTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSA 758
Cdd:COG3842 95 AENVAFG--LRMRGVPKAeIRARvaeLLELvGLEGLAD---RYPHQ----LSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 759 VDAHTAGVLfhkcvEDSLKE------KTVILVTH-QVEFLSEVDQILVMEEGTITQSGKYEEL 814
Cdd:COG3842 166 LDAKLREEM-----REELRRlqrelgITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
624-815 |
8.00e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.98 E-value: 8.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 624 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVkvfgSIAYVSQT---------SWI-QSG------TIRDNI 687
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI----LWNGQDLTalppaerpvSMLfQENnlfphlTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 LYG-KPmeSRRYNAAIKA---CALDKdmngFGhgdLTEIGQR--GInLSGGQKQRIQLARAVYADADVYLLDDPFSAVD- 760
Cdd:COG3840 93 GLGlRP--GLKLTAEQRAqveQALER----VG---LAGLLDRlpGQ-LSGGQRQRVALARCLVRKRPILLLDEPFSALDp 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 761 AHTAGVLfhKCVEDSLKEK--TVILVTHQVE-FLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:COG3840 163 ALRQEML--DLVDELCRERglTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
618-815 |
1.17e-21 |
|
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: 95.34 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG----------------SIAYVSQT-SWIQ 679
Cdd:cd03258 17 KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPT-SGSVLVDGtdltllsgkelrkarrRIGMIFQHfNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 680 SGTIRDNILYgkPMESRRYNAAIKACALDKDMNGFGHGDLTEIgqRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAV 759
Cdd:cd03258 96 SRTVFENVAL--PLEIAGVPKAEIEERVLELLELVGLEDKADA--YPAQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 760 D-AHTAGVLfhkcveDSLKEK------TVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:cd03258 172 DpETTQSIL------ALLRDInrelglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1222-1428 |
1.22e-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: 94.91 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1222 HLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGidiskiglKDLRMKLSII 1301
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPLEKERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1302 ---PQE-------PTLFRGCIRTNLDP----LGVYSDDEIWKALEKcqLKTT-ISNLPNKLDSSVSdeGenwsvGQRQLF 1366
Cdd:cd03235 71 gyvPQRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADKAKVDEA--LERVgLSELADRQIGELS--G-----GQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 1367 CLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFAD-CTVITVAHRVPTVIDS-DMVMVL 1428
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYfDRVLLL 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
618-827 |
1.25e-21 |
|
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: 95.64 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQ---TS----W 677
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrVQMVFQdpyASlhprH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 678 iqsgTIRDNI-----LYGKPMESRRYNAAIKACALDKD-MNGFGHgdlteigQrginLSGGQKQRIQLARAVYADADVYL 751
Cdd:COG1124 97 ----TVDRILaeplrIHGLPDREERIAELLEQVGLPPSfLDRYPH-------Q----LSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 752 LDDPFSAVDAHT-AGV--LFHKcvedsLKEK---TVILVTHQ---VEFLSevDQILVMEEGTITQSGKYEELLMMGT--A 820
Cdd:COG1124 162 LDEPTSALDVSVqAEIlnLLKD-----LREErglTYLFVSHDlavVAHLC--DRVAVMQNGRIVEELTVADLLAGPKhpY 234
|
....*..
gi 1063712898 821 FQQLVNA 827
Cdd:COG1124 235 TRELLAA 241
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
622-815 |
1.71e-21 |
|
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: 95.10 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-----------IAYVSQT-SWIQSGTIRDNILY 689
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 690 GkpMESRRYN-AAIKACALD-KDMNGFGHgdltEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVL 767
Cdd:cd03299 95 G--LKKRKVDkKEIERKVLEiAEMLGIDH----LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 768 FH--KCVEDSLkEKTVILVTH-QVEFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:cd03299 169 REelKKIRKEF-GVTVLHVTHdFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
620-804 |
2.54e-21 |
|
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: 91.74 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--SIAYVSQtswiqsgtirdnilygkpmesrr 697
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ----------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 698 ynaaikacaldkdmngfghgdlteigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLfhkcvEDSLK 777
Cdd:cd03221 71 -------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL-----EEALK 114
|
170 180 190
....*....|....*....|....*....|
gi 1063712898 778 E--KTVILVTHQVEFLSEV-DQILVMEEGT 804
Cdd:cd03221 115 EypGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1221-1414 |
3.56e-21 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 92.08 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGlKDLRMKLSI 1300
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLFRgcirtNLdplgvysddeiwkalekcqlkTTISNLpnKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILV 1380
Cdd:cd03230 78 LPEEPSLYE-----NL---------------------TVRENL--KL-----------SGGMKQRLALAQALLHDPELLI 118
|
170 180 190
....*....|....*....|....*....|....*
gi 1063712898 1381 LDEATASIDSATDAIIQRIIREEFAD-CTVITVAH 1414
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEgKTILLSSH 153
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1221-1431 |
3.89e-21 |
|
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: 92.25 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG--LKDLRMKL 1298
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPTLFRGcirtnldplgvysddeiwkalekcqlKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKI 1378
Cdd:cd03229 79 GMVFQDFALFPH--------------------------LTVLENIALGL-----------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 1379 LVLDEATASIDSATDAIIQRIIREEFAD--CTVITVAHRVPTVID-SDMVMVLSFG 1431
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
622-814 |
7.01e-21 |
|
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: 93.40 E-value: 7.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGsiayVSQTSWI---------QSGTI--------R 684
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDG----TDINKLKgkalrqlrrQIGMIfqqfnlieR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 ----DNILYG--------KPMESRRYNAAIKAC--ALDK-DMNGFGHgdlteigQRGINLSGGQKQRIQLARAVYADADV 749
Cdd:cd03256 93 lsvlENVLSGrlgrrstwRSLFGLFPKEEKQRAlaALERvGLLDKAY-------QRADQLSGGQQQRVAIARALMQQPKL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 750 YLLDDPFSAVDAHTA----GVLFHKCVEdslKEKTVILVTHQVEF-LSEVDQILVMEEGTITQSGKYEEL 814
Cdd:cd03256 166 ILADEPVASLDPASSrqvmDLLKRINRE---EGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1221-1446 |
9.57e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 93.23 E-value: 9.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKiglkdLRMKLSI 1300
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQeptlfrgciRTNLDP-----------LGVYSD------------DEIWKALEKCQL----KTTISNLpnkldssvsd 1353
Cdd:COG1121 80 VPQ---------RAEVDWdfpitvrdvvlMGRYGRrglfrrpsradrEAVDEALERVGLedlaDRPIGEL---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1354 egenwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFA-DCTVITVAHRVPTVID-SDMVMVLSfG 1431
Cdd:COG1121 141 -----SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREyFDRVLLLN-R 214
|
250
....*....|....*
gi 1063712898 1432 DLVEYNEPSKLMETD 1446
Cdd:COG1121 215 GLVAHGPPEEVLTPE 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
618-815 |
1.20e-20 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 92.11 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQTSWIQSG-T 682
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 683 IRDNILYGkpmESRRYNAAIKAcALDK--DMngFghGDLTEI-GQRGINLSGGQKQRIQLARAVYADADVYLLDDPfsav 759
Cdd:cd03224 92 VEENLLLG---AYARRRAKRKA-RLERvyEL--F--PRLKERrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP---- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 760 dahTAGvLFHKCVED------SLKEK--TVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:cd03224 160 ---SEG-LAPKIVEEifeairELRDEgvTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
622-805 |
1.59e-20 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 91.44 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFGSIAYVSQTSWI----------QS------GTIR 684
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLlEEPD-SGTIIIDGLKLTDDKKNINelrqkvgmvfQQfnlfphLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 DNILYGkPMESRRYN-AAIKACALDKdmngfghgdLTEIG------QRGINLSGGQKQRIQLARAVYADADVYLLDDPFS 757
Cdd:cd03262 95 ENITLA-PIKVKGMSkAEAEERALEL---------LEKVGladkadAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 758 AVDAHTAG-VLfhKCVEDSLKEK-TVILVTHQVEFLSEV-DQILVMEEGTI 805
Cdd:cd03262 165 ALDPELVGeVL--DVMKDLAEEGmTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
622-809 |
3.27e-20 |
|
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: 90.82 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIK---HGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-----------------IAYVSQT-SWIQS 680
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQyALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 681 GTIRDNILYGKPmesRRYNAAIKACAlDKDMNGFGhgdLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAV 759
Cdd:cd03297 90 LNVRENLAFGLK---RKRNREDRISV-DELLDLLG---LDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 760 DAHTAGVLfHKCVEDSLKE--KTVILVTHQvefLSEV----DQILVMEEGTITQSG 809
Cdd:cd03297 163 DRALRLQL-LPELKQIKKNlnIPVIFVTHD---LSEAeylaDRIVVMEDGRLQYIG 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
617-814 |
3.42e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.00 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 617 TKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-----------IAYVSQT-SWIQSGTIR 684
Cdd:PRK10851 15 TQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 DNILYGKPMESRRYN---AAIKAcaldKDMNGFGHGDLTEIGQR-GINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 760
Cdd:PRK10851 93 DNIAFGLTVLPRRERpnaAAIKA----KVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 761 AHTAGVL--FHKCVEDSLKeKTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEEL 814
Cdd:PRK10851 169 AQVRKELrrWLRQLHEELK-FTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQV 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1221-1455 |
4.56e-20 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 90.89 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKiGLKDLRMKLSI 1300
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLFRG-CIRTNLDPLGVY-------SDDEIWKALEKCqlkttisNLPNKLDSSVSdegeNWSVGQRQLFCLGRVL 1372
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFARLyglprkeARERIDELLELF-------GLTDAADRKVG----TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1373 LKRNKILVLDEATASIDSATDAIIQRIIREEFAD-CTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMET--DSY 1448
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARllEDV 226
|
....*..
gi 1063712898 1449 FSKLVAE 1455
Cdd:COG1131 227 FLELTGE 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
620-809 |
5.04e-20 |
|
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: 90.16 E-value: 5.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDN 686
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 I-LYGKPMESRRYNAaikacaldkdmngfghgdlTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTaG 765
Cdd:cd03369 102 LdPFDEYSDEEIYGA-------------------LRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-D 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063712898 766 VLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSG 809
Cdd:cd03369 162 ALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1220-1426 |
5.31e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.03 E-value: 5.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1220 TIHLQELKIRYRPNAPL---VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIS--KIGLKDL 1294
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1295 RMKLSIIPQEP--TLFRGCIRTNLD--P--LGVySDDEIWKALEKCqLKTTISNLPNKLDSSVSDegenWSVGQRQLFCL 1368
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIEKDIAfgPinLGL-SEEEIENRVKRA-MNIVGLDYEDYKDKSPFE----LSGGQKRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 1369 GRVLLKRNKILVLDEATASID-SATDAIIQRI--IREEFaDCTVITVAHR---VPTVIDSDMVM 1426
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDpKGRDEILNKIkeLHKEY-NMTIILVSHSmedVAKLADRIIVM 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
622-815 |
5.61e-20 |
|
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: 90.81 E-value: 5.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWI----------QSG------TIR 684
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYelrrrigmlfQGGalfdslTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 DNILYgkPM-ESRRYNAA-IKACALDKdmngfghgdLTEIGQRGIN------LSGGQKQRIQLARAVYADADVYLLDDPF 756
Cdd:COG1127 101 ENVAF--PLrEHTDLSEAeIRELVLEK---------LELVGLPGAAdkmpseLSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 757 SAVDAHTAGVlFHKCVEDsLKEK---TVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:COG1127 170 AGLDPITSAV-IDELIRE-LRDElglTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELL 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
622-813 |
6.08e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 6.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVfGS---IAYVSQTswiQSG-----TIRDNILYGKP- 692
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQH---QEEldpdkTVLDELRDGAPg 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 693 ---MESRRYnaaikacaldkdMNGFG-HGD--LTEIGqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGV 766
Cdd:COG0488 407 gteQEVRGY------------LGRFLfSGDdaFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 767 LfhkcvEDSLK--EKTVILVTHQVEFLSEV-DQILVMEEGTITQ-SGKYEE 813
Cdd:COG0488 471 L-----EEALDdfPGTVLLVSHDRYFLDRVaTRILEFEDGGVREyPGGYDD 516
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
618-809 |
9.05e-20 |
|
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: 89.24 E-value: 9.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------SIAYVSQT-SWIQSGTIRD 685
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 686 NILYgkPMESRRY-NAAIKACALD-KDMNGFGHgdltEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH- 762
Cdd:cd03301 92 NIAF--GLKLRKVpKDEIDERVREvAELLQIEH----LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKl 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 763 -----TAGVLFHKCVedslkEKTVILVTH-QVEFLSEVDQILVMEEGTITQSG 809
Cdd:cd03301 166 rvqmrAELKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1221-1416 |
1.19e-19 |
|
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: 89.93 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM---K 1297
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1298 LSIIPQEPTL--------------------FRGCirtnldpLGVYSDDEIWKA---LEKCQLKTTISNLPNKLdssvsde 1354
Cdd:cd03256 80 IGMIFQQFNLierlsvlenvlsgrlgrrstWRSL-------FGLFPKEEKQRAlaaLERVGLLDKAYQRADQL------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1355 genwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE---EFADcTVITVAHRV 1416
Cdd:cd03256 146 ----SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinrEEGI-TVIVSLHQV 205
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
622-815 |
1.40e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 89.67 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG--------SIAYVSQtswiQSG----------- 681
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLlEEPD-SGTITVDGedltdskkDINKLRR----KVGmvfqqfnlfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 -TIRDNILYGkPMESRRYN---AAIKACALdkdmngfghgdLTEIG------QRGINLSGGQKQRIQLARAVYADADVYL 751
Cdd:COG1126 92 lTVLENVTLA-PIKVKKMSkaeAEERAMEL-----------LERVGladkadAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 752 LDDPFSAVDAHTAGVlfhkcVEDSLKE-----KTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:COG1126 160 FDEPTSALDPELVGE-----VLDVMRDlakegMTMVVVTHEMGFAREVaDRVVFMDGGRIVEEGPPEEFF 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1221-1436 |
1.41e-19 |
|
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: 89.56 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI---SKIGLKDLR 1295
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1296 MKLSIIPQEPTLFRGciRTNLD----PLgvysddEIWKaLEKCQLKTTISNLPNKLDssVSDEGENW----SVGQRQLFC 1367
Cdd:cd03258 82 RRIGMIFQHFNLLSS--RTVFEnvalPL------EIAG-VPKAEIEERVLELLELVG--LEDKADAYpaqlSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1368 LGRVLLKRNKILVLDEATASIDSA-TDAIIQRI--IREEFaDCTVITVAHRVPTVID-SDMVMVLSFGDLVEY 1436
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPEtTQSILALLrdINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1221-1447 |
1.68e-19 |
|
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: 89.10 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI---SKIGLKDLRMK 1297
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1298 LSIIPQEPTLFrgcirTNLD-------PL---GVYSDDEIWK-ALEKCQ---LKTTISNLPNKLdssvsdegenwSVGQR 1363
Cdd:cd03261 79 MGMLFQSGALF-----DSLTvfenvafPLrehTRLSEEEIREiVLEKLEavgLRGAEDLYPAEL-----------SGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1364 QLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPS 1440
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPE 222
|
....*..
gi 1063712898 1441 KLMETDS 1447
Cdd:cd03261 223 ELRASDD 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1237-1429 |
3.15e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 94.71 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILI-DGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTN 1315
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1316 ----------LDPLGVYS------------------------------------------------DDEIWKALEKCQLK 1337
Cdd:PTZ00265 480 ikyslyslkdLEALSNYYnedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIH 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1338 TTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVIT--VAHR 1415
Cdd:PTZ00265 560 DFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITiiIAHR 639
|
250
....*....|....
gi 1063712898 1416 VPTVIDSDMVMVLS 1429
Cdd:PTZ00265 640 LSTIRYANTIFVLS 653
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1221-1414 |
3.69e-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: 87.93 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAP--LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDL---- 1294
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1295 RMKLSIIPQEPTLFRGciRTNLD----PL------GVYSDDEIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQ 1364
Cdd:cd03255 81 RRHIGFVFQSFNLLPD--LTALEnvelPLllagvpKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 1365 LFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAH 1414
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTH 199
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1221-1414 |
5.65e-19 |
|
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: 87.18 E-value: 5.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKiGLKDLRMKLSI 1300
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLFrgcirTNLDPL----------GVYSDDEIwkalEKCQLKTTISNLPNKLDSSVSDegenWSVGQRQLFCLGR 1370
Cdd:cd03263 80 CPQFDALF-----DELTVRehlrfyarlkGLPKSEIK----EEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063712898 1371 VLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAH 1414
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
622-812 |
7.26e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 7.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--SIAYVSQ-TSWIQSGTIRDNILYGKP----ME 694
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQePPLDDDLTVLDTVLDGDAelraLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 695 SRRYNAAIKACALDKDMNGFG--HGDLTEIG-----QR--------GI----------NLSGGQKQRIQLARAVYADADV 749
Cdd:COG0488 94 AELEELEAKLAEPDEDLERLAelQEEFEALGgweaeARaeeilsglGFpeedldrpvsELSGGWRRRVALARALLSEPDL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 750 YLLDDPFSAVDAHTAGVLfhkcvEDSLK--EKTVILVTHQVEFLSEV-DQILVMEEGTITQ-SGKYE 812
Cdd:COG0488 174 LLLDEPTNHLDLESIEWL-----EEFLKnyPGTVLVVSHDRYFLDRVaTRILELDRGKLTLyPGNYS 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1221-1414 |
7.34e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.02 E-value: 7.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYR--PNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDL---- 1294
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1295 RMKLSIIPQE---------------PTLFRGCIRTNldplgvySDDEIWKALEKCQLKTTISNLPNKLdssvsdegenwS 1359
Cdd:COG1136 85 RRHIGFVFQFfnllpeltalenvalPLLLAGVSRKE-------RRERARELLERVGLGDRLDHRPSQL-----------S 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 1360 VGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE---EFaDCTVITVAH 1414
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnrEL-GTTIVMVTH 203
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
620-814 |
9.19e-19 |
|
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: 86.79 E-value: 9.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------------SIAYVSQTSWIQSG-TIRDN 686
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 I-----LYGKPMESRRYNAA--IKACALDKDMNgfghgdlTEIGqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAV 759
Cdd:cd03263 96 LrfyarLKGLPKSEIKEEVEllLRVLGLTDKAN-------KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 760 DAHTAGVLFhKCVEDSLKEKTVILVTHQ---VEFLSevDQILVMEEGTITQSGKYEEL 814
Cdd:cd03263 165 DPASRRAIW-DLILEVRKGRSIILTTHSmdeAEALC--DRIAIMSDGKLRCIGSPQEL 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
619-842 |
9.22e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.67 E-value: 9.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 619 IPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQ-TSWIQSGTIR 684
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQdTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 DNILYGKPMESRRYNAAIKA--CALDKDMNgfgHGDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:PRK09536 96 QVVEMGRTPHRSRFDTWTETdrAAVERAME---RTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 762 HTAG---VLFHKCVEDSlkeKTVILVTHQVEFLSE-VDQILVMEEGTITQSGKYEELLMMGT---AF--QQLV--NAHND 830
Cdd:PRK09536 173 NHQVrtlELVRRLVDDG---KTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTADTlraAFdaRTAVgtDPATG 249
|
250
....*....|..
gi 1063712898 831 AVTVLPLASNES 842
Cdd:PRK09536 250 APTVTPLPDPDR 261
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
622-816 |
9.24e-19 |
|
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: 88.08 E-value: 9.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWI-----------QS------GTI 683
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqDIAAMSRKELRelrrkkismvfQSfallphRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 684 RDNILYGkpMESR------RYNAAIKACALdKDMNGFGHGDLTEigqrginLSGGQKQRIQLARAVYADADVYLLDDPFS 757
Cdd:cd03294 120 LENVAFG--LEVQgvpraeREERAAEALEL-VGLEGWEHKYPDE-------LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 758 AVDAhtagvLFHKCVEDSL------KEKTVILVTHQV-EFLSEVDQILVMEEGTITQSGKYEELLM 816
Cdd:cd03294 190 ALDP-----LIRREMQDELlrlqaeLQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
622-837 |
1.02e-18 |
|
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: 87.99 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVL------GEIpKVSGTV----------KVFGSIayvSQTSWIQSGTIRD 685
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDI-QIDGVSwnsvplqkwrKAFGVI---PQKVFIFSGTFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 686 NI-LYGKPMESRRYNAAiKACALDKDMNGF-GHGDLTEIgQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHT 763
Cdd:cd03289 96 NLdPYGKWSDEEIWKVA-EEVGLKSVIEQFpGQLDFVLV-DGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 764 AGVLfHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQLVnAHNDAVTVLPL 837
Cdd:cd03289 174 YQVI-RKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI-SPSDRLKLFPR 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
611-815 |
1.09e-18 |
|
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: 91.50 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 611 FGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG----------------SIAYVSQ 674
Cdd:COG1123 270 YPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 675 ---TSWIQSGTIRDNILYG--------KPMESRRYNAAIKACALDKD-MNGFGHGdlteigqrginLSGGQKQRIQLARA 742
Cdd:COG1123 350 dpySSLNPRMTVGDIIAEPlrlhgllsRAERRERVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 743 VYADADVYLLDDPFSAVDAHT-AGVLfhkcveDSLKE------KTVILVTHQ---VEFLSevDQILVMEEGTITQSGKYE 812
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVqAQIL------NLLRDlqrelgLTYLFISHDlavVRYIA--DRVAVMYDGRIVEDGPTE 490
|
...
gi 1063712898 813 ELL 815
Cdd:COG1123 491 EVF 493
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1221-1402 |
1.22e-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: 85.99 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLkDLRMKLSI 1300
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLFRGC-IRTNLD------PLGVySDDEIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLL 1373
Cdd:COG4133 80 LGHADGLKPELtVRENLRfwaalyGLRA-DREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLLL 147
|
170 180
....*....|....*....|....*....
gi 1063712898 1374 KRNKILVLDEATASIDSATDAIIQRIIRE 1402
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1221-1435 |
1.24e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 86.26 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD---LRMK 1297
Cdd:COG2884 2 IRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1298 LSIIPQEPTLFRGciRTNLD----PLGV--YSDDEIWK----ALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFC 1367
Cdd:COG2884 81 IGVVFQDFRLLPD--RTVYEnvalPLRVtgKSRKEIRRrvreVLDLVGLSDKAKALPHEL-----------SGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1368 LGRVLLKRNKILVLDEATASIDSATdaiIQRIIR--EEFAD--CTVITVAHrvptviDSDM-------VMVLSFGDLVE 1435
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPET---SWEIMEllEEINRrgTTVLIATH------DLELvdrmpkrVLELEDGRLVR 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
627-810 |
2.27e-18 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 85.30 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 627 LEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKV-----FGSIAYVSQTSWI-QSG------TIRDNILYGkpme 694
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVndqshTGLAPYQRPVSMLfQENnlfahlTVRQNIGLG---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 695 srrYNAAIKACALDKD-----MNGFGHGDLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD----AHTAG 765
Cdd:TIGR01277 95 ---LHPGLKLNAEQQEkvvdaAQQVGIADYLD--RLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllrEEMLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063712898 766 VLFHKCVEdslKEKTVILVTHQVEFLSEV-DQILVMEEGTITQSGK 810
Cdd:TIGR01277 170 LVKQLCSE---RQRTLLMVTHHLSDARAIaSQIAVVSQGKIKVVSD 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
622-809 |
2.60e-18 |
|
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: 85.28 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQtswIQSG-----TIRDNIlygkpmesr 696
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG---LGGGfnpelTGRENI--------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 697 RYNAAIKACaLDKDMNGFGHG--DLTEIGQRgINL-----SGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAgvlfH 769
Cdd:cd03220 106 YLNGRLLGL-SRKEIDEKIDEiiEFSELGDF-IDLpvktySSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ----E 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063712898 770 KCVE--DSLKE--KTVILVTHQVEFLSEV-DQILVMEEGTITQSG 809
Cdd:cd03220 180 KCQRrlRELLKqgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1221-1444 |
4.04e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 86.22 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1300
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEP------TLFRGCIRTNLDPLGVYSDDEIWK---ALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRV 1371
Cdd:PRK13635 86 VFQNPdnqfvgATVQDDVAFGLENIGVPREEMVERvdqALRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1372 LLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLME 1444
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1221-1434 |
4.88e-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: 85.94 E-value: 4.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG-LKDLRMKLS 1299
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1300 IIPQEPtlfrgcirTN--------------LDPLGVySDDEIWK----ALEKCQLKTTISNLPNKLdssvsdegenwSVG 1361
Cdd:TIGR04520 81 MVFQNP--------DNqfvgatveddvafgLENLGV-PREEMRKrvdeALKLVGMEDFRDREPHLL-----------SGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1362 QRQLFCLGRVLLKRNKILVLDEATASIDSATD----AIIQRIIREEfaDCTVITVAHRVPTVIDSDMVMVLSFGDLV 1434
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRkevlETIRKLNKEE--GITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1221-1446 |
5.56e-18 |
|
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: 85.03 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG---LKDLRMK 1297
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1298 LSIIPQEPTLFrgcirTNLD-------PL---GVYSDDEIWK-ALEKCQ---LKTTISNLPNKLdssvsdegenwSVGQR 1363
Cdd:COG1127 84 IGMLFQGGALF-----DSLTvfenvafPLrehTDLSEAEIRElVLEKLElvgLPGAADKMPSEL-----------SGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1364 QlfclgRVLLKRN-----KILVLDEATASIDSATDAIIQRIIRE---EFaDCTVITVAHRVPTVID-SDMVMVLSFGDLV 1434
Cdd:COG1127 148 K-----RVALARAlaldpEILLYDEPTAGLDPITSAVIDELIRElrdEL-GLTSVVVTHDLDSAFAiADRVAVLADGKII 221
|
250
....*....|..
gi 1063712898 1435 EYNEPSKLMETD 1446
Cdd:COG1127 222 AEGTPEELLASD 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
622-812 |
5.88e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.70 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS----------IAYVSQTS---WIQSGTIRDNIL 688
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 689 ---YGKPMESRRYNAAIKAC---ALDK-DMNGFGHgdlTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:PRK15056 103 mgrYGHMGWLRRAKKRDRQIvtaALARvDMVEFRH---RQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 762 HTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYE 812
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
618-815 |
6.17e-18 |
|
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: 84.65 E-value: 6.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQTSWIQSG-T 682
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 683 IRDNILYGkpMESRRYNAAIKAcaldkdmngfghgDLTEI-----------GQRGINLSGGQKQriQLA--RAVYADADV 749
Cdd:COG0410 95 VEENLLLG--AYARRDRAEVRA-------------DLERVyelfprlkerrRQRAGTLSGGEQQ--MLAigRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 750 YLLDDPfsavdahTAGV-------LFHKCVEdsLKEK--TVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:COG0410 158 LLLDEP-------SLGLapliveeIFEIIRR--LNREgvTILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELL 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1221-1434 |
6.29e-18 |
|
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: 84.17 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNapLVLKGISCTFREGTrVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKdLRMKLSI 1300
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLF-RGCIRTNLDPLGVYS-------DDEIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVL 1372
Cdd:cd03264 77 LPQEFGVYpNFTVREFLDYIAWLKgipskevKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1373 LKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDS-DMVMVLSFGDLV 1434
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLV 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1442 |
7.05e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.67 E-value: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDISKIGLKDLRMKL 1298
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEP--TLFRGCIRTNLDpLGVYS----DDEIWKALEKCQLKTTISNLPNKLDSSVsdegenwSVGQRQLFCLGRVL 1372
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVS-FGAVNlklpEDEVRKRVDNALKRTGIEHLKDKPTHCL-------SFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1373 LKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTV-IDSDMVMVLSFGDLVEYNEPSKL 1442
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1221-1436 |
8.00e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 86.26 E-value: 8.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEP---ASGCILIDGIDISKIG---LK 1292
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1293 DLRMK-LSIIPQEPTlfrgcirTNLDPL--------------GVYSDDEIWK----ALEKCQL---KTTISNLPNKLdss 1350
Cdd:COG0444 82 KIRGReIQMIFQDPM-------TSLNPVmtvgdqiaeplrihGGLSKAEAREraieLLERVGLpdpERRLDRYPHEL--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1351 vsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATasidSATDAIIQRII-------REEFaDCTVITVAHRVPTV--Id 1421
Cdd:COG0444 152 --------SGGMRQRVMIARALALEPKLLIADEPT----TALDVTIQAQIlnllkdlQREL-GLAILFITHDLGVVaeI- 217
|
250
....*....|....*
gi 1063712898 1422 SDMVMVLSFGDLVEY 1436
Cdd:COG0444 218 ADRVAVMYAGRIVEE 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
622-813 |
9.32e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.92 E-value: 9.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTV------------------KVFGSIAYVSQTswiqsgT 682
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfETPD-SGRImldgqdithvpaenrhvnTVFQSYALFPHM------T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 683 IRDNILYGKPMEsRRYNAAIKACALDK-DMNgfghgDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 760
Cdd:PRK09452 103 VFENVAFGLRMQ-KTPAAEITPRVMEAlRMV-----QLEEFAQRKPhQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 761 AHtagvlFHKCVEDSLKEK------TVILVTH-QVEFLSEVDQILVMEEGTITQSGK----YEE 813
Cdd:PRK09452 177 YK-----LRKQMQNELKALqrklgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTpreiYEE 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
622-813 |
1.23e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.98 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIayvsqtSW---IQSG-----TIRDNI-----L 688
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV------SAlleLGAGfhpelTGRENIylngrL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 689 YGkpMESRRYNAAIKACAldkdmngfghgDLTEIGQRgINL-----SGGQKQRIQLARAVYADADVYLLDDPFSAVDAHt 763
Cdd:COG1134 116 LG--LSRKEIDEKFDEIV-----------EFAELGDF-IDQpvktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAA- 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 764 agvlF-HKCVE--DSLKE--KTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEE 813
Cdd:COG1134 181 ----FqKKCLAriRELREsgRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEE 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1221-1435 |
1.57e-17 |
|
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: 82.95 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISkiGLKDLRMKLSI 1300
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLF-----RGCIRTNLDPLGVYSDDEIWKALEKCQLkTTISNLPNKLDSSVSdeGenwsvGQRQLFCLGRVLLKR 1375
Cdd:cd03259 77 VFQDYALFphltvAENIAFGLKLRGVPKAEIRARVRELLEL-VGLEGLLNRYPHELS--G-----GQQQRVALARALARE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1376 NKILVLDEATasidSATDAIIQRIIREEFAD------CTVITVAHrvptviD-------SDMVMVLSFGDLVE 1435
Cdd:cd03259 149 PSLLLLDEPL----SALDAKLREELREELKElqrelgITTIYVTH------DqeealalADRIAVMNEGRIVQ 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
617-810 |
1.84e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.79 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 617 TKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG----------------SIAYVSQTSW-IQ 679
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQDFRlLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 680 SGTIRDNILYgkPME-----SRRYNAAIKAcALDKdmngFGHGDLteIGQRGINLSGGQKQRIQLARAVYADADVYLLDD 754
Cdd:COG2884 93 DRTVYENVAL--PLRvtgksRKEIRRRVRE-VLDL----VGLSDK--AKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 755 PFSAVDAHTAGVLFhkcveDSLKE-----KTVILVTHQVEFLSEVDQ-ILVMEEGTITQSGK 810
Cdd:COG2884 164 PTGNLDPETSWEIM-----ELLEEinrrgTTVLIATHDLELVDRMPKrVLELEDGRLVRDEA 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1237-1435 |
2.22e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.42 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVE-----PASGCILIDGIDISKIGLKDLRMKLSIIPQEP------ 1305
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1306 TLFRG-CIRTNLDPLgVYSDDEIWK----ALEKCQLKTTISnlpNKLDSSVSdegeNWSVGQRQLFCLGRVLLKRNKILV 1380
Cdd:PRK14247 98 SIFENvALGLKLNRL-VKSKKELQErvrwALEKAQLWDEVK---DRLDAPAG----KLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 1381 LDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVID-SDMVMVLSFGDLVE 1435
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVE 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
612-809 |
2.75e-17 |
|
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: 82.70 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 612 GWEPETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPK---VSGTVKVFG----------SIAYVSQTS-W 677
Cdd:cd03234 15 NWNKYARI--LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGqprkpdqfqkCVAYVRQDDiL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 678 IQSGTIRDNILYGKPMESRRY--NAAIKACALDKDMNGFGHGDLTeiGQRGINLSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKssDAIRKKRVEDVLLRDLALTRIG--GNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 756 FSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQ--VEFLSEVDQILVMEEGTITQSG 809
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
595-828 |
2.80e-17 |
|
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: 83.42 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 595 SGLDASGTAVDIQVGNFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------- 667
Cdd:cd03288 11 SGLVGLGGEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 668 ------SIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLAR 741
Cdd:cd03288 90 lhtlrsRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 742 AVYADADVYLLDDPFSAVDAHTAGVLfHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMM-GTA 820
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENIL-QKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGV 248
|
....*...
gi 1063712898 821 FQQLVNAH 828
Cdd:cd03288 249 FASLVRTD 256
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
620-804 |
4.64e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKV--FGSIAYVSQTSWIQSGTIRDNILYgkPMESRR 697
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLY--PATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 698 Y-NAAIKAcALDKdmNGFGH--GDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKcVED 774
Cdd:COG4178 455 FsDAELRE-ALEA--VGLGHlaERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LRE 530
|
170 180 190
....*....|....*....|....*....|
gi 1063712898 775 SLKEKTVILVTHQVEFLSEVDQILVMEEGT 804
Cdd:COG4178 531 ELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
622-806 |
5.26e-17 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 79.78 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGsiayvsqtswiqsgtirdnilygKPMESRRYNAA 701
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------------------KEVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 702 IKAcaldkdmngfghgdlteigqrGIN----LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFhKCVEDsLK 777
Cdd:cd03216 73 RRA---------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF-KVIRR-LR 129
|
170 180 190
....*....|....*....|....*....|....*
gi 1063712898 778 E--KTVILVTHqveFLSEV----DQILVMEEGTIT 806
Cdd:cd03216 130 AqgVAVIFISH---RLDEVfeiaDRVTVLRDGRVV 161
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
622-815 |
6.13e-17 |
|
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: 81.82 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--------------SIAYVSQTSWIQSG-TIRDN 686
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILygKPMESRRYNAAIKACALDKDMNGFGhgdLTEI-GQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAhtag 765
Cdd:cd03218 96 IL--AVLEIRGLSKKEREEKLEELLEEFH---ITHLrKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP---- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 766 vlfhKCVED------SLKEKTV-ILVT-HQV-EFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:cd03218 167 ----IAVQDiqkiikILKDRGIgVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1237-1434 |
8.38e-17 |
|
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: 80.94 E-value: 8.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD-LRMKLSIIPQEPTLFRG-CIRT 1314
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1315 NLDpLGVYsddeiwkALEKCQLKTTISNL----PnKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATA---- 1386
Cdd:cd03224 95 NLL-LGAY-------ARRRAKRKARLERVyelfP-RLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEglap 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063712898 1387 SIDSATDAIIQRIIREEFadcTVITVAHRVPTVID-SDMVMVLSFGDLV 1434
Cdd:cd03224 166 KIVEEIFEAIRELRDEGV---TILLVEQNARFALEiADRAYVLERGRVV 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
620-800 |
9.58e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.83 E-value: 9.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSI--------AYVSQTS----WIqsgTIRDNI 687
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKDallpWL---NVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 -----LYGKPMESRRynaAIKACALDKdmngfghGDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:COG4525 98 afglrLRGVPKAERR---ARAEELLAL-------VGLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 762 HTagvlfhkcvEDSLKE----------KTVILVTHQVE---FLSEvdQILVM 800
Cdd:COG4525 168 LT---------REQMQEllldvwqrtgKGVFLITHSVEealFLAT--RLVVM 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
620-789 |
1.04e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.67 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSI--------AYVSQTS----WIqsgTIRDNI 687
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNEgllpWR---NVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 -----LYGKPMESRRYNAaikacaldKDMngFGHGDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:PRK11248 92 afglqLAGVEKMQRLEIA--------HQM--LKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190
....*....|....*....|....*....|.
gi 1063712898 762 HT---AGVLFHKCVEDSLKEktVILVTHQVE 789
Cdd:PRK11248 162 FTreqMQTLLLKLWQETGKQ--VLLITHDIE 190
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1237-1445 |
1.19e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.63 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVE------PASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRG 1310
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1311 C-----IRTNLDPLGVYSDDEIWKALEKCQLKTTI-SNLPNKLDSSVSdegeNWSVGQRQLFCLGRVLLKRNKILVLDEA 1384
Cdd:PRK14246 105 LsiydnIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPAS----QLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 1385 TASIDSATDAIIQRIIREEFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMET 1445
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
624-814 |
1.23e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 83.23 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 624 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPkVSGTV------------------KVFGSIAYVSQTSwiqsgtIR 684
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKP-TEGQIfidgedvthrsiqqrdicMVFQSYALFPHMS------LG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 DNILYGKPMESRRyNAAIK-----ACALdKDMNGFGHGDLTEIgqrginlSGGQKQRIQLARAVYADADVYLLDDPFSAV 759
Cdd:PRK11432 97 ENVGYGLKMLGVP-KEERKqrvkeALEL-VDLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 760 DAHtagvlfhkcVEDSLKEK----------TVILVTH-QVEFLSEVDQILVMEEGTITQSGKYEEL 814
Cdd:PRK11432 168 DAN---------LRRSMREKirelqqqfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1221-1414 |
1.35e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.57 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYrPNAPLvlkGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGlKDLRmKLSI 1300
Cdd:COG3840 2 LRLDDLTYRY-GDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-PAER-PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLFRG-CIRTN----LDPLGVYSDDE---IWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVL 1372
Cdd:COG3840 76 LFQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARCL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063712898 1373 LKRNKILVLDEATASIDSATDA----IIQRIIREEFAdcTVITVAH 1414
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQemldLVDELCRERGL--TVLMVTH 188
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
622-814 |
1.47e-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: 80.74 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSI-----AYVSQTSWI-QSG------TIRDNILY 689
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpPHKRPVNTVfQNYalfphlTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 690 GKPMEsRRYNAAIK---ACALDK-DMNGFGHGDLTEigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAhtag 765
Cdd:cd03300 96 GLRLK-KLPKAEIKervAEALDLvQLEGYANRKPSQ-------LSGGQQQRVAIARALVNEPKVLLLDEPLGALDL---- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 766 vlfhKCVEDSLKE---------KTVILVTH-QVEFLSEVDQILVMEEGTITQSGKYEEL 814
Cdd:cd03300 164 ----KLRKDMQLElkrlqkelgITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1181-1456 |
1.54e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 86.15 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1181 TLSNSIISVERIKQYMNIPE-EPPAIidDKRPPSSWPSNgTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGS 1259
Cdd:TIGR00957 599 SIVQASVSLKRLRIFLSHEElEPDSI--ERRTIKPGEGN-SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGC 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1260 GKSTLISALFRLVEPASGCILIDGidiskiglkdlrmKLSIIPQEPTLFRGCIRTNLdPLGVYSDDEIWKA-LEKCQLKT 1338
Cdd:TIGR00957 676 GKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENI-LFGKALNEKYYQQvLEACALLP 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1339 TISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDS-ATDAIIQRIIREE--FADCTVITVAHR 1415
Cdd:TIGR00957 742 DLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPEgvLKNKTRILVTHG 821
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1063712898 1416 VPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLVAEY 1456
Cdd:TIGR00957 822 ISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTY 862
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1221-1426 |
1.60e-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: 80.10 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLkDLRMKL 1298
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPTLF-RGCIRTNLDPLG-VYsddeiwkALEKCQLKTTISNLPNKLD--SSVSDEGENWSVGQRQLFCLGRVLLK 1374
Cdd:cd03266 81 GFVSDSTGLYdRLTARENLEYFAgLY-------GLKGDELTARLEELADRLGmeELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 1375 RNKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHR---VPTVIDSDMVM 1426
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHImqeVERLCDRVVVL 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
622-815 |
1.71e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 80.95 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-LGEIPKvSGTVKVF-----GSIAYVSQTSWI-----QSG--------- 681
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQPE-AGTIRVGditidTARSLSQQKGLIrqlrqHVGfvfqnfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 ---TIRDNILYGKPMESRRYNAAikACALDKDMngfghgdLTEIGQRGIN------LSGGQKQRIQLARAVYADADVYLL 752
Cdd:PRK11264 98 phrTVLENIIEGPVIVKGEPKEE--ATARAREL-------LAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 753 DDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALF 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
636-815 |
1.89e-16 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 82.84 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 636 AVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------------SIAYVSQtswiQSG-----TIRDNILYGkpm 693
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQ----EARlfphlSVRGNLLYG--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 694 eSRRYNAAIKACALDK--DMNGFGHgdLteIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTagvlfhKC 771
Cdd:COG4148 102 -RKRAPRAERRISFDEvvELLGIGH--L--LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR------KA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 772 vE-----DSLKEKT---VILVTHQVEflsEV----DQILVMEEGTITQSGKYEELL 815
Cdd:COG4148 171 -EilpylERLRDELdipILYVSHSLD---EVarlaDHVVLLEQGRVVASGPLAEVL 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
620-802 |
2.48e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.45 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIP---KVSGTVKVFGS-----------IAYVSQTS-----Wiqs 680
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRrltalpaeqrrIGILFQDDllfphL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 681 gTIRDNILYGKPMESRRYN--AAIKAcALDK-DMNGFGHGDLTEigqrginLSGGQKQRIQLARAVYADADVYLLDDPFS 757
Cdd:COG4136 92 -SVGENLAFALPPTIGRAQrrARVEQ-ALEEaGLAGFADRDPAT-------LSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063712898 758 AVDAHTAgVLFHKCVEDSLKEKT--VILVTHQVEFLSEVDQILVMEE 802
Cdd:COG4136 163 KLDAALR-AQFREFVFEQIRQRGipALLVTHDEEDAPAAGRVLDLGN 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
622-815 |
2.57e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.94 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQ---------------SGTIRDN 686
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRskvglvfqdpddqvfSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILYG------KPME-SRRYNAAIKACaldkDMNGFGHgdlteigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAV 759
Cdd:PRK13647 101 VAFGpvnmglDKDEvERRVEEALKAV----RMWDFRD-------KPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 760 DAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSE-VDQILVMEEG-TITQSGKyeELL 815
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGrVLAEGDK--SLL 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
622-801 |
2.60e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.96 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--IAYVSQTSWIQSGTIRDNILYgkpmesrryn 699
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGedLLFLPQRPYLPLGTLREQLIY---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 700 aaikacALDKdmngfghgdlteigqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLkek 779
Cdd:cd03223 87 ------PWDD------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI--- 139
|
170 180
....*....|....*....|..
gi 1063712898 780 TVILVTHQVEFLSEVDQILVME 801
Cdd:cd03223 140 TVISVGHRPSLWKFHDRVLDLD 161
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
615-824 |
3.07e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.83 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 615 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGsIAYVSQTSW---------IQS----- 680
Cdd:PRK13635 16 PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrrqvgmvFQNpdnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 681 --GTIRDNILY-----GKPMES--RRYNAAIKACaldkDMNGFGHgdlteigQRGINLSGGQKQRIQLARAVYADADVYL 751
Cdd:PRK13635 95 vgATVQDDVAFgleniGVPREEmvERVDQALRQV----GMEDFLN-------REPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 752 LDDPFSAVD-AHTAGVLfhKCVEDsLKEK---TVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGTAFQQL 824
Cdd:PRK13635 164 LDEATSMLDpRGRREVL--ETVRQ-LKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHMLQEI 237
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
599-815 |
4.20e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.61 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 599 ASGTaVDIQVGNFGWEPETkiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG----------- 667
Cdd:PRK10790 337 QSGR-IDIDNVSFAYRDDN--LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvl 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 668 --SIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYA 745
Cdd:PRK10790 414 rqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 746 DADVYLLDDPFSAVDAHTagvlfHKCVEDSL----KEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:PRK10790 494 TPQILILDEATANIDSGT-----EQAIQQALaavrEHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1218-1445 |
4.22e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.52 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1218 NGTIHLQELKIRYRPNAPL-VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM 1296
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1297 KLSIIPQEP-TLFRGCIRTNLDPLGVYSD----DEIWKALEKCQLKTTISNLPNKldssvsdEGENWSVGQRQLFCLGRV 1371
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLAVNMLDFKTR-------EPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 1372 LLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMET 1445
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEikEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFAT 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1230-1451 |
4.33e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.64 E-value: 4.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1230 YRPNAPLVLKG---ISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI----SKIGLKDLRMKLSIIP 1302
Cdd:PRK13641 12 YSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1303 Q--EPTLFRGCIRTNLD--PLGV-YSDDE----IWKALEKCQLKTT-ISNLPNKLdssvsdegenwSVGQRQLFCLGRVL 1372
Cdd:PRK13641 92 QfpEAQLFENTVLKDVEfgPKNFgFSEDEakekALKWLKKVGLSEDlISKSPFEL-----------SGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1373 LKRNKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMETDSYFS 1450
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKEWLK 240
|
.
gi 1063712898 1451 K 1451
Cdd:PRK13641 241 K 241
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
622-809 |
5.96e-16 |
|
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: 78.39 E-value: 5.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQkVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS------------IAYVSQT-SWIQSGTIRDNIL 688
Cdd:cd03264 16 LDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQEfGVYPNFTVREFLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 689 YG---KPMESRRYNAAIkaCALDKDMNGFGHGDlTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPfsavdahTAG 765
Cdd:cd03264 95 YIawlKGIPSKEVKARV--DEVLELVNLGDRAK-KKIGS----LSGGMRRRVGIAQALVGDPSILIVDEP-------TAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 766 ------VLFHKCVEDSLKEKTVILVTHQVEFLSEV-DQILVMEEGTITQSG 809
Cdd:cd03264 161 ldpeerIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
622-803 |
7.80e-16 |
|
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: 77.71 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS---------IAYVSQTSWI-QSGTIRDNILY-- 689
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEERGLyPKMKVIDQLVYla 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 690 ---G-KPMESRRynaaikacALDKDMNGFGHGDLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAG 765
Cdd:cd03269 96 qlkGlKKEEARR--------RIDEWLERLELSEYAN--KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063712898 766 VLFHKCVEDSLKEKTVILVTHQVEFLSEV-DQILVMEEG 803
Cdd:cd03269 166 LLKDVIRELARAGKTVILSTHQMELVEELcDRVLLLNKG 204
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
615-824 |
8.91e-16 |
|
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: 79.01 E-value: 8.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 615 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSL---LHAVLgeIPKvSGTVKVFGSIAYVSQTSW-------------- 677
Cdd:TIGR04520 11 PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLL--LPT-SGKVTVDGLDTLDEENLWeirkkvgmvfqnpd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 678 --IQSGTIRDNILYGkpMES---------RRYNAAIKACaldkDMNGFGHgdlteigQRGINLSGGQKQRIQLARAVYAD 746
Cdd:TIGR04520 88 nqFVGATVEDDVAFG--LENlgvpreemrKRVDEALKLV----GMEDFRD-------REPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 747 ADVYLLDDPFSAVDAhtagvlfhKCVED------SLKE---KTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMM 817
Cdd:TIGR04520 155 PDIIILDEATSMLDP--------KGRKEvletirKLNKeegITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQ 226
|
....*..
gi 1063712898 818 GTAFQQL 824
Cdd:TIGR04520 227 VELLKEI 233
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
622-805 |
9.28e-16 |
|
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: 76.70 E-value: 9.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVkvfgsiayvsqtswiqsgtirdnILYGKPMESRRYNAA 701
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEI-----------------------TLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 702 IKAcaldkdmnGFGHgdLTE-------IGQRGIN--------LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGV 766
Cdd:cd03215 73 IRA--------GIAY--VPEdrkreglVLDLSVAenialsslLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063712898 767 LFHKCVEDSLKEKTVILVTHQV-EFLSEVDQILVMEEGTI 805
Cdd:cd03215 143 IYRLIRELADAGKAVLLISSELdELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1221-1443 |
9.48e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 9.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG-LKDLRMKLS 1299
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1300 IIPQEP-TLFRGciRTNLDPLGVYSDD------EIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVL 1372
Cdd:PRK13644 81 IVFQNPeTQFVG--RTVEEDLAFGPENlclppiEIRKRVDRALAEIGLEKYRHRSPKTLSG-------GQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 1373 LKRNKILVLDEATASID-SATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLM 1443
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDpDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1221-1389 |
9.68e-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: 77.57 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI--SKIGLKDLRMKL 1298
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPTLFRGciRTNLD-----PLGVY--SDDEI----WKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFC 1367
Cdd:cd03262 79 GMVFQQFNLFPH--LTVLEnitlaPIKVKgmSKAEAeeraLELLEKVGLADKADAYPAQL-----------SGGQQQRVA 145
|
170 180
....*....|....*....|..
gi 1063712898 1368 LGRVLLKRNKILVLDEATASID 1389
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALD 167
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
622-814 |
1.10e-15 |
|
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: 77.89 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS---------IAYVSQTSWIQSGTIRDNILYGKP 692
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqitepgpdrMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 693 MESRRYNAAIKACALDK--DMNGFGHGDLTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVL--- 767
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEhiALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLqee 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 768 FHKCVEDSlkEKTVILVTHQVE---FLSevDQILVMEEGTITQSGKYEEL 814
Cdd:TIGR01184 157 LMQIWEEH--RVTVLMVTHDVDealLLS--DRVVMLTNGPAANIGQILEV 202
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
623-814 |
1.57e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.07 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 623 RNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG--EI----------------PKVSGTVKVFGSIAYVSQTSwiqsgtIR 684
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleDItsgdlfigekrmndvpPAERGVGMVFQSYALYPHLS------VA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 DNILYG-------KPMESRRYNAAIKACALDKdmngfghgdLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFS 757
Cdd:PRK11000 94 ENMSFGlklagakKEEINQRVNQVAEVLQLAH---------LLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 758 AVDahtAGVLFHKCVEDSLKEK----TVILVTH-QVEFLSEVDQILVMEEGTITQSGKYEEL 814
Cdd:PRK11000 163 NLD---AALRVQMRIEISRLHKrlgrTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
622-815 |
1.92e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 79.35 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-LGEIPkVSGTVKVFG----------------SIAYVSQT-SWIQSGTI 683
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInLLERP-TSGSVLVDGvdltalserelraarrKIGMIFQHfNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 684 RDNILYgkPMESRRYNAAikacaldkdmngfghgdltEIGQR--------GI---------NLSGGQKQRIQLARAVYAD 746
Cdd:COG1135 100 AENVAL--PLEIAGVPKA-------------------EIRKRvaellelvGLsdkadaypsQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 747 ADVYLLDDPFSAVDAH-TAGVLfhkcveDSLKE------KTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:COG1135 159 PKVLLCDEATSALDPEtTRSIL------DLLKDinrelgLTIVLITHEMDVVRRIcDRVAVLENGRIVEQGPVLDVF 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1220-1443 |
2.27e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1220 TIHLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLS 1299
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1300 IIPQEPTLFRGCIRTNLDPLG----------VYSDDE--IWKALEkcqlKTTISNLPNKLDSSVSDegenwsvGQRQLFC 1367
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGrspwlslwgrLSAEDNarVNQAME----QTRINHLADRRLTDLSG-------GQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1368 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHrvptviD-------SDMVMVLSFGDLVEYNEP 1439
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRElNTQGKTVVTVLH------DlnqasryCDHLVVLANGHVMAQGTP 222
|
....
gi 1063712898 1440 SKLM 1443
Cdd:PRK11231 223 EEVM 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1221-1443 |
3.17e-15 |
|
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: 76.96 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVlKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1300
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLFRGciRTNLDPLGVYSDDEIWKaleKCQLKTTISNL-------PNKLDSSVSDEgenWSVGQRQLFCLGRVLL 1373
Cdd:cd03295 80 VIQQIGLFPH--MTVEENIALVPKLLKWP---KEKIRERADELlalvgldPAEFADRYPHE---LSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1374 KRNKILVLDEATasidSATDAIIQRIIREEFADC------TVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLM 1443
Cdd:cd03295 152 ADPPLLLMDEPF----GALDPITRDQLQEEFKRLqqelgkTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEIL 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1237-1389 |
4.04e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTL---FRGCI- 1312
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVRQv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1313 --------RTNLDPLGvySDDEiwKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLDEA 1384
Cdd:PRK09536 98 vemgrtphRSRFDTWT--ETDR--AAVERAMERTGVAQFADRPVTSLSG-------GERQRVLLARALAQATPVLLLDEP 166
|
....*
gi 1063712898 1385 TASID 1389
Cdd:PRK09536 167 TASLD 171
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1242-1416 |
5.03e-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: 75.61 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1242 SCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISkiGLKDLRMKLSIIPQEPTLFRG-CIRTNLDpLG 1320
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVG-LG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1321 VYS----DDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAII 1396
Cdd:cd03298 95 LSPglklTAEDRQAIEVALARVGLAGLEKRLPGELSG-------GERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180
....*....|....*....|..
gi 1063712898 1397 QRIIREEFAD--CTVITVAHRV 1416
Cdd:cd03298 168 LDLVLDLHAEtkMTVLMVTHQP 189
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
622-813 |
5.11e-15 |
|
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: 76.32 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQTSWI-QSGTIRDN 686
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLfPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIG------QRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 760
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREARERAEELLERVGladladRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 761 ----AHTAGVLfhkcveDSLKEK--TVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEE 813
Cdd:cd03219 176 peetEELAELI------RELRERgiTVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
615-815 |
5.30e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.95 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 615 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQS-------------- 680
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKkigiifqnpdnqfi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 681 -GTIRDNILYGkpMESRRYN-----AAIKACALDKDMNGFghgdlteIGQRGINLSGGQKQRIQLARAVYADADVYLLDD 754
Cdd:PRK13632 98 gATVEDDIAFG--LENKKVPpkkmkDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 755 PFSAVDA---HTAGVLFHKCVEDslKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:PRK13632 169 STSMLDPkgkREIKKIMVDLRKT--RKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
622-809 |
6.35e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.21 E-value: 6.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-LGEIPKvSGTVKVFGSIAYVSQTSWIQSG-TIRDNIlygkPMESRRYN 699
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNHFDFSKTPSDKAIrELRRNV----GMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 700 -------------AAIKACALDKD------MNGFGHGDLTEIGQR-GINLSGGQKQRIQLARAVYADADVYLLDDPFSAV 759
Cdd:PRK11124 93 lwphltvqqnlieAPCRVLGLSKDqalaraEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 760 DAH-TAGVLfhkcveDSLKEK-----TVILVTHQVEFLSEV-DQILVMEEGTITQSG 809
Cdd:PRK11124 173 DPEiTAQIV------SIIRELaetgiTQVIVTHEVEVARKTaSRVVYMENGHIVEQG 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
618-815 |
6.37e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.90 E-value: 6.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV--LGEIPK----VSGtVKVFGSIAYVSQTSwIQSG---------- 681
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSgdliVDG-LKVNDPKVDERLIR-QEAGmvfqqfylfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 --TIRDNILYGkPMESRRynaAIKACALDKDMNGFGHGDLTE-IGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSA 758
Cdd:PRK09493 91 hlTALENVMFG-PLRVRG---ASKEEAEKQARELLAKVGLAErAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 759 VDAHtagvLFHKC--VEDSLKEK--TVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:PRK09493 167 LDPE----LRHEVlkVMQDLAEEgmTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
627-809 |
6.45e-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: 75.22 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 627 LEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG-----------SIAYVSQTSWIQSG-TIRDNILYGKpM 693
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQ-SGRVLINGvdvtaappadrPVSMLFQENNLFAHlTVEQNVGLGL-S 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 694 ESRRYNA----AIKACALDKDMNGFghgDLTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVD-AHTAGVLf 768
Cdd:cd03298 97 PGLKLTAedrqAIEVALARVGLAGL---EKRLPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDpALRAEML- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063712898 769 hKCVEDSLKEK--TVILVTHQVEFLSEVDQILV-MEEGTITQSG 809
Cdd:cd03298 169 -DLVLDLHAETkmTVLMVTHQPEDAKRLAQRVVfLDNGRIAAQG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
622-836 |
6.53e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 6.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQ-SGTIRDNI 687
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLSfPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 LYGK-PM-ESRRYNAAIKACALDK-DMNGFGHGDLTEigqrginLSGGQKQRIQLARA---VYADAD---VYLLDDPFSA 758
Cdd:PRK13548 98 AMGRaPHgLSRAEDDALVAAALAQvDLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqLWEPDGpprWLLLDEPTSA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 759 VD-AH---TAGVLFHKCVEDSLkekTVILVTHQVEFLSE-VDQILVMEEGTITQSGKYEELL---MMGTAFQQ--LVNAH 828
Cdd:PRK13548 171 LDlAHqhhVLRLARQLAHERGL---AVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEVLtpeTLRRVYGAdvLVQPH 247
|
250
....*....|
gi 1063712898 829 --NDAVTVLP 836
Cdd:PRK13548 248 peTGAPLVLP 257
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1218-1444 |
7.96e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.03 E-value: 7.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1218 NGTIHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVE-----PASGCILIDGIDI--SKIG 1290
Cdd:PRK14267 2 KFAIETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1291 LKDLRMKLSIIPQEPTLF-------RGCIRTNLDPLgVYSDDEIWKALEKCQLKTTisnLPNKLDSSVSDEGENWSVGQR 1363
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFphltiydNVAIGVKLNGL-VKSKKELDERVEWALKKAA---LWDEVKDRLNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1364 QLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAH------RVptvidSDMVMVLSFGDLVEYN 1437
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaqaaRV-----SDYVAFLYLGKLIEVG 230
|
....*..
gi 1063712898 1438 EPSKLME 1444
Cdd:PRK14267 231 PTRKVFE 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1225-1442 |
9.30e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.20 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1225 ELKIRYRpNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDISKIGLKDLRMKLSIIP 1302
Cdd:PRK13638 6 DLWFRYQ-DEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1303 QEP------TLFRGCIRTNLDPLGVySDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRN 1376
Cdd:PRK13638 84 QDPeqqifyTDIDSDIAFSLRNLGV-PEAEITRRVDEALTLVDAQHFRHQPIQCLSH-------GQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 1377 KILVLDEATASIDSATD----AIIQRIIREefaDCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKL 1442
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRtqmiAIIRRIVAQ---GNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEV 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1221-1414 |
1.02e-14 |
|
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: 74.75 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISkiGLKD-----LR 1295
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1296 MKLSIIPQEPTLfrgcirtnLDPLGVYSD------------DEIWK----ALEKCQLKTTISNLPNKLdssvsdegenwS 1359
Cdd:cd03292 78 RKIGVVFQDFRL--------LPDRNVYENvafalevtgvppREIRKrvpaALELVGLSHKHRALPAEL-----------S 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 1360 VGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAH 1414
Cdd:cd03292 139 GGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATH 194
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
622-805 |
1.04e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 74.12 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG--EIPKVSGTVKVFG----------SIAYVSQtswiqsgtirDNILY 689
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGrpldkrsfrkIIGYVPQ----------DDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 690 GK--PMESRRYNAAIKacaldkdmngfghgdlteigqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAgvl 767
Cdd:cd03213 95 PTltVRETLMFAAKLR------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA--- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063712898 768 FHkcVEDSLKE-----KTVILVTHQV--EFLSEVDQILVMEEGTI 805
Cdd:cd03213 148 LQ--VMSLLRRladtgRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1237-1431 |
1.24e-14 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 75.17 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISkiGLK-DLRMKLSIIP--QEPTLFRGC-- 1311
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT--GLPpHEIARLGIGRtfQIPRLFPELtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1312 ---------IRTNLDPLGVYSDDEIWKALEKCQ--LKTTisNLPNKLDSSVSdegeNWSVGQRQLFCLGRVLLKRNKILV 1380
Cdd:cd03219 93 lenvmvaaqARTGSGLLLARARREEREARERAEelLERV--GLADLADRPAG----ELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1381 LDEATASIDSA-TDAIIQRI--IREEfaDCTVITVAHRVPTVID-SDMVMVLSFG 1431
Cdd:cd03219 167 LDEPAAGLNPEeTEELAELIreLRER--GITVLLVEHDMDVVMSlADRVTVLDQG 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1237-1419 |
1.29e-14 |
|
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: 73.93 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKiglkdlrmkLSIIPQEPTLFRG------ 1310
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE---------QRDEPHENILYLGhlpglk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1311 ---CIRTNLD---PLGVYSDDEIWKALEKCQLkTTISNLP-NKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDE 1383
Cdd:TIGR01189 86 pelSALENLHfwaAIHGGAQRTIEDALAAVGL-TGFEDLPaAQL-----------SAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063712898 1384 ATASIDSATDAIIQRIIREEFAD--CTVITVAHRVPTV 1419
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARggIVLLTTHQDLGLV 191
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
622-815 |
1.37e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 75.54 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQ-SGTIRDNI 687
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQHSSLAfPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 ---LYGKPMESRRYNAAIKAcALDK-DMNGFGHGDLTEigqrginLSGGQKQRIQLARA-------VYADADVYLLDDPF 756
Cdd:COG4559 97 algRAPHGSSAAQDRQIVRE-ALALvGLAHLAGRSYQT-------LSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 757 SAVD-AHTAGVLfhkcveDSLKEKT-----VILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:COG4559 169 SALDlAHQHAVL------RLARQLArrgggVVAVLHDLNLAAQYaDRILLLHQGRLVAQGTPEEVL 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
622-814 |
1.65e-14 |
|
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: 74.33 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------------SIAYVSQTSWIQSG-TIRDNI- 687
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 ----LYGKPMESRRYNAaikacalDKDMNGFGhgdLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 762
Cdd:cd03265 96 iharLYGVPGAERRERI-------DELLDFVG---LLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 763 T-AGVLFHkcVEDSLKEK--TVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEEL 814
Cdd:cd03265 166 TrAHVWEY--IEKLKEEFgmTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1221-1429 |
1.71e-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: 74.05 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPN--APLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLkdlrmKL 1298
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPTLFRGciRTNLD----PL---GVySDDEIW----KALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFC 1367
Cdd:cd03293 76 GYVFQQDALLPW--LTVLDnvalGLelqGV-PKAEAReraeELLELVGLSGFENAYPHQL-----------SGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 1368 LGRVLLKRNKILVLDEATASIDSATDAIIQ----RIIREEFAdcTVITVAHRvptvID-----SDMVMVLS 1429
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQeellDIWRETGK--TVLLVTHD----IDeavflADRVVVLS 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1237-1434 |
1.75e-14 |
|
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: 72.46 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDlrmklsiipqepTLFRGcIRTnl 1316
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD------------ARRAG-IAM-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1317 dplgVYsddeiwkalekcQLkttisnlpnkldssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSA-TDAI 1395
Cdd:cd03216 80 ----VY------------QL----------------------SVGERQMVEIARALARNARLLILDEPTAALTPAeVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063712898 1396 IQRI--IREEfaDCTVITVAHRVPTVID-SDMVMVLSFGDLV 1434
Cdd:cd03216 122 FKVIrrLRAQ--GVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1216-1444 |
2.18e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.22 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1216 PSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKST---LISALFRLVEPASGCILIDGIDISKIGLK 1292
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1293 DLRMKLSIIPQEP-TLFRGcirtnldplGVYSDDEIW----KALEKCQLKTTISNLPNKLD--SSVSDEGENWSVGQRQL 1365
Cdd:PRK13640 81 DIREKVGIVFQNPdNQFVG---------ATVGDDVAFglenRAVPRPEMIKIVRDVLADVGmlDYIDSEPANLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1366 FCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLM 1443
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
.
gi 1063712898 1444 E 1444
Cdd:PRK13640 232 S 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1217-1444 |
2.25e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.17 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1217 SNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM 1296
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1297 KLSIIPQEP-TLFRGCIRT-----NLDPLGVYSDD---EIWKALEKCqlkttisNLPNKLDSsvsdEGENWSVGQRQLFC 1367
Cdd:PRK13648 84 HIGIVFQNPdNQFVGSIVKydvafGLENHAVPYDEmhrRVSEALKQV-------DMLERADY----EPNALSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1368 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLME 1444
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
622-815 |
2.38e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 74.30 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQTSWIQSG-TIRDN 686
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlTVEDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILygKPMESRRYNAAIKACALDKDMNGFGhgdLTEI-GQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD--Aht 763
Cdd:COG1137 99 IL--AVLELRKLSKKEREERLEELLEEFG---ITHLrKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiA-- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 764 agvlfhkcVED------SLKEKTV-ILVT-HQV-EFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:COG1137 172 --------VADiqkiirHLKERGIgVLITdHNVrETLGICDRAYIISEGKVLAEGTPEEIL 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
620-815 |
3.00e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 74.35 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSG-TIRD 685
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQENHINSRlTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 686 NILYGKPMESR-RYNAAIKAcALDKDMNGFghgDLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVD-AH 762
Cdd:COG4604 95 LVAFGRFPYSKgRLTAEDRE-IIDEAIAYL---DLEDLADRYLDeLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKH 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 763 TAGV--LFHKCVEDslKEKTVILVTHQVEFLSE-VDQILVMEEGTITQSGKYEELL 815
Cdd:COG4604 171 SVQMmkLLRRLADE--LGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEII 224
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
289-558 |
4.13e-14 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 74.22 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 289 IFIAVFAFLRTFAVVSLPLMLYVFVDY--ANSDHRDLRNGFFnLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAA 366
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVllPDGDPETQALNVY-SLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 367 YKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAG-AFPGLILLLLCGLLNLP 445
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 446 FAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSS 525
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1063712898 526 VV-FLGCALLKSAPLNASTIFTVLATLRVMSEPV 558
Cdd:pfam00664 241 LAlWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1221-1442 |
4.31e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.38 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAP-LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLS 1299
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1300 IIPQEP-TLFRGC-----IRTNLDPLGVYSDDEIWKALEKCQLkTTISNLPNKldssvsdEGENWSVGQRQLFCLGRVLL 1373
Cdd:PRK13650 85 MVFQNPdNQFVGAtveddVAFGLENKGIPHEEMKERVNEALEL-VGMQDFKER-------EPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 1374 KRNKILVLDEATASID-SATDAIIQRI--IREEFaDCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKL 1442
Cdd:PRK13650 157 MRPKIIILDEATSMLDpEGRLELIKTIkgIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1237-1434 |
4.87e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 72.20 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISAL--FRLVEPASGCILIDGIDISKiglKDLRMKLSIIPQEPTLfrgcirt 1314
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDIL------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1315 nldplgvYSDDEIWKALE---KCQlkttisnlpnkldssvsdegeNWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSA 1391
Cdd:cd03213 94 -------HPTLTVRETLMfaaKLR---------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063712898 1392 TDAIIQRIIReEFAD--CTVITVAHRVPTVIDS--DMVMVLSFGDLV 1434
Cdd:cd03213 146 SALQVMSLLR-RLADtgRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
906-1171 |
5.16e-14 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 74.22 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 906 LLWSSVLGQVGFVVFQAASTYWLAFAIgipkitntmLIGVYSIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFK 985
Cdd:pfam00664 16 PAFPLVLGRILDVLLPDGDPETQALNV---------YSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 986 APMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQDYYLASAR 1065
Cdd:pfam00664 87 QPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1066 ELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQNVTLFTCALL- 1144
Cdd:pfam00664 167 KLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFg 246
|
250 260
....*....|....*....|....*..
gi 1063712898 1145 LILIPKGYIAPGLVGLSLSYALTLTQT 1171
Cdd:pfam00664 247 AYLVISGELSVGDLVAFLSLFAQLFGP 273
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
620-815 |
6.08e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 73.87 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSL---LHAVL--------------GEIPKVSGTVKVFGSIAYVSQTSWIQSgT 682
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLrpqkgkvlvsgidtGDFSKLQGIRKLVGIVFQNPETQFVGR-T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 683 IRDNILYGK------PMESR-RYNAAIKACALDKdmngFGHgdlteigQRGINLSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:PRK13644 95 VEEDLAFGPenlclpPIEIRkRVDRALAEIGLEK----YRH-------RSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 756 FSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
622-809 |
6.51e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.51 E-value: 6.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIP--KVSG--------TVKVFGSIAYVSQTSWIQSG---------- 681
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGshiellgrTVQREGRLARDIRKSRANTGyifqqfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 --TIRDNILYGKPMES-------RRYNAAIKACALDK----DMNGFGHgdlteigQRGINLSGGQKQRIQLARAVYADAD 748
Cdd:PRK09984 100 rlSVLENVLIGALGSTpfwrtcfSWFTREQKQRALQAltrvGMVHFAH-------QRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 749 VYLLDDPFSAVDAHTAgvlfhKCVEDSLKE------KTVILVTHQVEF-LSEVDQILVMEEGTITQSG 809
Cdd:PRK09984 173 VILADEPIASLDPESA-----RIVMDTLRDinqndgITVVVTLHQVDYaLRYCERIVALRQGHVFYDG 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
622-786 |
8.34e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.15 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLL------HAvlgEIP--KVSGTVKVFG---------------SIAYVSQ---- 674
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLrclnrmND---LIPgaRVEGEILLDGediydpdvdvvelrrRVGMVFQkpnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 675 --TSwiqsgtIRDNILYGkP----MESRRYNAAI-----KACAL-D--KDmngfghgDLteiGQRGINLSGGQKQRIQLA 740
Cdd:COG1117 104 fpKS------IYDNVAYG-LrlhgIKSKSELDEIveeslRKAALwDevKD-------RL---KKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 741 RAVYADADVYLLDDPFSAVDAHTAGVlfhkcVED---SLKEK-TVILVTH 786
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAK-----IEElilELKKDyTIVIVTH 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
622-787 |
1.02e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.83 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVK----------VFGSIAYVSQtswiQSG-----TIRDN 686
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldggdiddpdVAEACHYLGH----RNAmkpalTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 I-----LYGkpmeSRRYNAAIKACAldkdmngFGHGDLTEIgqRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:PRK13539 94 LefwaaFLG----GEELDIAAALEA-------VGLAPLAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*..
gi 1063712898 762 HTAGvLFHKCVEDSLKEK-TVILVTHQ 787
Cdd:PRK13539 161 AAVA-LFAELIRAHLAQGgIVIAATHI 186
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1442 |
1.24e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.13 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAP---LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIS----KIGLKD 1293
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1294 LRMKLSIIPQ--EPTLFRGCIRTNL--DPL--GVYSDDEIWKALEKCQLkttiSNLPNK-LDSSVSDegenWSVGQRQLF 1366
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDIcfGPMnfGVSEEDAKQKAREMIEL----VGLPEElLARSPFE----LSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1367 CLGRVLLKRNKILVLDEATASIDSATdaiiQRIIREEFA------DCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEP 1439
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
...
gi 1063712898 1440 SKL 1442
Cdd:PRK13634 231 REI 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1223-1429 |
1.32e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1223 LQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIP 1302
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1303 QEPTLFRGCIRTNL-----------DPlgvysdDEIWKALEKCQLKTTIsnlpnkLDSSVSDegenWSVGQRQlfclgRV 1371
Cdd:PRK10247 88 QTPTLFGDTVYDNLifpwqirnqqpDP------AIFLDDLERFALPDTI------LTKNIAE----LSGGEKQ-----RI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1372 LLKRN-----KILVLDEATASIDSAT----DAIIQRIIREEfaDCTVITVAHRVPTVIDSDMVMVLS 1429
Cdd:PRK10247 147 SLIRNlqfmpKVLLLDEITSALDESNkhnvNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITLQ 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
616-812 |
1.35e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 616 ETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQTSWIQSGT 682
Cdd:PRK10247 19 DAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 683 IRDNILYgkPMESRryNAAIKACALDKDMNGFGHGDltEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:PRK10247 97 VYDNLIF--PWQIR--NQQPDPAIFLDDLERFALPD--TILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 762 HT---AGVLFHKCVEDslKEKTVILVTHQVEFLSEVDQILVME-EGTITQSGKYE 812
Cdd:PRK10247 171 SNkhnVNEIIHRYVRE--QNIAVLWVTHDKDEINHADKVITLQpHAGEMQEARYE 223
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
628-787 |
1.52e-13 |
|
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: 75.56 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 628 EIKHGQKVAVCGPVGAGKSSLLHaVLGEIPKVSG---TVKVFGSIAYVSQTSWIQSGTIRDNILYgkPMESrrynaaika 704
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIY--PDSS--------- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 705 caLDKDMNGFGHGDL---------TEIGQRGIN----------LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAG 765
Cdd:TIGR00954 542 --EDMKRRGLSDKDLeqildnvqlTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170 180
....*....|....*....|..
gi 1063712898 766 VLFHKCVEDSLkekTVILVTHQ 787
Cdd:TIGR00954 620 YMYRLCREFGI---TLFSVSHR 638
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
622-837 |
1.99e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.97 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSG-TIRDNI 687
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 LYGK-PMESR--RYNAAIKAcALDKDMNGFGHGDLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTA 764
Cdd:PRK11231 98 AYGRsPWLSLwgRLSAEDNA-RVNQAMEQTRINHLAD--RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 765 GVLFHKCVEDSLKEKTVILVTHQVEFLSE-VDQILVMEEGTITQSGKYEELL---MMGTAFQQLVNAHNDAVTVLPL 837
Cdd:PRK11231 175 VELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMtpgLLRTVFDVEAEIHPEPVSGTPM 251
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
613-807 |
2.28e-13 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 71.31 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 613 WEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLhAVLG--EIPKvSGTVKVFG-----------------SIAYVS 673
Cdd:COG4181 19 GTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLL-GLLAglDRPT-SGTVRLAGqdlfaldedararlrarHVGFVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 674 QTS-WIQSGTIRDNILYgkPMESRRY-NAAIKACALDKDMnGFGHgdltEIGQRGINLSGGQKQRIQLARAVYADADVYL 751
Cdd:COG4181 97 QSFqLLPTLTALENVML--PLELAGRrDARARARALLERV-GLGH----RLDHYPAQLSGGEQQRVALARAFATEPAILF 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 752 LDDPFSAVDAHT----AGVLFhkcvedSLKEK---TVILVTHQVEFLSEVDQILVMEEGTITQ 807
Cdd:COG4181 170 ADEPTGNLDAATgeqiIDLLF------ELNRErgtTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1223-1402 |
2.60e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 71.03 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1223 LQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGL-KDLRMKLSII 1301
Cdd:cd03218 3 AENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1302 PQEPTLFRG-CIRTNLdpLGV-----YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKR 1375
Cdd:cd03218 81 PQEASIFRKlTVEENI--LAVleirgLSKKEREEKLEELLEEFHITHLRKSKASSLSG-------GERRRVEIARALATN 151
|
170 180
....*....|....*....|....*..
gi 1063712898 1376 NKILVLDEATASIDSATDAIIQRIIRE 1402
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1238-1450 |
4.71e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.57 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRL--VEP---ASGCILIDGIDI--SKIGLKDLRMKLSIIPQEPTLFRG 1310
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1311 CIRTN----LDPLGVYSDDEIWKALEKCQLKTTISN-LPNKL-DSSVSDEGenwsvGQRQLFCLGRVLLKRNKILVLDEA 1384
Cdd:PRK14239 101 SIYENvvygLRLKGIKDKQVLDEAVEKSLKGASIWDeVKDRLhDSALGLSG-----GQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1385 TASIDSATDAIIQRIIREEFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLM------ETDSYFS 1450
Cdd:PRK14239 176 TSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFmnpkhkETEDYIS 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1238-1435 |
5.14e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 73.57 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVePASGCILIDGIDISKIG---LKDLRMKLSIIPQEPtlFrgcirT 1314
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-----G 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1315 NLDP-----------LGVYS--------DDEIWKALEKCQLK-TTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLK 1374
Cdd:COG4172 374 SLSPrmtvgqiiaegLRVHGpglsaaerRARVAEALEEVGLDpAARHRYPHEF-----------SGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1375 RNKILVLDEATasidSATDAIIQ-------RIIREEFA--------DCTVI-TVAHRvptvidsdmVMVLSFGDLVE 1435
Cdd:COG4172 443 EPKLLVLDEPT----SALDVSVQaqildllRDLQREHGlaylfishDLAVVrALAHR---------VMVMKDGKVVE 506
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1221-1401 |
5.55e-13 |
|
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: 69.55 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKigLKDLRMKLSI 1300
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLF-----RGCIRTNLDPLGVySDDEIWKALEkcqlkttISNLPNKLDSSVSdegeNWSVGQRQLFCLGRVLLKR 1375
Cdd:cd03268 77 LIEAPGFYpnltaRENLRLLARLLGI-RKKRIDEVLD-------VVGLKDSAKKKVK----GFSLGMKQRLGIALALLGN 144
|
170 180
....*....|....*....|....*.
gi 1063712898 1376 NKILVLDEATASIDSATDAIIQRIIR 1401
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIL 170
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1221-1435 |
5.71e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.14 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM-- 1296
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1297 -KLSIIPQEPTLFRGciRTnldplgVYsdDEIWKALE-----KCQLKTTISNLpnkLD-SSVSDEGE----NWSVGQRQL 1365
Cdd:PRK11153 82 rQIGMIFQHFNLLSS--RT------VF--DNVALPLElagtpKAEIKARVTEL---LElVGLSDKADrypaQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1366 FCLGRVLLKRNKILVLDEATASIDSA-TDAIIQ--RIIREEFaDCTVITVAHRVpTVIDS--DMVMVLSFGDLVE 1435
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPAtTRSILEllKDINREL-GLTIVLITHEM-DVVKRicDRVAVIDAGRLVE 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
606-807 |
6.03e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 606 IQVGNFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAvLGEIPKVSGTVKVFGSIAYVSQTSW-------- 677
Cdd:PRK14258 8 IKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYerrvnlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 678 -------------IQSGTIRDNILYGKPMESRR--------YNAAIKACALDKDMNgfghgdlTEIGQRGINLSGGQKQR 736
Cdd:PRK14258 86 lrrqvsmvhpkpnLFPMSVYDNVAYGVKIVGWRpkleiddiVESALKDADLWDEIK-------HKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 737 IQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLK-EKTVILVTH---QVEFLSEVDQILVMEEGTITQ 807
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRsELTMVIVSHnlhQVSRLSDFTAFFKGNENRIGQ 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
626-815 |
6.45e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.00 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 626 HLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-----------IAYVSQTSWIQSG-TIRDNILYGkpm 693
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQENNLFSHlTVAQNIGLG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 694 esrrYNAAIKacaldkdMNGFGHGDLTEIGQR-GIN---------LSGGQKQRIQLARAVYADADVYLLDDPFSAVD-AH 762
Cdd:PRK10771 96 ----LNPGLK-------LNAAQREKLHAIARQmGIEdllarlpgqLSGGQRQRVALARCLVREQPILLLDEPFSALDpAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 763 TAGVLfhKCVEDSLKEK--TVILVTHQVEflsEVDQI----LVMEEGTITQSGKYEELL 815
Cdd:PRK10771 165 RQEML--TLVSQVCQERqlTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELL 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1221-1414 |
6.47e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.50 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPL---VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKigLKDLR-- 1295
Cdd:COG1101 2 LELKNLSKTFNPGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK--LPEYKra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1296 MKLSIIPQEP---TLFRGCIRTNLD-----------PLGVYSDDeiwKALEKCQLKTTISNLPNKLDSSVsdegENWSVG 1361
Cdd:COG1101 80 KYIGRVFQDPmmgTAPSMTIEENLAlayrrgkrrglRRGLTKKR---RELFRELLATLGLGLENRLDTKV----GLLSGG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1362 QRQLFCLGRVLLKRNKILVLDEATASIDSATDAII----QRIIREEfaDCTVITVAH 1414
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEEN--NLTTLMVTH 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1237-1456 |
6.96e-13 |
|
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: 70.06 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISkiGLKDLRMKLSIIPQEPTLFrgcirtnl 1316
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALF-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1317 dP-LGVYSDDE---IWKALEKCQLKTTISNLPNKL--DSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDS 1390
Cdd:cd03299 84 -PhMTVYKNIAyglKKRKVDKKEIERKVLEIAEMLgiDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1391 ATDAIIQ---RIIREEFaDCTVITVAHRVPTV-IDSDMVMVLSFGDLVEYNEPSKLMETDSyfSKLVAEY 1456
Cdd:cd03299 163 RTKEKLReelKKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPK--NEFVAEF 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1221-1421 |
7.10e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 71.65 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM-- 1296
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1297 -KLSIIPQEPTLFRGciRTNLD----PLgvysddEIWKaLEKCQLKTTISNLpnkLDsSV--SDEGENW----SVGQRQl 1365
Cdd:COG1135 82 rKIGMIFQHFNLLSS--RTVAEnvalPL------EIAG-VPKAEIRKRVAEL---LE-LVglSDKADAYpsqlSGGQKQ- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 1366 fclgRV-----LLKRNKILVLDEATASIDSA-TDAIIQRI--IREEFaDCTV--IT--------VAHRVpTVID 1421
Cdd:COG1135 148 ----RVgiaraLANNPKVLLCDEATSALDPEtTRSILDLLkdINREL-GLTIvlIThemdvvrrICDRV-AVLE 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1237-1428 |
7.26e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD-LRMKLSIIPQEPTLF------- 1308
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVpnlsvae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1309 ----------RGCIRtnldplgvysddeiWKALEK------CQLKTTISnlpnkLDSSVSDegenWSVGQRQLFCLGRVL 1372
Cdd:COG1129 99 niflgreprrGGLID--------------WRAMRRrarellARLGLDID-----PDTPVGD----LSVAQQQLVEIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1373 LKRNKILVLDEATASIDSATDAIIQRIIReEFAD--CTVITVAHRVPTVID-SDMVMVL 1428
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIR-RLKAqgVAIIYISHRLDEVFEiADRVTVL 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
620-787 |
8.56e-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: 68.92 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQsgtirdNILYG------KP- 692
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE------NILYLghlpglKPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 693 ---MESRRYNAAIKACAlDKDMngfgHGDLTEIGQRGIN------LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAht 763
Cdd:TIGR01189 88 lsaLENLHFWAAIHGGA-QRTI----EDALAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-- 160
|
170 180
....*....|....*....|....*.
gi 1063712898 764 AGV-LFHKCVEDSL-KEKTVILVTHQ 787
Cdd:TIGR01189 161 AGVaLLAGLLRAHLaRGGIVLLTTHQ 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
672-815 |
9.22e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.52 E-value: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 672 VSQTSWIQSGTIRDNILYGKPMESRR-YNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVY 750
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKEDATREdVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 751 LLDDPFSAVDAHTAGVLFHKCVEDSLK-EKTVILVTHQVEFLSEVDQILVMEE----GTITQS-GKYEELL 815
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELL 1451
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1246-1414 |
1.06e-12 |
|
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: 69.98 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1246 REGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDL----RMKLSIIPQEPTLFRGciRTNLD---- 1317
Cdd:cd03294 48 REGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPH--RTVLEnvaf 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1318 PL---GVYSDDEIWKALEKCQ---LKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATasidSA 1391
Cdd:cd03294 126 GLevqGVPRAEREERAAEALElvgLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF----SA 190
|
170 180
....*....|....*....|....*....
gi 1063712898 1392 TDAIIQRIIREEFADC------TVITVAH 1414
Cdd:cd03294 191 LDPLIRREMQDELLRLqaelqkTIVFITH 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
613-809 |
1.30e-12 |
|
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: 69.28 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 613 WEPETK-IPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------SIAYVSQTSWI--QSGTI 683
Cdd:cd03267 27 FKRKYReVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkrRKKFLRRIGVVfgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 684 RDNIlygKPMESRRYNAAI---KACALDKDMNGFGhgDLTEIG----QRGINLSGGQKQRIQLARAVYADADVYLLDDPF 756
Cdd:cd03267 107 WWDL---PVIDSFYLLAAIydlPPARFKKRLDELS--ELLDLEelldTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 757 SAVDAHTAGVLfHKCVEDSLKEK--TVILVTH---QVEFLSevDQILVMEEGTITQSG 809
Cdd:cd03267 182 IGLDVVAQENI-RNFLKEYNRERgtTVLLTSHymkDIEALA--RRVLVIDKGRLLYDG 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
620-815 |
1.35e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS------------IAYVSQTSWI-QSGTIRDN 686
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIGVVPQFDNLdLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 IL-YGK--PMESRRYNAAIKA----CALDKDMNGfghgdlteigqRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAV 759
Cdd:PRK13536 135 LLvFGRyfGMSTREIEAVIPSllefARLESKADA-----------RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 760 DAHTAGVLFHKCVEDSLKEKTVILVTHqveFLSEV----DQILVMEEGTITQSGKYEELL 815
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGKTILLTTH---FMEEAerlcDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
618-816 |
1.41e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.42 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV--LGE-IPKVS--GTVKVFGSIAYVSQTSWIQ------------- 679
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDlNPEVTitGSIVYNGHNIYSPRTDTVDlrkeigmvfqqpn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 680 --SGTIRDNILYGKPMESRRYNAAIKAcALDKDMNGFGHGDltEIGQR----GINLSGGQKQRIQLARAVYADADVYLLD 753
Cdd:PRK14239 97 pfPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWD--EVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 754 DPFSAVDAHTAGVlfhkcVEDSL----KEKTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELLM 816
Cdd:PRK14239 174 EPTSALDPISAGK-----IEETLlglkDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYNDTKQMFM 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1228-1442 |
1.41e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 69.72 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1228 IRYR-PNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDISKIGLKDLRMKLSIIPQE 1304
Cdd:PRK13639 7 LKYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1305 P--TLFRGCIRTNL--DPLGV-YSDDEIWK----ALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKR 1375
Cdd:PRK13639 87 PddQLFAPTVEEDVafGPLNLgLSKEEVEKrvkeALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1376 NKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHRVPTV-IDSDMVMVLSFGDLVEYNEPSKL 1442
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1221-1444 |
1.54e-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: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVLK---GISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASG--CILI--DGIDISKIGLkD 1293
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVgdEWVDMTKPGP-D 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1294 LRMK----LSIIPQEPTLF--RGCIRTNLDPLGVYSDDEIWKALEKCQLKTT------ISNLPNKLDSSVsdegenwSVG 1361
Cdd:TIGR03269 359 GRGRakryIGILHQEYDLYphRTVLDNLTEAIGLELPDELARMKAVITLKMVgfdeekAEEILDKYPDEL-------SEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1362 QRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRII---REEFADcTVITVAHRVPTVID-SDMVMVLSFGDLVEYN 1437
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDvCDRAALMRDGKIVKIG 510
|
....*..
gi 1063712898 1438 EPSKLME 1444
Cdd:TIGR03269 511 DPEEIVE 517
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1237-1453 |
1.83e-12 |
|
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: 69.50 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGidiskiglkdlrmKLSIIPQEPTLFRGCIRTNL 1316
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1317 dPLGVYSDDEIWKALEK-CQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDA- 1394
Cdd:cd03291 119 -IFGVSYDEYRYKSVVKaCQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKe 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1395 IIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLV 1453
Cdd:cd03291 198 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
622-814 |
1.83e-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: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG--EIPKVSGtvKVFGSIAYVSQTSWIQ-------------------- 679
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSG--RIIYHVALCEKCGYVErpskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 680 ------SGTIRDNI-------------LYG---------KPMESRRYNA--AIKACALDKDMNGFGHgDLTEIGQrgiNL 729
Cdd:TIGR03269 94 vdfwnlSDKLRRRIrkriaimlqrtfaLYGddtvldnvlEALEEIGYEGkeAVGRAVDLIEMVQLSH-RITHIAR---DL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 730 SGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGvLFHKCVEDSLKEK--TVILVTHQVEFLSEV-DQILVMEEGTIT 806
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASgiSMVLTSHWPEVIEDLsDKAIWLENGEIK 248
|
....*...
gi 1063712898 807 QSGKYEEL 814
Cdd:TIGR03269 249 EEGTPDEV 256
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
616-813 |
1.96e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 69.69 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 616 ETKipTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG---------------SIAYVSQTSWIQ- 679
Cdd:PRK13637 19 EKK--ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPEYQl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 680 -SGTIRDNILYGkPME--------SRRYNAAIKACALD----KDMNGFghgdlteigqrgiNLSGGQKQRIQLARAVYAD 746
Cdd:PRK13637 97 fEETIEKDIAFG-PINlglseeeiENRVKRAMNIVGLDyedyKDKSPF-------------ELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 747 ADVYLLDDPFSAVDAHTAGVLFHKCVEdsLKEK---TVILVTHQVEFLSE-VDQILVMEEGTITQSGKYEE 813
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKE--LHKEynmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
950-1196 |
2.98e-12 |
|
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: 69.45 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 950 STLSAGFVyaRAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELT 1029
Cdd:cd18600 82 SLLAMGFF--RGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1030 AALLIMTYVTWQVIIIALLALAATKVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERF---FKNYL 1106
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFetlFHKAL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1107 NLVDADavlFFLSNAAMEWVILRIETLqNVTLFTCALLLILIPKGYiAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSI 1186
Cdd:cd18600 240 NLHTAN---WFLYLSTLRWFQMRIEMI-FVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLM 314
|
250
....*....|
gi 1063712898 1187 ISVERIKQYM 1196
Cdd:cd18600 315 RSVSRIFKFI 324
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
622-814 |
3.10e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.98 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS---------IAYVSQTSwiqsG-----TIRDNI 687
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpldpedrrrIGYLPEER----GlypkmKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 LY-----GkpMESRRYNAAIKAcALDKdmngFGhgdLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:COG4152 93 VYlarlkG--LSKAEAKRRADE-WLER----LG---LGDRANKKVeELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 762 HTAGVLfhkcvEDSLKE-----KTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEEL 814
Cdd:COG4152 163 VNVELL-----KDVIRElaakgTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1236-1443 |
3.39e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.06 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1236 LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG---LKDLRMK--------LSIIPQE 1304
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKkiamvfqsFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1305 PTLFRGCIRTNLdpLGVYSDDEIWKALEKCQ---LKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVL 1381
Cdd:PRK10070 122 TVLDNTAFGMEL--AGINAEERREKALDALRqvgLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1382 DEATasidSATDAIIQRIIREEFADC------TVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLM 1443
Cdd:PRK10070 189 DEAF----SALDPLIRTEMQDELVKLqakhqrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1237-1463 |
3.67e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGC-----ILIDGIDISKI-GLKDLRMKLSIIPQEPTLFRG 1310
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1311 CIRTNLdPLGVYSDDEIWKALEK--CQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASI 1388
Cdd:PRK14271 116 SIMDNV-LAGVRAHKLVPRKEFRgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1389 DSATDAIIQRIIREEFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLM------ETDSYFSKLVAEYWASCR 1461
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFsspkhaETARYVAGLSGDVKDAKR 274
|
..
gi 1063712898 1462 GN 1463
Cdd:PRK14271 275 GN 276
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1233-1434 |
3.74e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 68.58 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1233 NAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG-LKDLRMKLSIIPQEP------ 1305
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqiva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1306 TLFRGCIRTNLDPLGVYSdDEIWKALEKCQLKTTISNL----PNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVL 1381
Cdd:PRK13633 101 TIVEEDVAFGPENLGIPP-EEIRERVDESLKKVGMYEYrrhaPHLL-----------SGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 1382 DEATASID-SATDAIIQRI--IREEFAdCTVITVAHRVPTVIDSDMVMVLSFGDLV 1434
Cdd:PRK13633 169 DEPTAMLDpSGRREVVNTIkeLNKKYG-ITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1221-1415 |
4.06e-12 |
|
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: 66.02 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIrYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGidiskiglkdlRMKLSI 1300
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLFRGCIRTNLdplgVYSddeiWkalekcqlkttisnlpnkldssvsdeGENWSVGQRQLFCLGRVLLKRNKILV 1380
Cdd:cd03223 69 LPQRPYLPLGTLREQL----IYP----W--------------------------DDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 1063712898 1381 LDEATASIDSATDAIIQRIIREEFAdcTVITVAHR 1415
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
635-835 |
4.07e-12 |
|
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: 69.37 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 635 VAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------------SIAYVSQ-TSWIQSGTIRDNILYGKpmesR 696
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQeARLFPHLSVRGNLRYGM----K 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 697 RYNAAIKACALDK--DMNGFGHgdlteIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVD-AHTAGVL-FHKC 771
Cdd:TIGR02142 102 RARPSERRISFERviELLGIGH-----LLGRLPGrLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdPRKYEILpYLER 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 772 VEDSLKeKTVILVTHQvefLSEV----DQILVMEEGTITQSGKYEEllMMGTAFQQLVnAHNDAVTVL 835
Cdd:TIGR02142 177 LHAEFG-IPILYVSHS---LQEVlrlaDRVVVLEDGRVAAAGPIAE--VWASPDLPWL-AREDQGSLI 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
620-806 |
5.45e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.05 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVS----QTSWIQSG 681
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNI------------LYGKPMESRRYNAAIKAcaldkdmngFG---HGDLTEIGqrgiNLSGGQKQRIQLARAVYAD 746
Cdd:COG1129 346 SIRENItlasldrlsrggLLDRRRERALAEEYIKR---------LRiktPSPEQPVG----NLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 747 ADVYLLDDPFSAVD--AHTAgvlFHKCVEDSLKE-KTVILVThqveflSEV-------DQILVMEEGTIT 806
Cdd:COG1129 413 PKVLILDEPTRGIDvgAKAE---IYRLIRELAAEgKAVIVIS------SELpellglsDRILVMREGRIV 473
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1232-1439 |
7.01e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.34 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1232 PNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIS---------------KI-GLKDLR 1295
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGdkknnhelitnpyskKIkNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1296 MKLSIIPQEP--TLFRGCIRTNL--DP--LGVYSDDEIWKA---LEKCQLKTTIsnlpnkLDSSVSDegenWSVGQRQLF 1366
Cdd:PRK13631 116 RRVSMVFQFPeyQLFKDTIEKDImfGPvaLGVKKSEAKKLAkfyLNKMGLDDSY------LERSPFG----LSGGQKRRV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1367 CLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADC-TVITVAHRVPTVID-SDMVMVLSFGDLVEYNEP 1439
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1238-1453 |
7.28e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRlVEPA---SGCILIDGIDISKIGLKDLRMK-LSIIPQEPTL------ 1307
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNIRDTERAgIAIIHQELALvkelsv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1308 ----FRGCirtNLDPLGVYSDDEIWKALEKC--QLKTTIS-NLPnkldssVSDEGenwsVGQRQLFCLGRVLLKRNKILV 1380
Cdd:PRK13549 100 leniFLGN---EITPGGIMDYDAMYLRAQKLlaQLKLDINpATP------VGNLG----LGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1381 LDEATASIDSATDAIIQRIIREEFA-DCTVITVAHRVPTVID-SDMVMVLSFGDLVEyNEPSKLMETDSYFSKLV 1453
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAhGIACIYISHKLNEVKAiSDTICVIRDGRHIG-TRPAAGMTEDDIITMMV 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
622-805 |
8.22e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGeIPKVSGTVKVFGSiAYVSQTS--------------WiqsGTIRDNI 687
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGT-APLAEARedtrlmfqdarllpW---KKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 ---LYGKPMESRRynAAIKACALDKDMNGFGHGdlteigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTA 764
Cdd:PRK11247 103 glgLKGQWRDAAL--QALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063712898 765 gVLFHKCVEdSLKEK---TVILVTHQV-EFLSEVDQILVMEEGTI 805
Cdd:PRK11247 170 -IEMQDLIE-SLWQQhgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
622-810 |
8.44e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.11 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-----LGEIPKVSGTVKVFGSIAYVSQTSWIQ---------------SG 681
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPDVDPVEvrrrigmvfqkpnpfPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNILYGKpmesrrynaaikacaldkDMNGFgHGDLTEIGQR------------------GINLSGGQKQRIQLARAV 743
Cdd:PRK14243 106 SIYDNIAYGA------------------RINGY-KGDMDELVERslrqaalwdevkdklkqsGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 744 YADADVYLLDDPFSAVDA-HTAGV--LFHKcvedsLKEK-TVILVTHQVEFLSEVDQILVMEEGTITQSGK 810
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPiSTLRIeeLMHE-----LKEQyTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1221-1419 |
9.56e-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: 9.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDISKiglkdlRMKL 1298
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAA------RNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1299 SIIPQEPTLFRGciRTNLDPLgVYSDDeiWKALEKCQLKTTISNLPNKLDSSVSDEG--ENWSVGQRQLFCLGRVLLKRN 1376
Cdd:cd03269 73 GYLPEERGLYPK--MKVIDQL-VYLAQ--LKGLKKEEARRRIDEWLERLELSEYANKrvEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063712898 1377 KILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHRVPTV 1419
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELV 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1237-1414 |
9.63e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 65.33 E-value: 9.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGidisKIGLKDLRMKLSIIPQEPTLFRGCI---- 1312
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPLTVRDLVamgr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1313 ---RTNLDPLGVYSDDEIWKALEKCQLkTTISNLPnkLDSsvsdegenWSVGQRQLFCLGRVLLKRNKILVLDEATASID 1389
Cdd:NF040873 83 warRGLWRRLTRDDRAAVDDALERVGL-ADLAGRQ--LGE--------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180
....*....|....*....|....*.
gi 1063712898 1390 SATDAIIQRIIREEFAD-CTVITVAH 1414
Cdd:NF040873 152 AESRERIIALLAEEHARgATVVVVTH 177
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
622-792 |
1.11e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPK--VSGTVKVfgsiayvSQTSWIQSGTIRDNILYGKPMesrryN 699
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGtpVAGCVDV-------PDNQFGREASLIDAIGRKGDF-----K 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 700 AAIKAcaldkdMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKcVEDSLKE- 778
Cdd:COG2401 114 DAVEL------LNAVGLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN-LQKLARRa 186
|
170
....*....|....*
gi 1063712898 779 -KTVILVTHQVEFLS 792
Cdd:COG2401 187 gITLVVATHHYDVID 201
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1237-1446 |
1.12e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNL 1316
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1317 DPLGVY-----------SDDE-IWKALEKCQLKTtisnLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLDEA 1384
Cdd:PRK10575 106 VAIGRYpwhgalgrfgaADREkVEEAISLVGLKP----LAHRLVDSLSG-------GERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1385 TASIDSATD----AIIQRIIREEfaDCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMETD 1446
Cdd:PRK10575 175 TSALDIAHQvdvlALVHRLSQER--GLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1238-1431 |
1.25e-11 |
|
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: 65.82 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDL----RMKLSIIPQEPTLFRGCIR 1313
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1314 TNLdPLGVYSDDEIWKAL-EKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASID-SA 1391
Cdd:cd03290 97 ENI-TFGSPFNKQRYKAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063712898 1392 TDAIIQRIIREEFAD--CTVITVAHRVPTVIDSDMVMVLSFG 1431
Cdd:cd03290 176 SDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
623-787 |
1.29e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 623 RNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SI-----AYVSQTSWI--QSGtIRDNIlygKPME 694
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGePIrrqrdEYHQDLLYLghQPG-IKTEL---TALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 695 SRRYNAAIKACALDKDMngfgHGDLTEIGQRGI------NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDahTAGVlf 768
Cdd:PRK13538 94 NLRFYQRLHGPGDDEAL----WEALAQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID--KQGV-- 165
|
170 180
....*....|....*....|....
gi 1063712898 769 hKCVEDSLKEKT-----VILVTHQ 787
Cdd:PRK13538 166 -ARLEALLAQHAeqggmVILTTHQ 188
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
968-1196 |
1.31e-11 |
|
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: 67.24 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 968 GLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIAL 1047
Cdd:cd18559 66 GIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1048 LALAATKVvQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERfFKNYLNLVDADAVLFFLSNAAMEWVI 1127
Cdd:cd18559 146 LGLLYVPV-NRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEA-FIRQVDAKRDNELAYLPSIVYLRALA 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1128 LRIETLQNVtLFTCALLLILIPKGYIApGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1196
Cdd:cd18559 224 VRLWCVGPC-IVLFASFFAYVSRHSLA-GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
622-815 |
1.51e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.40 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-----LGEIPKVSGTVKVFGSIAYVSQTSWIQSG--------------- 681
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEVRrevgmvfqypnpfph 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 -TIRDNILYG-------KPMES--RRYNAAIKACALDKDMNgfghgdlTEIGQRGINLSGGQKQRIQLARAVYADADVYL 751
Cdd:PRK14267 100 lTIYDNVAIGvklnglvKSKKEldERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 752 LDDPFSAVDAHTAgvlfhKCVEDSL----KEKTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:PRK14267 173 MDEPTANIDPVGT-----AKIEELLfelkKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKVF 236
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
619-786 |
1.66e-11 |
|
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: 65.51 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 619 IPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG----------------SIAYVSQTS-WIQSG 681
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDFrLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDN------ILYGKPME-SRRYNAAIKACALDKDMNGFGHGdlteigqrginLSGGQKQRIQLARAVYADADVYLLDD 754
Cdd:cd03292 94 NVYENvafaleVTGVPPREiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1063712898 755 PFSAVDA-HTAGV--LFHKCvedSLKEKTVILVTH 786
Cdd:cd03292 163 PTGNLDPdTTWEImnLLKKI---NKAGTTVVVATH 194
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
620-814 |
1.70e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.33 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSW----------IQSG------T 682
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGeNIPAMSRSRLytvrkrmsmlFQSGalftdmN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 683 IRDNILYGKPMESRRYNAAIKACALDKdmngfghgdLTEIGQRGI------NLSGGQKQRIQLARAVYADADVYLLDDPF 756
Cdd:PRK11831 101 VFDNVAYPLREHTQLPAPLLHSTVMMK---------LEAVGLRGAaklmpsELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 757 SAVDAHTAGVLFhKCVeDSLKEK---TVILVTHQV-EFLSEVDQILVMEEGTITQSGKYEEL 814
Cdd:PRK11831 172 VGQDPITMGVLV-KLI-SELNSAlgvTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
622-814 |
2.06e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 66.58 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVfGSIAYVSQTSWIQSGTIRD---------------- 685
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLKPLRKkvgivfqfpehqlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 686 ----NILYGkPME--------SRRYNAAIKACALDKDMngfghgdlteIGQRGINLSGGQKQRIQLARAVYADADVYLLD 753
Cdd:PRK13634 102 tvekDICFG-PMNfgvseedaKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 754 DPfsavdahTAGV----------LFHKCvedsLKEK--TVILVTHQVEFLSE-VDQILVMEEGTITQSGKYEEL 814
Cdd:PRK13634 171 EP-------TAGLdpkgrkemmeMFYKL----HKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
723-815 |
2.23e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.76 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 723 GQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEV-DQILVME 801
Cdd:PRK10619 147 GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLH 226
|
90
....*....|....
gi 1063712898 802 EGTITQSGKYEELL 815
Cdd:PRK10619 227 QGKIEEEGAPEQLF 240
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1234-1433 |
2.32e-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: 63.99 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1234 APLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI----------SKIGL--KDlRMKLSII 1301
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrrsprdairAGIAYvpED-RKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1302 PQEPtlfrgcIRTNLdplgvysddeiwkalekcqlkttisNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVL 1381
Cdd:cd03215 91 LDLS------VAENI-------------------------ALSSLL-----------SGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1382 DEATASIDSATDAIIQRIIReEFAD--CTVITVAHRVPTVID-SDMVMVLSFGDL 1433
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIR-ELADagKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
622-818 |
2.47e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.12 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQ-TSWIQSGTIRDN 686
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQeLNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILYGKPMESR---RYNAAIKACA--LDKdmngFG-HGDL-TEIGqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAV 759
Cdd:COG1129 100 IFLGREPRRGgliDWRAMRRRARelLAR----LGlDIDPdTPVG----DLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 760 DAHTAGVLFhKCVEDsLKEK--TVILVTHqveFLSEV----DQILVMEEGTITQSGKYEEL-------LMMG 818
Cdd:COG1129 172 TEREVERLF-RIIRR-LKAQgvAIIYISH---RLDEVfeiaDRVTVLRDGRLVGTGPVAELtedelvrLMVG 238
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1221-1444 |
2.76e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVLKG---ISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG----LKD 1293
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRAlfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1294 LRMKLSIIPQEP--TLFRGCIRTNL----DPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFC 1367
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafgpQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSG-------GQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1368 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLME 1444
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
606-824 |
3.28e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 65.91 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 606 IQVGN--FGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IA 670
Cdd:PRK13650 5 IEVKNltFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwdirhkIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 671 YVSQTSWIQ--SGTIRDNILYG--------KPMESRrynaaikacaLDKDMNGFGHGDLTEigQRGINLSGGQKQRIQLA 740
Cdd:PRK13650 85 MVFQNPDNQfvGATVEDDVAFGlenkgiphEEMKER----------VNEALELVGMQDFKE--REPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 741 RAVYADADVYLLDDPFSAVDAHTAGVLFhKCVEdSLKEK---TVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMM 817
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELI-KTIK-GIRDDyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
....*..
gi 1063712898 818 GTAFQQL 824
Cdd:PRK13650 231 GNDLLQL 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1221-1414 |
3.43e-11 |
|
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: 64.70 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKiGLKDLRMKLSI 1300
Cdd:cd03265 1 IEVENLVKKYGDF--EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEPTLfrgcirtnldplgvysdDEIWKALEKCQLKTTISNLPNKLDSSVSDE-------GE-------NWSVGQRQLF 1366
Cdd:cd03265 78 VFQDLSV-----------------DDELTGWENLYIHARLYGVPGAERRERIDElldfvglLEaadrlvkTYSGGMRRRL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 1367 CLGRVLLKRNKILVLDEATASIDSATDAIIQRIIR---EEFaDCTVITVAH 1414
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEklkEEF-GMTILLTTH 190
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
616-820 |
3.82e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.84 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 616 ETKIPT--LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSiaYVSQTSWIQSGTIRDN------- 686
Cdd:PRK11629 17 EGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAELRNQklgfiyq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 -----------------ILYG--KPMES-RRYNAAIKACALDKDMNgfghgdlteigQRGINLSGGQKQRIQLARAVYAD 746
Cdd:PRK11629 95 fhhllpdftalenvampLLIGkkKPAEInSRALEMLAAVGLEHRAN-----------HRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 747 ADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVIL-VTHQVEFLSEVDQILVMEEGTITQsgkyeELLMMGTA 820
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLvVTHDLQLAKRMSRQLEMRDGRLTA-----ELSLMGAE 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1237-1442 |
4.34e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.06 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEpASGCILIDG--------IDISKIGLKDLRMKLSIIPQEPTLF 1308
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNLNRLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1309 rgcirtnldPLGVYS-----------------DDEIWKALEKCQLKTTISNlpnKLDSSVSDegenWSVGQRQLFCLGRV 1371
Cdd:PRK14258 101 ---------PMSVYDnvaygvkivgwrpkleiDDIVESALKDADLWDEIKH---KIHKSALD----LSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1372 LLKRNKILVLDEATASIDSATDAIIQRIIREEF--ADCTVITVAHRVPTVID-SDMVMVLS-----FGDLVEYNEPSKL 1442
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRlSDFTAFFKgnenrIGQLVEFGLTKKI 243
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
618-813 |
4.46e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 65.98 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-LGEIPKvSGTVKVFG----------------SIAYVSQT-SWIQ 679
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInLLERPT-SGRVLVDGqdltalsekelrkarrQIGMIFQHfNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 680 SGTIRDNI-----LYGKPmesrryNAAIKACALDK-DMNGfghgdLTEIGQR-GINLSGGQKQRIQLARAVYADADVYLL 752
Cdd:PRK11153 96 SRTVFDNValpleLAGTP------KAEIKARVTELlELVG-----LSDKADRyPAQLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 753 DDPFSAVD-AHTAGVLfhkcveDSLKE------KTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEE 813
Cdd:PRK11153 165 DEATSALDpATTRSIL------ELLKDinrelgLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGTVSE 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
622-809 |
4.50e-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: 63.70 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKVSGtvkvfGSIAYVSQtswiqsgtirdNILyGKPMESR---- 696
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhPKYEVTE-----GEILFKGE-----------DIT-DLPPEERarlg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 697 -----RYNAAIKacaldkdmnGFGHGDLTeigqRGIN--LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAhTAGVLFH 769
Cdd:cd03217 79 iflafQYPPEIP---------GVKNADFL----RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DALRLVA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063712898 770 KCVEDSLKEKT-VILVTHQVEFLSEV--DQILVMEEGTITQSG 809
Cdd:cd03217 145 EVINKLREEGKsVLIITHYQRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
624-815 |
4.85e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 624 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTV--------------KVFGSIAYVSQTSWI-QSGTIRDNIL 688
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplhaRARRGIGYLPQEASIfRRLSVYDNLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 689 ygKPMESRR-YNAAIKACALDKDMNGFGHGDLTE-IGQrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAhtAGV 766
Cdd:PRK10895 101 --AVLQIRDdLSAEQREDRANELMEEFHIEHLRDsMGQ---SLSGGERRRVEIARALAANPKFILLDEPFAGVDP--ISV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 767 LFHKCVEDSLKEK--TVILVTHQV-EFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:PRK10895 174 IDIKRIIEHLRDSglGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
610-809 |
5.81e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.14 E-value: 5.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 610 NFGWEPETKIPT--LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVfGSIAYVSQTSWIQSGTIRDN- 686
Cdd:PRK13643 8 NYTYQPNSPFASraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIKPVRKKv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 -ILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGI---------------NLSGGQKQRIQLARAVYADADVY 750
Cdd:PRK13643 87 gVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLemvgladefwekspfELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 751 LLDDPFSAVDAhTAGVLFHKCVEDSLKE-KTVILVTHQVEFLSE-VDQILVMEEGTITQSG 809
Cdd:PRK13643 167 VLDEPTAGLDP-KARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
622-889 |
6.05e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.21 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------------SIAYVSQT-SWIQSGTI 683
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 684 RDNILYGK-----PMESRRYNA--AIKACALDKdmngFGHGDLTEigqrginLSGGQKQRIQLARAVYADADVYLLDDPF 756
Cdd:PRK10070 124 LDNTAFGMelagiNAEERREKAldALRQVGLEN----YAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 757 SAVDAHTAGVLFHKCVEDSLK-EKTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELLMmgtafqqlvNAHNDAVTV 834
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILN---------NPANDYVRT 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 835 ----LPLASNESLGDLRKEGKDREIRNMtvvekieeeiektdiPG------VQLTQEEEKESGYV 889
Cdd:PRK10070 264 ffrgVDISQVFSAKDIARRTPNGLIRKT---------------PGfgprsaLKLLQDEDREYGYV 313
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
606-816 |
6.31e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.82 E-value: 6.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 606 IQVGNFGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYV 672
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 673 SQTS--WIQSGTIRDNILYGkPME--------SRRYNAAIKACALDKDMNGFGHgdlteigqrgiNLSGGQKQRIQLARA 742
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFG-PINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 743 VYADADVYLLDDPFSAVDAHTAGVLFhKCVEDSLKE--KTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELLM 816
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETygMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFL 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
611-852 |
6.49e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.73 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 611 FGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQTSW 677
Cdd:PRK13642 12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwnlrrkIGMVFQNPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 678 IQ--SGTIRDNILYGKPMESRRYNAAIKAcaLDKDMNGFGHGDLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:PRK13642 92 NQfvGATVEDDVAFGMENQGIPREEMIKR--VDEALLAVNMLDFKT--REPARLSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 756 FSAVDAHTAGVLFHkcVEDSLKEK---TVILVTHQVEFLSEVDQILVMEEGTITQSGKYEELLMMGtafQQLVNAHNDav 832
Cdd:PRK13642 168 TSMLDPTGRQEIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS---EDMVEIGLD-- 240
|
250 260
....*....|....*....|
gi 1063712898 833 tvLPLASNeSLGDLRKEGKD 852
Cdd:PRK13642 241 --VPFSSN-LMKDLRKNGFD 257
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
622-814 |
8.37e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.33 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-IAY-------VSQTSWIQ---------SGTIR 684
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYdkkslleVRKTVGIVfqnpddqlfAPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 DNILYGK-----PME--SRRYNAAIKACaldkDMNGFG----HgdlteigqrgiNLSGGQKQRIQLARAVYADADVYLLD 753
Cdd:PRK13639 98 EDVAFGPlnlglSKEevEKRVKEALKAV----GMEGFEnkppH-----------HLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 754 DPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSE-VDQILVMEEGTITQSGKYEEL 814
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1238-1453 |
9.92e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 9.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRlVEPA---SGCILIDGIDISKIGLKDLRMK-LSIIPQEPTL------ 1307
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLvpelsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1308 ----FRGCIRTNldPLGVYSDDEIWKALEKCQLKTTISNLPNKLdsSVSDEGenwsVGQRQLFCLGRVLLKRNKILVLDE 1383
Cdd:TIGR02633 96 aeniFLGNEITL--PGGRMAYNAMYLRAKNLLRELQLDADNVTR--PVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 1384 ATASIDSATDAIIQRIIREEFA-DCTVITVAHRVPTVID-SDMVMVLSFGDLVEyNEPSKLMETDSYFSKLV 1453
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHVA-TKDMSTMSEDDIITMMV 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1221-1444 |
1.06e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.38 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPL---VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG----LKD 1293
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1294 LRMKLSIIPQ--EPTLFRGCIRTNL----DPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFC 1367
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVafgpQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSG-------GQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1368 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFAD-CTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLME 1444
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
632-787 |
1.10e-10 |
|
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: 62.51 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 632 GQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGsiayvsQTSWIQSGTIRDNILYG----------KPMESRRYNAA 701
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG------GPLDFQRDSIARGLLYLghapgikttlSVLENLRFWHA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 702 IKAC-----ALDK-DMNGFGHgdlTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDS 775
Cdd:cd03231 100 DHSDeqveeALARvGLNGFED---RPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHC 172
|
170
....*....|..
gi 1063712898 776 LKEKTVILVTHQ 787
Cdd:cd03231 173 ARGGMVVLTTHQ 184
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1237-1451 |
1.40e-10 |
|
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: 65.59 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRL--VEPASGCIL---------------------------------I 1281
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1282 DGIDISKIGLKDLRMKLSIIPQ-------EPTLFRGCIRTnLDPLGVYSDDEIWKA---LEKCQLKTTISNLPNKLdssv 1351
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQrtfalygDDTVLDNVLEA-LEEIGYEGKEAVGRAvdlIEMVQLSHRITHIARDL---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1352 sdegenwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHrVPTVID--SDMVMV 1427
Cdd:TIGR03269 170 -------SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSH-WPEVIEdlSDKAIW 241
|
250 260
....*....|....*....|....*...
gi 1063712898 1428 LSFGDLVEYNEP----SKLMETDSYFSK 1451
Cdd:TIGR03269 242 LENGEIKEEGTPdevvAVFMEGVSEVEK 269
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1237-1443 |
1.41e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD-LRMKLSIIPQEPTLFRgcirtn 1315
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFR------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1316 ldPLGVYSDD----EIWKALEKCQLKTTISNLPNKLD-SSVSDE-GENWSVGQRQLFCLGRVLLKRNKILVLDEATASID 1389
Cdd:PRK10895 92 --RLSVYDNLmavlQIRDDLSAEQREDRANELMEEFHiEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1390 SATDAIIQRIIrEEFAD--CTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLM 1443
Cdd:PRK10895 170 PISVIDIKRII-EHLRDsgLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1238-1435 |
1.47e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.66 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDISKIGLKDLRMKLsiIPQEPT--------- 1306
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRSQRIRM--IFQDPStslnprqri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1307 --LFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISN-LPNKLDSsvsdegenwsvGQRQLFCLGRVLLKRNKILVLDE 1383
Cdd:PRK15112 107 sqILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASyYPHMLAP-----------GQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1384 ATASID-SATDAIIQRIIR-EEFADCTVITVAHRVPTVID-SDMVMVLSFGDLVE 1435
Cdd:PRK15112 176 ALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVE 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
622-815 |
1.50e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.84 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPK---VSGTVKVFGSI----------AYVSQTS-WIQSGTIRDNI 687
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPidakemraisAYVQQDDlFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 LYGKPME-SRRYNAAIKACALDK--DMNGFGHGDLTEIGQRGI--NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 762
Cdd:TIGR00955 121 MFQAHLRmPRRVTKKEKRERVDEvlQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 763 TAGVLFHKCVEDSLKEKTVILVTHQ--VEFLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:TIGR00955 201 MAYSVVQVLKGLAQKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1237-1428 |
1.80e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCIlidgidiskigLKDLRMKLSIIPQ----EPTLFRGCI 1312
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQklylDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1313 R-TNLDPlGVYSDDeIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATASID-- 1389
Cdd:PRK09544 88 RfLRLRP-GTKKED-ILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDvn 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063712898 1390 ---SATDAIIQriIREEFaDCTVITVAHRVPTVI-DSDMVMVL 1428
Cdd:PRK09544 155 gqvALYDLIDQ--LRREL-DCAVLMVSHDLHLVMaKTDEVLCL 194
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
616-840 |
1.98e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 616 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHaVLGEIPK-VSGTVKV--------------------FGSI----A 670
Cdd:PRK10535 18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVagqdvatldadalaqlrrehFGFIfqryH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 671 YVSQTSWIQSGTIrDNILYGKPMESRRYnaaiKACALdkdMNGFGHGDltEIGQRGINLSGGQKQRIQLARAVYADADVY 750
Cdd:PRK10535 97 LLSHLTAAQNVEV-PAVYAGLERKQRLL----RAQEL---LQRLGLED--RVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 751 LLDDPFSAVDAHTAGVLFhkCVEDSLKEK--TVILVTHQVEFLSEVDQILVMEEGTITQS----------GKYEELLMMG 818
Cdd:PRK10535 167 LADEPTGALDSHSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIVRNppaqekvnvaGGTEPVVNTA 244
|
250 260
....*....|....*....|....
gi 1063712898 819 TAFQQLVNAHNDAVTV--LPLASN 840
Cdd:PRK10535 245 SGWRQFVSGFREALTMawRAMAAN 268
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
619-814 |
2.60e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 619 IPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQTSWI-QSGTI 683
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLfPNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 684 RDNILYGKPME---SRRYNAAIKA--CALDKDMNGfghGDLtEIGQRginlsggqkQRIQLARAVYADADVYLLDDPFSA 758
Cdd:PRK15439 104 KENILFGLPKRqasMQKMKQLLAAlgCQLDLDSSA---GSL-EVADR---------QIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 759 VDAHTAGVLFHKCveDSLKEKTV--ILVTHQvefLSEV----DQILVMEEGTITQSGKYEEL 814
Cdd:PRK15439 171 LTPAETERLFSRI--RELLAQGVgiVFISHK---LPEIrqlaDRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
610-814 |
2.62e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.31 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 610 NFGWEPETKIPT--LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------------SIA 670
Cdd:PRK13641 9 DYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 671 YVSQTSWIQ--SGTIRDNILYGkPM-----ESRRYNAA---IKACALDKDMngfghgdlteIGQRGINLSGGQKQRIQLA 740
Cdd:PRK13641 89 LVFQFPEAQlfENTVLKDVEFG-PKnfgfsEDEAKEKAlkwLKKVGLSEDL----------ISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 741 RAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSE-VDQILVMEEGTITQSGKYEEL 814
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
622-809 |
2.73e-10 |
|
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: 62.00 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGsIAYVSQTSWIQSG--------------TIRDNI 687
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-FDVVKEPAEARRRlgfvsdstglydrlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 -----LYGkpMESRRYNAAIKACALDKDMNGFghgdlteIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 762
Cdd:cd03266 100 eyfagLYG--LKGDELTARLEELADRLGMEEL-------LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 763 TAGVLFhkcveDSLKE-----KTVILVTHQVEFLSEV-DQILVMEEGTITQSG 809
Cdd:cd03266 171 ATRALR-----EFIRQlralgKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1446 |
3.10e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1300
Cdd:PRK13647 5 IEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEP-------TLFR----GCIRTNLDPLGVysDDEIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLG 1369
Cdd:PRK13647 84 VFQDPddqvfssTVWDdvafGPVNMGLDKDEV--ERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1370 RVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVA-HRVPTVID-SDMVMVLSFGDLVEYNEPSKLMETD 1446
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1216-1397 |
3.75e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 61.68 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1216 PSNGTIHLQELKIRY-RPNAPL-VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKI---G 1290
Cdd:COG4181 4 SSAPIIELRGLTKTVgTGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1291 LKDLR-MKLSIIPQE----PTLfrgcirTNLD----PLGVYSDDEIWK----ALEKCQLKTTISNLPNKLdssvsdegen 1357
Cdd:COG4181 84 RARLRaRHVGFVFQSfqllPTL------TALEnvmlPLELAGRRDARAraraLLERVGLGHRLDHYPAQL---------- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063712898 1358 wSVGQRQLFCLGRVLLKRNKILVLDEATASIDSAT-DAIIQ 1397
Cdd:COG4181 148 -SGGEQQRVALARAFATEPAILFADEPTGNLDAATgEQIID 187
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1238-1452 |
3.84e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.49 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI-SKIG---LKDLRMKLSIIPQ--EPTLFRGC 1311
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKdkyIRPVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1312 I-----------RTNLDPLGVYSDDEIwkaLEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILV 1380
Cdd:PRK13646 103 VereiifgpknfKMNLDEVKNYAHRLL---MDLGFSRDVMSQSPFQM-----------SGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1381 LDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMETDSYFSKL 1452
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
631-793 |
3.94e-10 |
|
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: 59.69 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 631 HGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQSGTIrdnilygkpmesrrynaaikacaldkd 710
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 711 mngfghgdlteIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEK------TVILV 784
Cdd:smart00382 54 -----------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLkseknlTVILT 122
|
....*....
gi 1063712898 785 THQVEFLSE 793
Cdd:smart00382 123 TNDEKDLGP 131
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1246-1391 |
3.95e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.52 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1246 REGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIglKDLRMKLSIIPQEPTLF-----RGCIRTNLDPlG 1320
Cdd:PRK10771 23 ERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT--PPSRRPVSMLFQENNLFshltvAQNIGLGLNP-G 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 1321 VYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLDEATASIDSA 1391
Cdd:PRK10771 100 LKLNAAQREKLHAIARQMGIEDLLARLPGQLSG-------GQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1237-1435 |
5.24e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.01 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKI---GLKDLRMKLSIIPQE-PTLF--RG 1310
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDsISAVnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1311 CIR----------TNLDPlgvysDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILV 1380
Cdd:PRK10419 107 TVReiireplrhlLSLDK-----AERLARASEMLRAVDLDDSVLDKRPPQLSG-------GQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1381 LDEATASIDSATDA-IIQRI--IREEFAD-CTVIT--------VAHRvptvidsdmVMVLSFGDLVE 1435
Cdd:PRK10419 175 LDEAVSNLDLVLQAgVIRLLkkLQQQFGTaCLFIThdlrlverFCQR---------VMVMDNGQIVE 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
622-814 |
5.28e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.10 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVfGSIAYVSQTSWIQSGTIRDNI--LYGKPmESRRYN 699
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-DDITITHKTKDKYIRPVRKRIgmVFQFP-ESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 700 AAI--------KACALD-KDMNGFGHGDLTEIG-------QRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA-- 761
Cdd:PRK13646 101 DTVereiifgpKNFKMNlDEVKNYAHRLLMDLGfsrdvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPqs 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 762 -HTAGVLFHKCVEDslKEKTVILVTHQV-EFLSEVDQILVMEEGTITQSGKYEEL 814
Cdd:PRK13646 181 kRQVMRLLKSLQTD--ENKTIILVSHDMnEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
595-836 |
5.30e-10 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 61.74 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 595 SGLDASGTAVDIQVGNFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------- 667
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLFGAKQRA-PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqld 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 668 ---------SIAYVSQTSWIQ---SGTIRDNIlyGKPMES----------RRYNAAIKACALDKDmngfgHGDlteigQR 725
Cdd:TIGR02769 80 rkqrrafrrDVQLVFQDSPSAvnpRMTVRQII--GEPLRHltsldeseqkARIAELLDMVGLRSE-----DAD-----KL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 726 GINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEdsLKEK---TVILVTHQVEFLSEV-DQILVME 801
Cdd:TIGR02769 148 PRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRK--LQQAfgtAYLFITHDLRLVQSFcQRVAVMD 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 1063712898 802 EGTITQSGKYEELLMMGT-AFQQLVNAhndavtVLP 836
Cdd:TIGR02769 226 KGQIVEECDVAQLLSFKHpAGRNLQSA------VLP 255
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1228-1434 |
5.50e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 61.71 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1228 IRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTL 1307
Cdd:PRK13548 8 LSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1308 -F----RGCIRTNLDPLGVYS---DDEIWKALEKCQLkttiSNLPNKLDSSVSdeGenwsvGQRQLFCLGRVLL------ 1373
Cdd:PRK13548 88 sFpftvEEVVAMGRAPHGLSRaedDALVAAALAQVDL----AHLAGRDYPQLS--G-----GEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 1374 KRNKILVLDEATASIDSATDAIIQRIIReEFAD---CTVITVAHrvptviD-------SDMVMVLSFGDLV 1434
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLAR-QLAHergLAVIVVLH------DlnlaaryADRIVLLHQGRLV 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
615-814 |
5.57e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.12 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 615 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSS---LLHAVL--GEIPKVSGTVKvfgSIAYVSQTSW---------IQS 680
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLlpDDNPNSKITVD---GITLTAKTVWdirekvgivFQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 681 -------GTIRDNILYGkpMESRRYNAAIKACALDKDMNGFGHGDLteIGQRGINLSGGQKQRIQLARAVYADADVYLLD 753
Cdd:PRK13640 93 pdnqfvgATVGDDVAFG--LENRAVPRPEMIKIVRDVLADVGMLDY--IDSEPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 754 DPFSAVD-AHTAGVLfhKCVEDSLKEK--TVILVTHQVEFLSEVDQILVMEEGTITQSGKYEEL 814
Cdd:PRK13640 169 ESTSMLDpAGKEQIL--KLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1235-1435 |
6.74e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.42 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1235 PLVLK---GISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMK---LSIIPQEPtLF 1308
Cdd:PRK15079 31 PKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDP-LA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1309 RGCIRTNL-----DPLGVY----SDDEIWKALEKCQLKTTIsnLPNKLDSSVSDegenWSVGQRQLFCLGRVLLKRNKIL 1379
Cdd:PRK15079 110 SLNPRMTIgeiiaEPLRTYhpklSRQEVKDRVKAMMLKVGL--LPNLINRYPHE----FSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 1380 VLDEATASIDSATDA----IIQRIIREefADCTVITVAHRVPTV--IdSDMVMVLSFGDLVE 1435
Cdd:PRK15079 184 ICDEPVSALDVSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVkhI-SDRVLVMYLGHAVE 242
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
618-809 |
8.22e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.17 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG--EIpkVSGTVKVFGS-----------IAYVSQT-SWIQSGTI 683
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleRI--TSGEIWIGGRvvnelepadrdIAMVFQNyALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 684 RDNILYG-------KPMESRRYNAAIKacaldkdmngfghgdLTEIGQ----RGINLSGGQKQRIQLARAVYADADVYLL 752
Cdd:PRK11650 94 RENMAYGlkirgmpKAEIEERVAEAAR---------------ILELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 753 DDPFSAVDAHtagVLFHKCVE-----DSLKeKTVILVTH-QVEFLSEVDQILVMEEGTITQSG 809
Cdd:PRK11650 159 DEPLSNLDAK---LRVQMRLEiqrlhRRLK-TTSLYVTHdQVEAMTLADRVVVMNGGVAEQIG 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1237-1436 |
8.54e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 60.62 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLK-DLRMKLSIIpqEPTLFRGCIrtn 1315
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGgGFNPELTGR--ENIYLNGRL--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1316 ldpLGVySDDEIWKALEKCQlktTISNLPNKLDSSVSdegeNWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAI 1395
Cdd:cd03220 112 ---LGL-SRKEIDEKIDEII---EFSELGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063712898 1396 IQRIIREEFADC-TVITVAHRVPTVID-SDMVMVLSFGDLVEY 1436
Cdd:cd03220 181 CQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFD 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1244-1441 |
1.04e-09 |
|
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: 60.88 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1244 TFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKdlrmklsIIPQEPTLFRGCIRTNLDPLGVYS 1323
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY-------IKADYEGTVRDLLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1324 ddeiwkalekcQLKTTISNlPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIReE 1403
Cdd:cd03237 94 -----------YFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR-R 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063712898 1404 FADCTVITVahrvpTVIDSDMVMVLSFGD--LVEYNEPSK 1441
Cdd:cd03237 161 FAENNEKTA-----FVVEHDIIMIDYLADrlIVFEGEPSV 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
622-815 |
1.25e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.83 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYV--------------------SQTSWIQSG 681
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgkdifqidaiklrkevgmvfQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNILYgkPMES------RRYNAAIKACALDKDMNGFGHGDLTEIGQRginLSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:PRK14246 106 SIYDNIAY--PLKShgikekREIKKIVEECLRKVGLWKEVYDRLNSPASQ---LSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 756 FSAVDAHTAGVLfHKCVEDSLKEKTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:PRK14246 181 TSMIDIVNSQAI-EKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1451 |
1.35e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.97 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1300
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1301 IPQEP--TLFRGCIRTNL--DPLGVYSDDE-----IWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRV 1371
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIafGPINLGLDEEtvahrVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1372 LLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMETDSY 1448
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
...
gi 1063712898 1449 FSK 1451
Cdd:PRK13652 232 LAR 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
624-814 |
1.65e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.78 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 624 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQ-----TSWIQS------GTIRDNILYGK 691
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPPyqrpiNMMFQSyalfphMTVEQNIAFGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 692 PmESRRYNAAIKACAldKDMNGFGHgdLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHK 770
Cdd:PRK11607 117 K-QDKLPKAEIASRV--NEMLGLVH--MQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063712898 771 CVeDSLKE--KTVILVTH-QVEFLSEVDQILVMEEGTITQSGKYEEL 814
Cdd:PRK11607 192 VV-DILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1237-1283 |
2.02e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.71 E-value: 2.02e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG 1283
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1237-1434 |
2.06e-09 |
|
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: 59.65 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFrgcirTNL 1316
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLW-----WDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1317 DPLGVY---------SDDEIWKALEKCqlkTTISNLPNKLDSSVsdegENWSVGQRQLFCLGRVLLKRNKILVLDEATAS 1387
Cdd:cd03267 111 PVIDSFyllaaiydlPPARFKKRLDEL---SELLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1388 IDSATDAIIQRIIREEFAD--CTVITVAHRVPTVID-SDMVMVLSFGDLV 1434
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1237-1455 |
2.39e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.49 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDgidiskiglkdlrMKLSIIPQEPTLFRGCIRTNL 1316
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1317 dplgVYSDDE----IWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATasidSAT 1392
Cdd:PTZ00243 742 ----LFFDEEdaarLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL----SAL 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 1393 DAII-QRIIREEF----ADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETdSYFSKLVAE 1455
Cdd:PTZ00243 814 DAHVgERVVEECFlgalAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT-SLYATLAAE 880
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
622-813 |
2.73e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 59.67 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQTSWIQSG-TIRDN 686
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphriarlgIARTFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILYG--------------KPMESRRYNAAIKACA---LDKdmngFGhgdLTEI-GQRGINLSGGQKQRIQLARAVYADAD 748
Cdd:COG0411 100 VLVAaharlgrgllaallRLPRARREEREARERAeelLER----VG---LADRaDEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 749 VYLLDDPfsavdahTAGV----------LFHKCVEDslKEKTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEE 813
Cdd:COG0411 173 LLLLDEP-------AAGLnpeeteelaeLIRRLRDE--RGITILLIEHDMDLVMGLaDRIVVLDFGRVIAEGTPAE 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1190-1433 |
2.75e-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: 62.34 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1190 ERIKQYMNIPEEPPAIID---DKRPPSSWPSngtIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLIS 1266
Cdd:TIGR01257 898 EPLTEEMEDPEHPEGINDsffERELPGLVPG---VCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLS 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1267 ALFRLVEPASGCILIDGIDIsKIGLKDLRMKLSIIPQEPTLFRGCirTNLDPLGVYSDDEiWKALEKCQLKTTISNLPNK 1346
Cdd:TIGR01257 975 ILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHL--TVAEHILFYAQLK-GRSWEEAQLEMEAMLEDTG 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1347 LDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTV-IDSDMV 1425
Cdd:TIGR01257 1051 LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRI 1130
|
....*...
gi 1063712898 1426 MVLSFGDL 1433
Cdd:TIGR01257 1131 AIISQGRL 1138
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1237-1419 |
2.93e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG-LKDLRMKLSIIPQEPTLFrgcirTN 1315
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLF-----PN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1316 LDPLgvysdDEIWKALEKCQ-----LKTTISNLPNKLDSSVSdeGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDS 1390
Cdd:PRK15439 101 LSVK-----ENILFGLPKRQasmqkMKQLLAALGCQLDLDSS--AGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190
....*....|....*....|....*....|
gi 1063712898 1391 A-TDAIIQRIIREEFADCTVITVAHRVPTV 1419
Cdd:PRK15439 174 AeTERLFSRIRELLAQGVGIVFISHKLPEI 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
617-804 |
3.00e-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: 58.98 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 617 TKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIpKVSGtvkvfGSIAYVSQTSWIQSGTI---------RDNI 687
Cdd:COG4778 22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNY-LPDS-----GSILVRHDGGWVDLAQAspreilalrRRTI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 688 ------LYGKP--------MESRRYNAAIKACALDKDMNGFGHGDLTEigqrgiNL--------SGGQKQRIQLARAVYA 745
Cdd:COG4778 96 gyvsqfLRVIPrvsaldvvAEPLLERGVDREEARARARELLARLNLPE------RLwdlppatfSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 746 DADVYLLDDPFSAVDAHTAGVlfhkcVEDSLKEK-----TVILVTHQVEFLSEV-DQILVMEEGT 804
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAV-----VVELIEEAkargtAIIGIFHDEEVREAVaDRVVDVTPFS 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
620-816 |
4.10e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQTSwiqsgtIRD 685
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevvtrspqdglangIVYISEDR------KRD 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 686 NILYGkpMeSRRYNAAIkaCALDKDMNGFGH----------GDLTEI--------GQRGINLSGGQKQRIQLARAVYADA 747
Cdd:PRK10762 340 GLVLG--M-SVKENMSL--TALRYFSRAGGSlkhadeqqavSDFIRLfniktpsmEQAIGLLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 748 DVYLLDDPFSAVDahtAGV------LFHKCVEDSLkekTVILVTHQV-EFLSEVDQILVMEEGTItqSGKY------EEL 814
Cdd:PRK10762 415 KVLILDEPTRGVD---VGAkkeiyqLINQFKAEGL---SIILVSSEMpEVLGMSDRILVMHEGRI--SGEFtreqatQEK 486
|
..
gi 1063712898 815 LM 816
Cdd:PRK10762 487 LM 488
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
623-807 |
5.15e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 623 RNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQ----TSWIQSGTIR 684
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITEsrrdNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 DNILYGKPMESRRYNAAI----------KACALDKDMNGFGHgdltEIGQRGINLSGGQKQRIQLARAVYADADVYLLDD 754
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMglfhevdeqrTAENQRELLALKCH----SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 755 PFSAVDAHTAGVLFHkcVEDSLKE--KTVILVTHQV-EFLSEVDQILVMEEGTITQ 807
Cdd:PRK09700 436 PTRGIDVGAKAEIYK--VMRQLADdgKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
606-815 |
5.57e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 606 IQVGNFGWEPETKIPT----LRNIHLEIKHGQKVAVCGPVGAGKSSL---LHAVL----GEI---------PKVSGTVKV 665
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLlpdtGTIewifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 666 FGS---------------------IAYVSQTSWIQ--SGTIRDNILYG-------KPMESRRYNAAIKACALDKdmngfg 715
Cdd:PRK13651 83 VLEklviqktrfkkikkikeirrrVGVVFQFAEYQlfEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGLDE------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 716 hgdltEIGQRG-INLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHtaGV-----LFHKCVEdslKEKTVILVTHQVE 789
Cdd:PRK13651 157 -----SYLQRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQ--GVkeileIFDNLNK---QGKTIILVTHDLD 226
|
250 260
....*....|....*....|....*..
gi 1063712898 790 -FLSEVDQILVMEEGTITQSGKYEELL 815
Cdd:PRK13651 227 nVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
603-815 |
5.79e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.29 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 603 AVDIQVGNFGWEPEtkiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKvfgsiayvsqtsWIQsgt 682
Cdd:PRK15064 319 ALEVENLTKGFDNG---PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------------WSE--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 683 irdnilygkpmesrryNAAIKACALD------KDMNGF---------GHGDLT-------------EIGQRGINLSGGQK 734
Cdd:PRK15064 381 ----------------NANIGYYAQDhaydfeNDLTLFdwmsqwrqeGDDEQAvrgtlgrllfsqdDIKKSVKVLSGGEK 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 735 QRIQLARAVYADADVYLLDDPFSAVDAHTAGVLfhkcvEDSLK--EKTVILVTHQVEFLSEV-DQIL-VMEEGTITQSGK 810
Cdd:PRK15064 445 GRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL-----NMALEkyEGTLIFVSHDREFVSSLaTRIIeITPDGVVDFSGT 519
|
....*
gi 1063712898 811 YEELL 815
Cdd:PRK15064 520 YEEYL 524
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1237-1389 |
6.18e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.84 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPT---------- 1306
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATtpgditvqel 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1307 LFRGciRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKldsSVsdegENWSVGQRQLFCLGRVLLKRNKILVLDEATA 1386
Cdd:PRK10253 102 VARG--RYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQ---SV----DTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
...
gi 1063712898 1387 SID 1389
Cdd:PRK10253 173 WLD 175
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
622-805 |
6.38e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.56 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQ-----TSwiQSGTI 683
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpeykrakYIGRVFQdpmmgTA--PSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 684 RDNIL--YGKpmeSRRYNAAIkacALDKDMNGFGHGDLTEIGqRGI---------NLSGGQKQRIQLARAVYADADVYLL 752
Cdd:COG1101 100 EENLAlaYRR---GKRRGLRR---GLTKKRRELFRELLATLG-LGLenrldtkvgLLSGGQRQALSLLMATLTKPKLLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 753 DDPFSAVDAHTAGV---LFHKCV-EDSLkekTVILVTHQVEF-LSEVDQILVMEEGTI 805
Cdd:COG1101 173 DEHTAALDPKTAALvleLTEKIVeENNL---TTLMVTHNMEQaLDYGNRLIMMHEGRI 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1218-1310 |
7.79e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.12 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1218 NGTIHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGL-KDLRM 1296
Cdd:COG1137 1 MMTLEAENLVKSYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhKRARL 78
|
90
....*....|....
gi 1063712898 1297 KLSIIPQEPTLFRG 1310
Cdd:COG1137 79 GIGYLPQEASIFRK 92
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
614-814 |
8.79e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.56 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 614 EPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSL---LHAVLgeIPKvSGTVKVFGSIAYVSQTSWiqsgTIRDN--IL 688
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL--IPS-EGKVYVDGLDTSDEENLW----DIRNKagMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 689 YGKPmesrryNAAIKACALDKDMnGFGHGDL----TEIGQRGIN-----------------LSGGQKQRIQLARAVYADA 747
Cdd:PRK13633 91 FQNP------DNQIVATIVEEDV-AFGPENLgippEEIRERVDEslkkvgmyeyrrhaphlLSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 748 DVYLLDDPFSAVDAhtAGvlfHKCVEDSLKE------KTVILVTHQVEFLSEVDQILVMEEGTITQSGKYEEL 814
Cdd:PRK13633 164 ECIIFDEPTAMLDP--SG---RREVVNTIKElnkkygITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1237-1396 |
1.05e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVePASGCILIDGIDISKIGLKDL---RMKLSIIPQEPTlfrgcir 1313
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1314 TNLDP-----------LGVYS--------DDEIWKALEKCQLK-TTISNLPNKldssvsdegenWSVGQRQLFCLGRVLL 1373
Cdd:PRK15134 373 SSLNPrlnvlqiieegLRVHQptlsaaqrEQQVIAVMEEVGLDpETRHRYPAE-----------FSGGQRQRIAIARALI 441
|
170 180
....*....|....*....|...
gi 1063712898 1374 KRNKILVLDEATASIDSATDAII 1396
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQI 464
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1238-1434 |
1.10e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.19 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD---LRMKLSIIPQEPTLFRGciRT 1314
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMD--RT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1315 NLD----PL---GVYSDD---EIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEA 1384
Cdd:PRK10908 96 VYDnvaiPLiiaGASGDDirrRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1385 TASIDSATDAIIQRIIrEEF--ADCTVITVAHRVPTVIDSDM-VMVLSFGDLV 1434
Cdd:PRK10908 165 TGNLDDALSEGILRLF-EEFnrVGVTVLMATHDIGLISRRSYrMLTLSDGHLH 216
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1142-1383 |
1.12e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.43 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1142 ALLLILIpkG---YIAPGLVGLSLS----YALTLTqtqvFLTR-------WYCTLSNSIISVERIKQY---MNIPEEPPA 1204
Cdd:COG4615 241 LLFFALI--GlilFLLPALGWADPAvlsgFVLVLL----FLRGplsqlvgALPTLSRANVALRKIEELelaLAAAEPAAA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1205 IIDDKRPPSSWpsnGTIHLQELKIRYRP---NAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILI 1281
Cdd:COG4615 315 DAAAPPAPADF---QTLELRGVTYRYPGedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1282 DGIDISKIGLKDLRMKLSIIPQEPTLFrgciRTNLDPLGVYSDDEIWKALEKCQL--KTTISNlpNKLdSSVsdegeNWS 1359
Cdd:COG4615 392 DGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLERLELdhKVSVED--GRF-STT-----DLS 459
|
250 260
....*....|....*....|....*....
gi 1063712898 1360 VGQRQlfclgRV-----LLKRNKILVLDE 1383
Cdd:COG4615 460 QGQRK-----RLallvaLLEDRPILVFDE 483
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1237-1431 |
1.18e-08 |
|
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: 56.73 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKiglkdlrmklsiipQEPTLFRGC----- 1311
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF--------------QRDSIARGLlylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1312 ---IRTNLDPL-------GVYSDDEIWKALEKCQLkTTISNLP-NKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILV 1380
Cdd:cd03231 81 apgIKTTLSVLenlrfwhADHSDEQVEEALARVGL-NGFEDRPvAQL-----------SAGQQRRVALARLLLSGRPLWI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 1381 LDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFG 1431
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
628-811 |
1.19e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 57.42 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 628 EIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQT-SWIQSGTIRDnILYGKP---MESRRYNAAI 702
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYiKADYEGTVRD-LLSSITkdfYTHPYFKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 703 kacaldkdMNGFGHGDLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA----HTAGVLFHKCVEdslKE 778
Cdd:cd03237 100 --------AKPLQIEQILD--REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFAEN---NE 166
|
170 180 190
....*....|....*....|....*....|...
gi 1063712898 779 KTVILVTHQVEFLSEVDQILVMEEGtitQSGKY 811
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIVFEG---EPSVN 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
729-824 |
1.21e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.84 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 729 LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLF---HKCVEDslKEKTVILVTHQVEFLSEVDQILVMEEGTI 805
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLdlvRKVKSE--HNITIISITHDLSEAMEADHVIVMNKGTV 220
|
90
....*....|....*....
gi 1063712898 806 TQSGKYEELLMMGTAFQQL 824
Cdd:PRK13648 221 YKEGTPTEIFDHAEELTRI 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1238-1445 |
1.23e-08 |
|
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: 57.35 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDlrMKLSIIPQEPTLFRG-CIRTNL 1316
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1317 dPLGV--------YSDDEIWKA----LEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEA 1384
Cdd:cd03296 96 -AFGLrvkprserPPEAEIRAKvhelLKLVQLDWLADRYPAQL-----------SGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 1385 TASIDSATDAIIQRIIREEFADCTVIT--VAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMET 1445
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDELHVTTvfVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1221-1416 |
1.28e-08 |
|
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: 57.40 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGC---IL---IDGIDI----SKIG 1290
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLFgerRGGEDVwelrKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1291 LKDLRMKLSIIPQEPTL------FRGCIrtnldplGVY---SDDEIWKALEkcQLKTT-ISNLPNKLDSSVSDegenwsv 1360
Cdd:COG1119 82 LVSPALQLRFPRDETVLdvvlsgFFDSI-------GLYrepTDEQRERARE--LLELLgLAHLADRPFGTLSQ------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1361 GQRQLFCLGRVLLKRNKILVLDEATASID-SATDAIIQRIirEEFA---DCTVITVAHRV 1416
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDlGARELLLALL--DKLAaegAPTLVLVTHHV 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
682-816 |
1.37e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 58.32 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNILYGK-PMESRRYNAAIKAcalDKDMNGFGHGDlTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 760
Cdd:PRK13631 133 TIEKDIMFGPvALGVKKSEAKKLA---KFYLNKMGLDD-SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 761 AHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELLM 816
Cdd:PRK13631 209 PKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVaDEVIVMDKGKILKTGTPYEIFT 265
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1238-1435 |
1.56e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.05 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI---SKIGLKDLRMKLSIIPQEP--TLF-RGC 1311
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPygSLNpRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1312 IRTNL-DPLGVYSD-------DEIWKALEKCQLKTTISN-LPNKldssvsdegenWSVGQRQLFCLGRVLLKRNKILVLD 1382
Cdd:PRK11308 111 VGQILeEPLLINTSlsaaerrEKALAMMAKVGLRPEHYDrYPHM-----------FSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 1383 EATasidSATDAIIQRIIREEFAD------CTVITVAHRVPTV--IdSDMVMVLSFGDLVE 1435
Cdd:PRK11308 180 EPV----SALDVSVQAQVLNLMMDlqqelgLSYVFISHDLSVVehI-ADEVMVMYLGRCVE 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
635-813 |
1.59e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 635 VAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVfGS---IAYVSQ---------TSW--IQSGTirDNILYGK-PMESRRYN 699
Cdd:TIGR03719 351 VGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GEtvkLAYVDQsrdaldpnkTVWeeISGGL--DIIKLGKrEIPSRAYV 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 700 AAIkacaldkdmnGFGHGDLTE-IGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLfhkcvEDSLKE 778
Cdd:TIGR03719 428 GRF----------NFKGSDQQKkVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL-----EEALLN 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063712898 779 --KTVILVTHQVEFLSEV-DQILVME--------EGTITQsgkYEE 813
Cdd:TIGR03719 489 faGCAVVISHDRWFLDRIaTHILAFEgdshvewfEGNFSE---YEE 531
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
618-809 |
1.99e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 56.12 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIP---KVSGTV-------KVF-----GSIAYVSQTSW-IQSG 681
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIhyngipyKEFaekypGEIIYVSEEDVhFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNIlygkpmesrryNAAIKACAldkdmNGFghgdlteigQRGInlSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:cd03233 99 TVRETL-----------DFALRCKG-----NEF---------VRGI--SGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 762 HTAgvlFH--KCVEDSLKE-KTVILVT-HQ--VEFLSEVDQILVMEEGTITQSG 809
Cdd:cd03233 152 STA---LEilKCIRTMADVlKTTTFVSlYQasDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
612-815 |
2.00e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.11 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 612 GWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKV------FGSIAYVSQ----------- 674
Cdd:PRK15112 19 GWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhFGDYSYRSQrirmifqdpst 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 675 -------TSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKD-MNGFGHGdlteigqrginLSGGQKQRIQLARAVYAD 746
Cdd:PRK15112 99 slnprqrISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 747 ADVYLLDDPFSAVDAHTAGVLFHKCVEdsLKEK---TVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLE--LQEKqgiSYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
624-815 |
2.23e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.51 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 624 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS------------IAYVSQTSWIQSG-TIRDNILyg 690
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQFDNLDPDfTVRENLL-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 691 kpMESRRYNAAIKAC-ALDKDMNGFGHGDLTEIGQRGiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFH 769
Cdd:PRK13537 103 --VFGRYFGLSAAAArALVPPLLEFAKLENKADAKVG-ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 770 KCVEDSLKEKTVILVTHqveFLSEV----DQILVMEEGTITQSGKYEELL 815
Cdd:PRK13537 180 RLRSLLARGKTILLTTH---FMEEAerlcDRLCVIEEGRKIAEGAPHALI 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
622-760 |
2.46e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.66 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--IAYVSQTSWIQS--------------GTIRD 685
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYLDTtlpltvnrflrlrpGTKKE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 686 NILygkPMeSRRYNAaikACALDKDMNgfghgdlteigqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 760
Cdd:PRK09544 100 DIL---PA-LKRVQA---GHLIDAPMQ---------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
622-832 |
2.49e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG----------------SIAYvSQTSWIQSGTIRD 685
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlgiGIIY-QELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 686 NILYGKPMESR------------RYNAAI--KACALDKDMNgfghgdlTEIGqrgiNLSGGQKQRIQLARAVYADADVYL 751
Cdd:PRK09700 100 NLYIGRHLTKKvcgvniidwremRVRAAMmlLRVGLKVDLD-------EKVA----NLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 752 LDDPFSAVDAHTAGVLFhkCVEDSLKE--KTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEEL-------LMMGTAF 821
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLF--LIMNQLRKegTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDVsnddivrLMVGREL 246
|
250
....*....|.
gi 1063712898 822 QQLVNAHNDAV 832
Cdd:PRK09700 247 QNRFNAMKENV 257
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1236-1402 |
2.58e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.65 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1236 LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDISK-------IGLKDLrMKLSIIPQEPT 1306
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdIDDPDvaeachyLGHRNA-MKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1307 LFRGCIRtNLDPLGVYSddeiwkALEKCQLKtTISNLPNKldssvsdegeNWSVGQRQLFCLGRVLLKRNKILVLDEATA 1386
Cdd:PRK13539 95 EFWAAFL-GGEELDIAA------ALEAVGLA-PLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170
....*....|....*.
gi 1063712898 1387 SIDSATDAIIQRIIRE 1402
Cdd:PRK13539 157 ALDAAAVALFAELIRA 172
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1217-1443 |
2.70e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.52 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1217 SNGTIHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM 1296
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1297 KLSIIPQEPTLfrgciRTNLDPlgVYSDDEIWK----------------ALEKCQLKTTISNLPNKLDSSVSDEGE---N 1357
Cdd:PRK10619 80 KVADKNQLRLL-----RTRLTM--VFQHFNLWShmtvlenvmeapiqvlGLSKQEARERAVKYLAKVGIDERAQGKypvH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1358 WSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADC-TVITVAHRVPTVID-SDMVMVLSFGDLVE 1435
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGkTMVVVTHEMGFARHvSSHVIFLHQGKIEE 232
|
....*...
gi 1063712898 1436 YNEPSKLM 1443
Cdd:PRK10619 233 EGAPEQLF 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1241-1433 |
2.80e-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: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1241 ISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPA-SGCILIDG--IDIsKIGLKDLRMKLSIIPQE------------- 1304
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDI-RNPAQAIRAGIAMVPEDrkrhgivpilgvg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1305 -----PTLFRGCIRTNLDPLGvySDDEIWKALEKCQLKTTISNLP-NKLdssvsdegenwSVGQRQLFCLGRVLLKRNKI 1378
Cdd:TIGR02633 358 knitlSVLKSFCFKMRIDAAA--ELQIIGSAIQRLKVKTASPFLPiGRL-----------SGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1379 LVLDEATASIDSATDAIIQRIIREEFAD-CTVITVAHRVPTVID-SDMVMVLSFGDL 1433
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
620-806 |
3.39e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTL-RNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTV----KVfgSIAYVSQTSWIQSGTIRDNILYgkpmE 694
Cdd:PLN03073 522 PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsaKV--RMAVFSQHHVDGLDLSSNPLLY----M 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 695 SRRYNAAIKAcALDKDMNGFG-HGDLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVe 773
Cdd:PLN03073 596 MRCFPGVPEQ-KLRAHLGSFGvTGNLAL--QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV- 671
|
170 180 190
....*....|....*....|....*....|....
gi 1063712898 774 dsLKEKTVILVTHQVEFLS-EVDQILVMEEGTIT 806
Cdd:PLN03073 672 --LFQGGVLMVSHDEHLISgSVDELWVVSEGKVT 703
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1238-1416 |
3.61e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD-LRMKLSIIPQE----------PT 1306
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQElsvideltvlEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1307 LFRGCIRTNlDPLGVYSDDeiWKAL-EKCQLKTTISNLPNKLDSSVsdegENWSVGQRQLFCLGRVLLKRNKILVLDEAT 1385
Cdd:PRK09700 101 LYIGRHLTK-KVCGVNIID--WREMrVRAAMMLLRVGLKVDLDEKV----ANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1063712898 1386 ASI-DSATD---AIIQRIIREEFAdctVITVAHRV 1416
Cdd:PRK09700 174 SSLtNKEVDylfLIMNQLRKEGTA---IVYISHKL 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1216-1435 |
4.87e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1216 PSNGTIHLQELKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI-------------L 1280
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1281 IDGIDISKIGLKDLR-MKLSIIPQEPTlfrgcirTNLDPL---------------GVYSDDEIWKA---LEKCQL---KT 1338
Cdd:PRK10261 88 IELSEQSAAQMRHVRgADMAMIFQEPM-------TSLNPVftvgeqiaesirlhqGASREEAMVEAkrmLDQVRIpeaQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1339 TISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIR--EEFADCTVITVAHRV 1416
Cdd:PRK10261 161 ILSRYPHQL-----------SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDM 229
|
250 260
....*....|....*....|
gi 1063712898 1417 PTVID-SDMVMVLSFGDLVE 1435
Cdd:PRK10261 230 GVVAEiADRVLVMYQGEAVE 249
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
622-811 |
5.23e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--SIAYVSQTSWIQSGTIRDNILYGKpMESRRYN 699
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQETPALPQPALEYVIDGD-REYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 700 AAIKACALDKDMNGFG--HGDLTEIGQRGIN-----------------------LSGGQKQRIQLARAVYADADVYLLDD 754
Cdd:PRK10636 96 AQLHDANERNDGHAIAtiHGKLDAIDAWTIRsraasllhglgfsneqlerpvsdFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 755 PFSAVDAHtaGVLFhkcVEDSLK--EKTVILVTHQVEFLSE-VDQILVMEEGTITQ-SGKY 811
Cdd:PRK10636 176 PTNHLDLD--AVIW---LEKWLKsyQGTLILISHDRDFLDPiVDKIIHIEQQSLFEyTGNY 231
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
729-829 |
5.43e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 55.61 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 729 LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEdsLKEK---TVILVTHQ---VEFLSevDQILVMEE 802
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLE--LQEKlgiSYIYVSQHlgiVKHIS--DKVLVMHQ 225
|
90 100 110
....*....|....*....|....*....|.
gi 1063712898 803 GTITQSGKYEELLM----MGTafQQLVNAHN 829
Cdd:COG4167 226 GEVVEYGKTAEVFAnpqhEVT--KRLIESHF 254
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
613-809 |
5.57e-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: 58.10 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 613 WEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQSG----------- 681
Cdd:TIGR01257 938 FEPSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLgmcpqhnilfh 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 --TIRDNILYGKPMESRRYN-AAIKACALDKDmNGFGHgdltEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSA 758
Cdd:TIGR01257 1017 hlTVAEHILFYAQLKGRSWEeAQLEMEAMLED-TGLHH----KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 759 VDAHTagvlfHKCVEDSLKE----KTVILVTHQVEFLSEV-DQILVMEEGTITQSG 809
Cdd:TIGR01257 1092 VDPYS-----RRSIWDLLLKyrsgRTIIMSTHHMDEADLLgDRIAIISQGRLYCSG 1142
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
622-815 |
5.99e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.30 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV--LGEI---PKVSGTVKVFGS-------------IAYVSQT-SWIQSGT 682
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELypeARVSGEVYLDGQdifkmdvielrrrVQMVFQIpNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 683 IRDNILYG----------KPMESRRYNAAIKACALDKDMNgfghgdltEIGQRGINLSGGQKQRIQLARAVYADADVYLL 752
Cdd:PRK14247 99 IFENVALGlklnrlvkskKELQERVRWALEKAQLWDEVKD--------RLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 753 DDPFSAVDAHTAGVLFHKCVEDSlKEKTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREVF 233
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1237-1403 |
6.28e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.27 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGL-KDLRMKLSIIPQEPTLF-RGCIRT 1314
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFsRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1315 NLDPLGVYSDDEIWKalekcQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIdsaTDA 1394
Cdd:PRK11614 100 NLAMGGFFAERDQFQ-----ERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---API 171
|
170
....*....|....*
gi 1063712898 1395 IIQRI------IREE 1403
Cdd:PRK11614 172 IIQQIfdtieqLREQ 186
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
622-815 |
7.69e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.87 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSI--AYVSQTSWI-QSGTIRDNILYG---KPMES 695
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIkvGYLPQEPQLdPTKTVRENVEEGvaeIKDAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 696 RRYNA-AIKACALDKDMNGFG--HGDLTEIGQRG-------------------------INLSGGQKQRIQLARAVYADA 747
Cdd:TIGR03719 101 DRFNEiSAKYAEPDADFDKLAaeQAELQEIIDAAdawdldsqleiamdalrcppwdadvTKLSGGERRRVALCRLLLSKP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 748 DVYLLDDPFSAVDAHTAGVLfhkcvEDSLKE--KTVILVTHQVEFLSEVDQ-ILVMEEGT-ITQSGKYEELL 815
Cdd:TIGR03719 181 DMLLLDEPTNHLDAESVAWL-----ERHLQEypGTVVAVTHDRYFLDNVAGwILELDRGRgIPWEGNYSSWL 247
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1237-1414 |
9.05e-08 |
|
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: 54.18 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDlrMKLSIIPQEPTLF-RGCIRTN 1315
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYpHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1316 LD-PLGV--YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLDEATasidSAT 1392
Cdd:cd03301 93 IAfGLKLrkVPKDEIDERVREVAELLQIEHLLDRKPKQLSG-------GQRQRVALGRAIVREPKVFLMDEPL----SNL 161
|
170 180
....*....|....*....|....*...
gi 1063712898 1393 DAIIQRIIREEFA------DCTVITVAH 1414
Cdd:cd03301 162 DAKLRVQMRAELKrlqqrlGTTTIYVTH 189
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
620-795 |
1.16e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS------IAYVSQTSWI--QSG-----TIRDN 686
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVghRSGinpylTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILYGKPMESrrynaaiKACALDKDMNGFGHGDLTEIgQRGInLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGV 766
Cdd:PRK13540 95 CLYDIHFSP-------GAVGITELCRLFSLEHLIDY-PCGL-LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*....
gi 1063712898 767 LFHKCVEDSLKEKTVILVTHQVEFLSEVD 795
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
616-805 |
1.29e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.01 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 616 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------------SIAYVSQT-SW 677
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakHVGFVFQSfML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 678 IQSGTIRDNI-----LYGKPMESRRYNAAikacALDKDMNgfghgdlteIGQR----GINLSGGQKQRIQLARAVYADAD 748
Cdd:PRK10584 100 IPTLNALENVelpalLRGESSRQSRNGAK----ALLEQLG---------LGKRldhlPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 749 VYLLDDPFSAVDAHT----AGVLFhkcvedSLKEK---TVILVTHQVEFLSEVDQILVMEEGTI 805
Cdd:PRK10584 167 VLFADEPTGNLDRQTgdkiADLLF------SLNREhgtTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1223-1308 |
1.34e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.84 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1223 LQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDgidiskiglKDLRMklSIIP 1302
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLRI--GYLP 67
|
....*.
gi 1063712898 1303 QEPTLF 1308
Cdd:COG0488 68 QEPPLD 73
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1238-1428 |
1.34e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDIS--------KIGlkdlrMklsiIPQEPTL 1307
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRsprdaialGIG-----M----VHQHFML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1308 FRgcirtNL------------DPLGVYSDDEIWKALEKcqlkttIS---NLPNKLDSSVSDegenWSVGQRQlfclgRV- 1371
Cdd:COG3845 92 VP-----NLtvaenivlglepTKGGRLDRKAARARIRE------LSeryGLDVDPDAKVED----LSVGEQQ-----RVe 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1372 ----LLKRNKILVLDEATASI-DSATDAIIqRIIReEFAD--CTVITVAHRVPTVID-SDMVMVL 1428
Cdd:COG3845 152 ilkaLYRGARILILDEPTAVLtPQEADELF-EILR-RLAAegKSIIFITHKLREVMAiADRVTVL 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
624-815 |
1.64e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 55.58 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 624 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQT---------------------SWIQSGT 682
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTkpgpdgrgrakryigilhqeyDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 683 IRDNILYGKPMESRRYNAAIKACALDKdMNGFGHGDLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKAVITLK-MVGFDEEKAEEILDKYPDeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDP 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 762 HTAgVLFHKCVEDSLKE--KTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:TIGR03269 461 ITK-VDVTHSILKAREEmeQTFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDPEEIV 516
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1229-1416 |
1.69e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.30 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1229 RYRPNAPLVLKGISCTFRE-------------GTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIgLKDLR 1295
Cdd:PRK11247 6 RLNQGTPLLLNAVSKRYGErtvlnqldlhipaGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-REDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1296 MKLsiipQEPTLFRGciRTNLD--PLGVYSD--DEIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRV 1371
Cdd:PRK11247 85 LMF----QDARLLPW--KKVIDnvGLGLKGQwrDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALARA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1372 LLKRNKILVLDEATASIDSATDAIIQRII-----REEFadcTVITVAHRV 1416
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIeslwqQHGF---TVLLVTHDV 194
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
622-836 |
1.99e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 54.31 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG-SIAYVSQTSW------IQ------------SG 681
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESPS-QGNVSWRGePLAKLNRAQRkafrrdIQmvfqdsisavnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 TIRDNIlyGKPM----------ESRRYNAAIKACALDKdmngfGHGDlteigQRGINLSGGQKQRIQLARAVYADADVYL 751
Cdd:PRK10419 107 TVREII--REPLrhllsldkaeRLARASEMLRAVDLDD-----SVLD-----KRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 752 LDDPFSAVDAH-TAGVLfhKCVEDsLKEKT---VILVTHQVEFLSEVDQ-ILVMEEGTITQSGKYEELLMMGT-AFQQLV 825
Cdd:PRK10419 175 LDEAVSNLDLVlQAGVI--RLLKK-LQQQFgtaCLFITHDLRLVERFCQrVMVMDNGQIVETQPVGDKLTFSSpAGRVLQ 251
|
250
....*....|.
gi 1063712898 826 NAhndavtVLP 836
Cdd:PRK10419 252 NA------VLP 256
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
632-810 |
2.02e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.66 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 632 GQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQSGTI-RDNILY--------------------- 689
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVtQDDILYphltvretlvfcsllrlpksl 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 690 GKPMESRRYNAAIKACALDKDMNgfghgdlTEIGQ---RGInlSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGV 766
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCEN-------TIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063712898 767 LFHKCVEDSLKEKTVILVTHQVEflSEV----DQILVMEEGTITQSGK 810
Cdd:PLN03211 245 LVLTLGSLAQKGKTIVTSMHQPS--SRVyqmfDSVLVLSEGRCLFFGK 290
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1210-1389 |
2.12e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1210 RPPSSWPsngTIHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKI 1289
Cdd:PRK10522 315 QAFPDWQ---TLELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1290 GLKDLRMKLSIIPQEPTLFRgciRTnLDPLGVYSDDEI---WKALEKCQLKTTISnlpnklDSSVSDegENWSVGQRQLF 1366
Cdd:PRK10522 391 QPEDYRKLFSAVFTDFHLFD---QL-LGPEGKPANPALvekWLERLKMAHKLELE------DGRISN--LKLSKGQKKRL 458
|
170 180
....*....|....*....|...
gi 1063712898 1367 CLGRVLLKRNKILVLDEATASID 1389
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQD 481
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
620-810 |
2.16e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.98 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWIQSgtIRDNI-LYGKPMESRR 697
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtLITSTSKNKDIKQ--IRKKVgLVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 698 YNAAI-KACALDKDMNGFGHGDLTEIGQR-----GIN----------LSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 761
Cdd:PRK13649 99 FEETVlKDVAFGPQNFGVSQEEAEALAREklalvGISeslfeknpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 762 htAG-----VLFHKCVEDSLkekTVILVTHQVEFLSE-VDQILVMEEGTITQSGK 810
Cdd:PRK13649 179 --KGrkelmTLFKKLHQSGM---TIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1237-1389 |
2.26e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 53.56 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI--SKIGLKDLRMKLSIIPQEPTLFR----- 1309
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFYLFPhltal 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1310 -----GCIRTNldplGVYSDDEIWKALE---KCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVL 1381
Cdd:PRK09493 96 envmfGPLRVR----GASKEEAEKQAREllaKVGLAERAHHYPSEL-----------SGGQQQRVAIARALAVKPKLMLF 160
|
....*...
gi 1063712898 1382 DEATASID 1389
Cdd:PRK09493 161 DEPTSALD 168
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
635-778 |
2.26e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 635 VAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVfGS---IAYVSQ---------TSW--IQSGTirDNILYGK-PMESRRYN 699
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvkLAYVDQsrdaldpnkTVWeeISGGL--DIIKVGNrEIPSRAYV 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 700 AAIkacaldkdmnGFGHGDlteigQRGI--NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLfhkcvEDSLK 777
Cdd:PRK11819 430 GRF----------NFKGGD-----QQKKvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRAL-----EEALL 489
|
.
gi 1063712898 778 E 778
Cdd:PRK11819 490 E 490
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1237-1414 |
2.27e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.50 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDL----RMKLSIIPQEPTLFRG-C 1311
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1312 IRTNLDPLGVYSDDEIWKALEKCQ-------LKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEA 1384
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQellqrlgLEDRVEYQPSQL-----------SGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190
....*....|....*....|....*....|.
gi 1063712898 1385 TASIDSATDAIIQRIIRE-EFADCTVITVAH 1414
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQlRDRGHTVIIVTH 202
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
636-815 |
2.39e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.95 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 636 AVCGPVGAGKSSLLHAVLGEIPKVSGtVKVFGSIAYVSQTSWIQSGTI----RDNILYGKP-------MESRRYNAAIKA 704
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRSIFNYRDVLefrrRVGMLFQRPnpfpmsiMDNVLAGVRAHK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 705 CALDKDMNGFGHGDLTEIG----------QRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVL--FHKCV 772
Cdd:PRK14271 130 LVPRKEFRGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIeeFIRSL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063712898 773 EDSLkekTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELL 815
Cdd:PRK14271 210 ADRL---TVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLF 250
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1218-1452 |
2.53e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.24 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1218 NGTIHLQELKIRYRPNAPLVLKGI---SCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG----IDISKIG 1290
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTPFEFKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1291 -LKDLRMKLSIIPQEP--TLFRGCIRTNL--DPLGVYSDDEiwKALEKCQLKTTISNLPNKLDSSVSDEgenWSVGQRQL 1365
Cdd:PRK13645 84 eVKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENKQ--EAYKKVPELLKLVQLPEDYVKRSPFE---LSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1366 FCLGRVLLKRNKILVLDEATASIDSATDA----IIQRIIREEFAdcTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPS 1440
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEdfinLFERLNKEYKK--RIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPF 236
|
250
....*....|..
gi 1063712898 1441 KLMETDSYFSKL 1452
Cdd:PRK13645 237 EIFSNQELLTKI 248
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1223-1389 |
3.25e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.04 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1223 LQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGlKDLRMKLSIIP 1302
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1303 QEPTL---FrgCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenWSVGQRQLFCLGRVLLKRNKIL 1379
Cdd:PRK13537 87 QFDNLdpdF--TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVL 160
|
170
....*....|
gi 1063712898 1380 VLDEATASID 1389
Cdd:PRK13537 161 VLDEPTTGLD 170
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1414 |
3.60e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.55 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1221 IHLQELKIRYRPNAPLVLK---GISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI------------------ 1279
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1280 LIDGIDISKI------GLKDLRMKLSIIPQ--EPTLFRGCIRTNL--DPLGVYSDDEiwKALEKCQLKTTISNLP-NKLD 1348
Cdd:PRK13651 83 VLEKLVIQKTrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSKE--EAKKRAAKYIELVGLDeSYLQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1349 SSVSdegeNWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADC-TVITVAH 1414
Cdd:PRK13651 161 RSPF----ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTH 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1228-1435 |
3.88e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1228 IRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVE--PASGCILIDGIDISKiglkdlrmKLSIIPqep 1305
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR--------EASLID--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1306 tlfrgCIRTNLDPLGV--------YSDDEIWKAlekcqlktTISNLpnkldssvsdegenwSVGQRQLFCLGRVLLKRNK 1377
Cdd:COG2401 105 -----AIGRKGDFKDAvellnavgLSDAVLWLR--------RFKEL---------------STGQKFRFRLALLLAERPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1378 ILVLDEATASIDSATDAIIQRIIREEF--ADCTVITVAHRvPTVIDS---DMVMVLSFGDLVE 1435
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQKLArrAGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1191-1414 |
4.19e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 54.30 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1191 RIKQYMNIPEEPPAIIDDK----RPPSSWPSNGTIHLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLIS 1266
Cdd:COG0488 282 RIKALEKLEREEPPRRDKTveirFPPPERLGKKVLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1267 ALFRLVEPASGCIlidgidisKIGLKdlrMKLSIIPQEptlfrgciRTNLDP-LGVYsdDEIWKALEKCQlKTTISNL-- 1343
Cdd:COG0488 360 LLAGELEPDSGTV--------KLGET---VKIGYFDQH--------QEELDPdKTVL--DELRDGAPGGT-EQEVRGYlg 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1344 -----PNKLDSSVSDegenWSVGQRQLFCLGRVLLKRNKILVLDEAT-----ASIDSATDAIiqriirEEFaDCTVITVA 1413
Cdd:COG0488 418 rflfsGDDAFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTnhldiETLEALEEAL------DDF-PGTVLLVS 486
|
.
gi 1063712898 1414 H 1414
Cdd:COG0488 487 H 487
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
622-815 |
4.73e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 53.31 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTV---------------KVFGSIAYVSQTSWIQ--SGTIR 684
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKLRESVGMVFQDPDNQlfSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 685 DNILYGkPME--------SRRYNAAIKACALDKDMNGFGHGdlteigqrginLSGGQKQRIQLARAVYADADVYLLDDPF 756
Cdd:PRK13636 102 QDVSFG-AVNlklpedevRKRVDNALKRTGIEHLKDKPTHC-----------LSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 757 SAVDAHTAGVLFhKCVEDSLKEK--TVILVTHQVEFLS-EVDQILVMEEGTITQSGKYEELL 815
Cdd:PRK13636 170 AGLDPMGVSEIM-KLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
622-815 |
5.14e-07 |
|
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: 53.52 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPK---VSGTVKVFGS-----------------IAYVSQ---TS-- 676
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEdllklsekelrkirgreIQMIFQdpmTSln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 677 --WiqsgTIRDNIlygkpMESRRYnaaikacaldkdmngfgHGDLT--EIGQR--------GIN------------LSGG 732
Cdd:COG0444 101 pvM----TVGDQI-----AEPLRI-----------------HGGLSkaEARERaiellervGLPdperrldrypheLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 733 QKQRIQLARAVYADADVYLLDDPFSAVDAHT-AGV--LFHKcvedsLKEK---TVILVTHQVEFLSEV-DQILVMEEGTI 805
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIqAQIlnLLKD-----LQRElglAILFITHDLGVVAEIaDRVAVMYAGRI 229
|
250
....*....|
gi 1063712898 806 TQSGKYEELL 815
Cdd:COG0444 230 VEEGPVEELF 239
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1221-1287 |
5.50e-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: 50.52 E-value: 5.50e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 1221 IHLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASG-CILIDGIDIS 1287
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGiVTWGSTVKIG 66
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
628-801 |
7.20e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 628 EIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQtsWI---QSGTIRDnILY--GKPMESRRYNAAI 702
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVED-LLRsiTDDLGSSYYKSEI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 703 kacaldkdMNGFGhgdLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPfSAvdahtagvlfHKCVEDSL----- 776
Cdd:PRK13409 438 --------IKPLQ---LERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEP-SA----------HLDVEQRLavaka 495
|
170 180 190
....*....|....*....|....*....|...
gi 1063712898 777 -------KEKTVILVTHQVEFLSEV-DQILVME 801
Cdd:PRK13409 496 irriaeeREATALVVDHDIYMIDYIsDRLMVFE 528
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
622-826 |
8.07e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQT-SWIQSGTIRDN 686
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaialgIGMVHQHfMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILYGkpMESRR-----YNAAIKacaldkdmngfghgDLTEIGQR-GIN---------LSGGQKQRIQLARAVYADADVYL 751
Cdd:COG3845 101 IVLG--LEPTKggrldRKAARA--------------RIRELSERyGLDvdpdakvedLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 752 LDDPfsavdahTAgVL--------FhkcveDSLKE-----KTVILVTHQvefLSEV----DQILVMEEGTITQSGKYEEL 814
Cdd:COG3845 165 LDEP-------TA-VLtpqeadelF-----EILRRlaaegKSIIFITHK---LREVmaiaDRVTVLRRGKVVGTVDTAET 228
|
250
....*....|....*....
gi 1063712898 815 -------LMMGTAFQQLVN 826
Cdd:COG3845 229 seeelaeLMVGREVLLRVE 247
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
605-815 |
8.22e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 52.32 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 605 DIQVGNFGWEPETKIP----TLRNIHLEIKHGQKVAVCGPVGAGKSSLL------------------HAVLGEIPKVSGT 662
Cdd:PRK13645 6 DIILDNVSYTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIqltngliisetgqtivgdYAIPANLKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 663 VKVFGSIAYVSQTSWIQ--SGTIRDNILYG-------KPMESRRYNAAIKACALDKDMngfghgdlteIGQRGINLSGGQ 733
Cdd:PRK13645 86 KRLRKEIGLVFQFPEYQlfQETIEKDIAFGpvnlgenKQEAYKKVPELLKLVQLPEDY----------VKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 734 KQRIQLARAVYADADVYLLDDPFSAVDAHTAG---VLFHKCVEDslKEKTVILVTHQV-EFLSEVDQILVMEEGTITQSG 809
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKE--YKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIG 233
|
....*.
gi 1063712898 810 KYEELL 815
Cdd:PRK13645 234 SPFEIF 239
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
628-801 |
8.85e-07 |
|
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: 53.63 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 628 EIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQ-TSWIQSGTIRDNI--LYGKPMESRRYNAAIka 704
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQyISPDYDGTVEEFLrsANTDDFGSSYYKTEI-- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 705 caldkdMNGFGhgdLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPfSAvdahtagvlfHKCVEDSL------- 776
Cdd:COG1245 440 ------IKPLG---LEKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEP-SA----------HLDVEQRLavakair 499
|
170 180 190
....*....|....*....|....*....|.
gi 1063712898 777 -----KEKTVILVTHQVEFLSEV-DQILVME 801
Cdd:COG1245 500 rfaenRGKTAMVVDHDIYLIDYIsDRLMVFE 530
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
727-811 |
1.19e-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: 50.26 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 727 INLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA----HTAGVLFHKCVEDslkEKTVILVTHQVEFLSEVDQILVMEE 802
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEEG---KKTALVVEHDLAVLDYLSDRIHVFE 146
|
....*....
gi 1063712898 803 GtitQSGKY 811
Cdd:cd03222 147 G---EPGVY 152
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1236-1402 |
1.25e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1236 LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLR-MKLSIIPQEPtLFRGCIRT 1314
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDR-LGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1315 -----NLDpLGVYSDDEI-------WKALE------------KCQ-LKTTISNLpnkldssvsdegenwSVGQRQLFCLG 1369
Cdd:COG3845 351 msvaeNLI-LGRYRRPPFsrggfldRKAIRafaeelieefdvRTPgPDTPARSL---------------SGGNQQKVILA 414
|
170 180 190
....*....|....*....|....*....|....
gi 1063712898 1370 RVLLKRNKILVLDEATASID-SATDAIIQRIIRE 1402
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDvGAIEFIHQRLLEL 448
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
616-828 |
1.27e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.62 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 616 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIP----KVSGTVKVFGSIAYVSQTSWIQSGTIRDN----- 686
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVAPCALRGRKIATIMQNprsaf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 --------------ILYGKPMESRRYNAAIKACALDkdmngfghgDLTEIGQR-GINLSGGQKQRIQLARAVYADADVYL 751
Cdd:PRK10418 93 nplhtmhtharetcLALGKPADDATLTAALEAVGLE---------NAARVLKLyPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 752 LDDPFSAVDAhTAGVLFHKCVEDSLKEKT--VILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELLMM--GTAFQQLVN 826
Cdd:PRK10418 164 ADEPTTDLDV-VAQARILDLLESIVQKRAlgMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNApkHAVTRSLVS 242
|
..
gi 1063712898 827 AH 828
Cdd:PRK10418 243 AH 244
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1237-1442 |
1.35e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 51.29 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI--------SKIGLKDLRMKLSIIPQEPTLF 1308
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1309 RGciRTNLD-----PL---GVYSDDEIWKA---LEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNK 1377
Cdd:PRK11264 98 PH--RTVLEniiegPVivkGEPKEEATARArelLAKVGLAGKETSYPRRL-----------SGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712898 1378 ILVLDEATASIDSATDAIIQRIIR---EEfaDCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKL 1442
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRqlaQE--KRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
620-806 |
1.40e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRN-IHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWIQSG---------------- 681
Cdd:PRK11288 266 PGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDAIRAGimlcpedrkaegiipv 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 -TIRDNIlygkPMESRRYNAAIKaCALD------------KDMNGFGHGDLTEIGqrgiNLSGGQKQRIQLARAVYADAD 748
Cdd:PRK11288 346 hSVADNI----NISARRHHLRAG-CLINnrweaenadrfiRSLNIKTPSREQLIM----NLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 749 VYLLDDPFSAVDA---HTAGVLFHKCVEDSLkekTVILVTHQvefLSEV----DQILVMEEGTIT 806
Cdd:PRK11288 417 VILLDEPTRGIDVgakHEIYNVIYELAAQGV---AVLFVSSD---LPEVlgvaDRIVVMREGRIA 475
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1238-1435 |
1.49e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD-LRMKLSIIPQE----PTLfrgCI 1312
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1313 RTNL------DPLGVysddeiwkaLEKCQLKTTISNLPNKLDSSVSDEG--ENWSVGQRQLFCLGRVLLKRNKILVLDEA 1384
Cdd:PRK11288 97 AENLylgqlpHKGGI---------VNRRLLNYEAREQLEHLGVDIDPDTplKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1385 TASIDSATDAIIQRIIREEFADCTVIT-VAHRVPTVID-SDMVMVLSFGDLVE 1435
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1226-1319 |
1.58e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 52.76 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1226 LKIRYRPNAPL--VLKGISCTFREGTRVGVVGRTGSGKS-TLISALfRLVEP----ASGCILIDGIDISKIGLKDLR--- 1295
Cdd:COG4172 12 LSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLLGLSERELRrir 90
|
90 100
....*....|....*....|....*
gi 1063712898 1296 -MKLSIIPQEPTlfrgcirTNLDPL 1319
Cdd:COG4172 91 gNRIAMIFQEPM-------TSLNPL 108
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1237-1434 |
1.86e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.33 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDIS--------KIGL--KDlRMKLSIIPQE 1304
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRsprdairaGIAYvpED-RKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1305 PtlfrgcIRTN--------LDPLGVYSDDEIWKALE--------KCQ-LKTTISNLpnkldssvsdegenwSVGQRQLFC 1367
Cdd:COG1129 346 S------IRENitlasldrLSRGGLLDRRRERALAEeyikrlriKTPsPEQPVGNL---------------SGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 1368 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIReEFAD--CTVItvahrvptVIDSDM---------VMVLSFGDLV 1434
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIR-ELAAegKAVI--------VISSELpellglsdrILVMREGRIV 473
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
730-812 |
2.16e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 730 SGGQKQRIQLARAVYADADVYLLDDPFSAVDAHtaGVLFhkcVEDSLKE--KTVILVTHQVEFLSEV--DQILVMEEGTI 805
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLH--AVLW---LETYLLKwpKTFIVVSHAREFLNTVvtDILHLHGQKLV 420
|
....*..
gi 1063712898 806 TQSGKYE 812
Cdd:PLN03073 421 TYKGDYD 427
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1236-1434 |
2.31e-06 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 50.35 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1236 LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPA---SGCILIDGidiskiglkdlrmklsiIPQEPTLFRGCI 1312
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG-----------------QPRKPDQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1313 R------TNLDPLGVYsddEIWkalekcqLKTTISNLPNKLDSSVSDEG-------------------ENWSVGQRQLFC 1367
Cdd:cd03234 84 AyvrqddILLPGLTVR---ETL-------TYTAILRLPRKSSDAIRKKRvedvllrdlaltriggnlvKGISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712898 1368 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIReEFA--DCTVITVAHRvPTvidSDM------VMVLSFGDLV 1434
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLS-QLArrNRIVILTIHQ-PR---SDLfrlfdrILLLSSGEIV 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
621-847 |
2.48e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 621 TLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGT-VKVFGSIAYVS--QTSWIQSGTIRDN---ILYGKPME 694
Cdd:PRK10938 18 TLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErQSQFSHITRLSfeQLQKLVSDEWQRNntdMLSPGEDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 695 SRRYNAAI--------KACA-LDKDmngFGHGDLteIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAG 765
Cdd:PRK10938 98 TGRTTAEIiqdevkdpARCEqLAQQ---FGITAL--LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 766 VLFHKCVEDSLKEKTVILVTHQVEFLSE-VDQILVMEEGTITQSGKYEELLMMgTAFQQLVNAHNDAVTVLP-------- 836
Cdd:PRK10938 173 QLAELLASLHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ-ALVAQLAHSEQLEGVQLPepdepsar 251
|
250
....*....|...
gi 1063712898 837 --LASNESLGDLR 847
Cdd:PRK10938 252 haLPANEPRIVLN 264
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1232-1414 |
3.01e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.86 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1232 PNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISalfrlvepasgciLIDGIDISKIG--LKDLRMKLSIIPQEPTL-- 1307
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAGVDKDFNGeaRPQPGIKVGYLPQEPQLdp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1308 --------FRGC--IRTNLDPL----GVYSD-DEIWKAL--EKCQLKTTIS-----NLPNKL------------DSSVsd 1353
Cdd:TIGR03719 82 tktvrenvEEGVaeIKDALDRFneisAKYAEpDADFDKLaaEQAELQEIIDaadawDLDSQLeiamdalrcppwDADV-- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 1354 egENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIReEFADcTVITVAH 1414
Cdd:TIGR03719 160 --TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ-EYPG-TVVAVTH 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1188-1389 |
3.26e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 50.98 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1188 SVERIKQYMNIPEEPPAIIDDKRPPSSWPSNGTIHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISA 1267
Cdd:PRK13536 9 EAPRRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1268 LFRLVEPASGCILIDGIDI-SKIGLKdlRMKLSIIPQEPTLFRG-CIRTNLDPLGVY---SDDEIWKALEKCqlkTTISN 1342
Cdd:PRK13536 87 ILGMTSPDAGKITVLGVPVpARARLA--RARIGVVPQFDNLDLEfTVRENLLVFGRYfgmSTREIEAVIPSL---LEFAR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063712898 1343 LPNKLDSSVSDegenWSVGQRQLFCLGRVLLKRNKILVLDEATASID 1389
Cdd:PRK13536 162 LESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1237-1439 |
4.04e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.85 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDlrMKLSIIPQEPTLFRGciRTNL 1316
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRH--MTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1317 D--------------PLGVYSDDEIWKALEKCQLkttiSNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLD 1382
Cdd:PRK10851 93 DniafgltvlprrerPNAAAIKAKVTQLLEMVQL----AHLADRYPAQLSG-------GQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 1383 EATASIDSATDAIIQRIIR---EEFaDCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEP 1439
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRqlhEEL-KFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTP 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
620-803 |
4.05e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 620 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIayvsqtswIQSGTIRDNILYGKPM--ESRR 697
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKK--------INNHNANEAINHGFALvtEERR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 698 -----------YNAAIKAcaLDKDMNGFG----------------------HGDLTEIGqrgiNLSGGQKQRIQLARAVY 744
Cdd:PRK10982 334 stgiyayldigFNSLISN--IRNYKNKVGlldnsrmksdtqwvidsmrvktPGHRTQIG----SLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 745 ADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQV-EFLSEVDQILVMEEG 803
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNG 467
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1248-1430 |
4.08e-06 |
|
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: 48.14 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1248 GTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGcirtnldplgvysddei 1327
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1328 wkalekcqlkttisnlpnkldssvsdegenwsVGQRQLFclGRVLLKRNKILVLDEATASIDSATDAIIQRIIR------ 1401
Cdd:smart00382 65 --------------------------------LRLRLAL--ALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180 190
....*....|....*....|....*....|
gi 1063712898 1402 -EEFADCTVITVAHRVPTVIDSDMVMVLSF 1430
Cdd:smart00382 111 lKSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1248-1454 |
4.26e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1248 GTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--ID-ISKIGLKDLRMKLSIIPQEPTlfrgcirTNLDPLGV--Y 1322
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDtLSPGKLQALRRDIQFIFQDPY-------ASLDPRQTvgD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1323 SDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENW------SVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAII 1396
Cdd:PRK10261 423 SIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWryphefSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1397 QRIIREEFADCTV--ITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMETDS--YFSKLVA 1454
Cdd:PRK10261 503 INLLLDLQRDFGIayLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQhpYTRKLMA 565
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
637-824 |
4.47e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.79 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 637 VCGPVG---AGKSSLL------------HAVLGEIPKVSGTVKVFG-SIAYVSQTSWIQSG-TIRDNILYGK-PMESR-- 696
Cdd:PRK10575 39 VTGLIGhngSGKSTLLkmlgrhqppsegEILLDAQPLESWSSKAFArKVAYLPQQLPAAEGmTVRELVAIGRyPWHGAlg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 697 RYNAAIKAcALDKDMNGFGhgdLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVD-AHTAGVLfhKCVED 774
Cdd:PRK10575 119 RFGAADRE-KVEEAISLVG---LKPLAHRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVL--ALVHR 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 775 SLKEK--TVILVTHQVEFLSE-VDQILVMEEGTITQSGKYEElLMMGTAFQQL 824
Cdd:PRK10575 193 LSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAE-LMRGETLEQI 244
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
622-810 |
5.38e-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: 48.47 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEipkvsgtvkvfgsiayvsqtswiqSGTIRDNilygkpmESRRYNAA 701
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA------------------------SGKARLI-------SFLPKFSR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 702 IKACALD--KDMNGFGHGDLTeIGQRGINLSGGQKQRIQLARAVYADAD--VYLLDDPFSAVDAHTAGVLFhKCVEDSLK 777
Cdd:cd03238 60 NKLIFIDqlQFLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLL-EVIKGLID 137
|
170 180 190
....*....|....*....|....*....|....
gi 1063712898 778 EK-TVILVTHQVEFLSEVDQILVMEEGTITQSGK 810
Cdd:cd03238 138 LGnTVILIEHNLDVLSSADWIIDFGPGSGKSGGK 171
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
941-1192 |
8.11e-06 |
|
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: 49.47 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 941 MLIGVYSIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIF 1020
Cdd:cd07346 40 WIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1021 VVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAER 1100
Cdd:cd07346 120 LLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEER 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1101 FFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQNvtLFTCALLLI---LIPKGYIAPGLVGLSLSYALTLTQTQVFLTR 1177
Cdd:cd07346 200 EIERFREANRDLRDANLRAARLSALFSPLIGLLTA--LGTALVLLYggyLVLQGSLTIGELVAFLAYLGMLFGPIQRLAN 277
|
250
....*....|....*
gi 1063712898 1178 WYCTLSNSIISVERI 1192
Cdd:cd07346 278 LYNQLQQALASLERI 292
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1216-1415 |
9.15e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.13 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1216 PSNGTIHLQELKIRYR------PNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLisalFRLVE---PASGCILIdgidi 1286
Cdd:TIGR00954 440 PGRGIVEYQDNGIKFEniplvtPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSL----FRILGelwPVYGGRLT----- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1287 skiglKDLRMKLSIIPQEPTLFRGCIRTNLdplgVY---SDDEIWKALEKCQLKTTISNLpnKLDSSVSDEG-----ENW 1358
Cdd:TIGR00954 511 -----KPAKGKLFYVPQRPYMTLGTLRDQI----IYpdsSEDMKRRGLSDKDLEQILDNV--QLTHILEREGgwsavQDW 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 1359 ----SVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREefADCTVITVAHR 1415
Cdd:TIGR00954 580 mdvlSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1216-1450 |
9.35e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.01 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1216 PSNGT---IHLQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFR---LVEP--ASGCILIDGIDI- 1286
Cdd:PRK14243 3 TLNGTetvLRTENLNVYYGSF--LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1287 -SKIGLKDLRMKLSIIPQEPTLFRGCIRTNL----DPLGVYSD-DE-IWKALEKCQLKTTISNlpnKLDSSvsdeGENWS 1359
Cdd:PRK14243 81 aPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIaygaRINGYKGDmDElVERSLRQAALWDEVKD---KLKQS----GLSLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1360 VGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAH------RVptvidSDMVMVLS---- 1429
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRV-----SDMTAFFNvelt 228
|
250 260 270
....*....|....*....|....*....|..
gi 1063712898 1430 -----FGDLVEYNEPSKLM------ETDSYFS 1450
Cdd:PRK14243 229 egggrYGYLVEFDRTEKIFnspqqqATRDYVS 260
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
587-790 |
1.50e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 587 LKMDEIERSGldasgtAVDIQVGNFGWEPETKIpTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVf 666
Cdd:PRK11147 307 MQVEEASRSG------KIVFEMENVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 667 GS---IAYVSQTSWI--QSGTIRDNILYGK----------------------PMESRrynAAIKAcaldkdmngfghgdl 719
Cdd:PRK11147 379 GTkleVAYFDQHRAEldPEKTVMDNLAEGKqevmvngrprhvlgylqdflfhPKRAM---TPVKA--------------- 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 720 teigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLfhkcvEDSLKE--KTVILVTHQVEF 790
Cdd:PRK11147 441 ---------LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELL-----EELLDSyqGTVLLVSHDRQF 499
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1172-1396 |
1.80e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1172 QVFLTRWYCTLSNSIISVERIKQYMNIPEEPPAIIDDK-----RPPSSWPsNGTIHLQELKIRYrpNAPLVLKGISCTFR 1246
Cdd:PRK10636 260 QSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPfhfsfRAPESLP-NPLLKMEKVSAGY--GDRIILDSIKLNLV 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1247 EGTRVGVVGRTGSGKSTLISALFRLVEPASGCI-LIDGIdiskiglkdlrmKLSIIPQEPTLFrgcIRTNLDPLGVYSDD 1325
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI------------KLGYFAQHQLEF---LRADESPLQHLARL 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 1326 EIwKALEKcQLKTTISNLPNKLDsSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASID-----SATDAII 1396
Cdd:PRK10636 402 AP-QELEQ-KLRDYLGGFGFQGD-KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDldmrqALTEALI 474
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
636-813 |
1.99e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.72 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 636 AVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-----------------IAYVSQTSWI-QSGTIRDNILYG-KPMESR 696
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDARLfPHYKVRGNLRYGmAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 697 RYNAAIKACALDKDMNGFGhgdlteigqrgINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDahtagvLFHK-----C 771
Cdd:PRK11144 108 QFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD------LPRKrellpY 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063712898 772 VEDSLKE-KTVIL-VTHQV-EFLSEVDQILVMEEGTITQSGKYEE 813
Cdd:PRK11144 171 LERLAREiNIPILyVSHSLdEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
622-803 |
2.18e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWIQSG--------------TIRDN 686
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqEMRFASTTAALAAGvaiiyqelhlvpemTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILYGK-PMesrrynaaiKACALD-KDMNGFGHGDLTEIG------QRGINLSGGQKQRIQLARAVYADADVYLLDDPFSA 758
Cdd:PRK11288 100 LYLGQlPH---------KGGIVNrRLLNYEAREQLEHLGvdidpdTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063712898 759 VDAHTAGVLFhKCVEDSLKEKTVIL-VTHQVEflsEV----DQILVMEEG 803
Cdd:PRK11288 171 LSAREIEQLF-RVIRELRAEGRVILyVSHRME---EIfalcDAITVFKDG 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
613-814 |
2.20e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.16 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 613 WEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSW------IQ------ 679
Cdd:PRK15079 28 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkDLLGMKDDEWravrsdIQmifqdp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 680 ------SGTIRDNI----------LYGKPMESRRYNAAIKACALDKDMNGFGHgdlteigqrgiNLSGGQKQRIQLARAV 743
Cdd:PRK15079 108 laslnpRMTIGEIIaeplrtyhpkLSRQEVKDRVKAMMLKVGLLPNLINRYPH-----------EFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 744 YADADVYLLDDPFSAVDahtagVLFHKCVEDSLKE------KTVILVTHQ---VEFLSevDQILVMEEGTITQSGKYEEL 814
Cdd:PRK15079 177 ILEPKLIICDEPVSALD-----VSIQAQVVNLLQQlqremgLSLIFIAHDlavVKHIS--DRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
618-814 |
2.21e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--------SIAYVSQTSWIQSGTIRDN--- 686
Cdd:PRK10261 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrQVIELSEQSAAQMRHVRGAdma 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILYGKPM--------------ESRRYNAAI---KACALDKDMNgfghgDLTEIGQRGI-------NLSGGQKQRIQLARA 742
Cdd:PRK10261 108 MIFQEPMtslnpvftvgeqiaESIRLHQGAsreEAMVEAKRML-----DQVRIPEAQTilsryphQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 743 VYADADVYLLDDPFSAVDAH-TAGVLFHKCVEDSLKEKTVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEEL 814
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTiQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIaDRVLVMYQGEAVETGSVEQI 256
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1221-1287 |
2.64e-05 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 48.17 E-value: 2.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712898 1221 IHLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIS 1287
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT 70
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
729-800 |
2.79e-05 |
|
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: 45.81 E-value: 2.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712898 729 LSGGQKQRIQLARAV----YADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEVDQILVM 800
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
618-755 |
3.00e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.18 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 618 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEiPKVSGtvkvfGSIAYVSQ--TSWIQSGTIRDNILY---GKP 692
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATS-----GRIVFDGKdiTDWQTAKIMREAVAIvpeGRR 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 693 MESR---RYNAAIKACALDKDMNGFGHGDLTEI--------GQRGINLSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:PRK11614 91 VFSRmtvEENLAMGGFFAERDQFQERIKWVYELfprlherrIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1237-1310 |
3.89e-05 |
|
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: 46.37 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISAL--FRLVEPASGCILIDGIDIskiglKDL------RMKLSIIPQEPTLF 1308
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDI-----TDLppeeraRLGIFLAFQYPPEI 89
|
..
gi 1063712898 1309 RG 1310
Cdd:cd03217 90 PG 91
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
289-578 |
4.91e-05 |
|
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: 47.16 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 289 IFIAVFAFLRTFAVVSLPLMLYVFVDYANSdHRDLRNGFFNLACLVMLKLVESLT--MRHWYFAsrRSGMRIRSALMVAA 366
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIP-AGDLSLLLWIALLLLLLALLRALLsyLRRYLAA--RLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 367 YKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWW-FHSGWSLSLQLLLSTAVLF------GVVGAGAFPGLILLLLC 439
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILFylnwklTLVALLLLPLYVLILRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 440 gllnlpFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMS 519
Cdd:cd07346 159 ------FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 520 PTIVSSVVFL-GCALLKSAPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 578
Cdd:cd07346 233 TALGTALVLLyGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
622-816 |
5.23e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWIQSG--------------TIRDN 686
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkEIDFKSSKEALENGismvhqelnlvlqrSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 687 ILYGK-PM------ESRRYNAAIKACA-LDKDMNGfghgdlteiGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSA 758
Cdd:PRK10982 94 MWLGRyPTkgmfvdQDKMYRDTKAIFDeLDIDIDP---------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712898 759 VDAHTAGVLFHkcVEDSLKEK--TVILVTHQVEFLSEV-DQILVMEEGTITQSGKYEELLM 816
Cdd:PRK10982 165 LTEKEVNHLFT--IIRKLKERgcGIVYISHKMEEIFQLcDEITILRDGQWIATQPLAGLTM 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1217-1419 |
7.35e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.41 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1217 SNGTIHLQELKIRYRpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLrm 1296
Cdd:PRK15056 3 QQAGIVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1297 kLSIIPQE-------PTLFRGCIRtnldpLGVYSDD---EIWKALEKCQLKTTISNLpNKLDSSVSDEGEnWSVGQRQLF 1366
Cdd:PRK15056 80 -VAYVPQSeevdwsfPVLVEDVVM-----MGRYGHMgwlRRAKKRDRQIVTAALARV-DMVEFRHRQIGE-LSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 1367 CLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFAD-CTVITVAHRVPTV 1419
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSV 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1236-1440 |
7.37e-05 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 45.69 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1236 LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIskIGLKDLRMKLSIIPQEPTLFrgcirtn 1315
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALF------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1316 ldP-LGVY------------SDDEIWK----ALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKI 1378
Cdd:cd03300 85 --PhLTVFeniafglrlkklPKAEIKErvaeALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1379 LVLDEATasidSATDAIIQRIIREEFAD------CTVITVAHrvptviD-------SDMVMVLSFGDLVE-------YNE 1438
Cdd:cd03300 152 LLLDEPL----GALDLKLRKDMQLELKRlqkelgITFVFVTH------DqeealtmSDRIAVMNKGKIQQigtpeeiYEE 221
|
..
gi 1063712898 1439 PS 1440
Cdd:cd03300 222 PA 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
729-814 |
7.65e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 729 LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEK-TVILVTHQVEFLSEV-DQILVMEEGTIT 806
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEAaHKIIVMYAGQVV 233
|
....*...
gi 1063712898 807 QSGKYEEL 814
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
729-815 |
1.14e-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: 46.60 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 729 LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHT-AGVLfhkcveDSLKE------KTVILVTHQ---VEFLSevDQIL 798
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVqAQIL------DLLRDlqrehgLAYLFISHDlavVRALA--HRVM 497
|
90
....*....|....*..
gi 1063712898 799 VMEEGTITQSGKYEELL 815
Cdd:COG4172 498 VMKDGKVVEQGPTEQVF 514
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1246-1427 |
1.15e-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: 46.70 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1246 REGTRVGVVGRTGSGKSTLISALFRLVEPASGCIlidgidiskiglkDLRMKLSIIPQ--EP-------TLFRGCIRTNL 1316
Cdd:COG1245 364 REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQyiSPdydgtveEFLRSANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1317 DplGVYSDDEIWKALekcqlkttisNLPNKLDSSVSDegenWSVGQRQLFCLGRVLLKRNKILVLDEATASIDS----AT 1392
Cdd:COG1245 431 G--SSYYKTEIIKPL----------GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAV 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063712898 1393 DAIIQRIIREEfaDCTVITVAHRVpTVID--SDMVMV 1427
Cdd:COG1245 495 AKAIRRFAENR--GKTAMVVDHDI-YLIDyiSDRLMV 528
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
622-859 |
1.22e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSI--AYVSQtswiqsgtirDNILYGKPMES---- 695
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIklGYFAQ----------HQLEFLRADESplqh 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 696 -RRYNAAIKACALDKDMNGFG-HGD-LTEIGQRginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCV 772
Cdd:PRK10636 398 lARLAPQELEQKLRDYLGGFGfQGDkVTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 773 EdslKEKTVILVTHQVEFL-SEVDQILVMEEGTITQ-SGKYEELLMMGTAFQQLVNAHNDAvtvlPLASNESLGDLRKEG 850
Cdd:PRK10636 475 D---FEGALVVVSHDRHLLrSTTDDLYLVHDGKVEPfDGDLEDYQQWLSDVQKQENQTDEA----PKENNANSAQARKDQ 547
|
250
....*....|.
gi 1063712898 851 KDR--EIRNMT 859
Cdd:PRK10636 548 KRReaELRTQT 558
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1223-1445 |
1.28e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1223 LQELKIRYRPNAPL--VLKGISCTFREGTRVGVVGRTGSGKS-TLISALFRLVEPA----SGCILIDGIDISKIGLKDLR 1295
Cdd:PRK15134 8 IENLSVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1296 M----KLSIIPQEPTLfrgcirtNLDPL---------------GVYSD---DEIWKALEKC---QLKTTISNLPNKLdss 1350
Cdd:PRK15134 88 GvrgnKIAMIFQEPMV-------SLNPLhtlekqlyevlslhrGMRREaarGEILNCLDRVgirQAAKRLTDYPHQL--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1351 vsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVID-SDMVMV 1427
Cdd:PRK15134 158 --------SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqQELNMGLLFITHNLSIVRKlADRVAV 229
|
250
....*....|....*...
gi 1063712898 1428 LSFGDLVEYNEPSKLMET 1445
Cdd:PRK15134 230 MQNGRCVEQNRAATLFSA 247
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
622-806 |
1.37e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.87 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGeIPKVSGTVKVFG-----------------SIAYVSQTS-WIQSGTI 683
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-IERPSAGKIWFSghditrlknrevpflrrQIGMIFQDHhLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 684 RDN-----ILYGKPMES--RRYNAAI-KACALDKDMNgfghgdlteigqRGINLSGGQKQRIQLARAVYADADVYLLDDP 755
Cdd:PRK10908 97 YDNvaiplIIAGASGDDirRRVSAALdKVGLLDKAKN------------FPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 756 FSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEVD-QILVMEEGTIT 806
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
920-1105 |
1.53e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 45.23 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 920 FQAASTYWLAFAIGIPKITNTMLI-GVYSIISTLSAGF-VYARAITTAHLGLKASKAFFSgftnAVFKAPMLFFDSTPVG 997
Cdd:cd18572 18 YTGAVIDAVVADGSREAFYRAVLLlLLLSVLSGLFSGLrGGCFSYAGTRLVRRLRRDLFR----SLLRQDIAFFDATKTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 998 RILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQ----VIIIALLALAATKVVQDYYlasaRELIRINGT 1073
Cdd:cd18572 94 ELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRltllAFITVPVIALITKVYGRYY----RKLSKEIQD 169
|
170 180 190
....*....|....*....|....*....|...
gi 1063712898 1074 TKApVMNYAAETSLGVV-TIRAFGTAERFFKNY 1105
Cdd:cd18572 170 ALA-EANQVAEEALSNIrTVRSFATEEREARRY 201
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
718-791 |
1.56e-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: 45.05 E-value: 1.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712898 718 DLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH---TAGVLFHKCVEDslkEKTVILVTHQVEFL 791
Cdd:cd03236 128 ELRHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAED---DNYVLVVEHDLAVL 202
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1249-1270 |
1.82e-04 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 45.53 E-value: 1.82e-04
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
939-1108 |
1.85e-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: 45.24 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 939 NTMLIGVYsIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAf 1018
Cdd:cd18568 42 NLILIGLL-IVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSA- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1019 IFVVAPAVELTAALLIMTYVTWQ----VIIIALLALAATKVVQDYYLASARELIRingtTKAPVMNYAAETSLGVVTIRA 1094
Cdd:cd18568 120 LTTILDLLMVFIYLGLMFYYNLQltliVLAFIPLYVLLTLLSSPKLKRNSREIFQ----ANAEQQSFLVEALTGIATIKA 195
|
170
....*....|....
gi 1063712898 1095 FGTAERFFKNYLNL 1108
Cdd:cd18568 196 LAAERPIRWRWENK 209
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
941-1192 |
1.99e-04 |
|
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: 45.07 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 941 MLIGVYSIISTLSAGFVYARAITTAHLGLKA-----SKAFfsgftNAVFKAPMLFFDSTPVGRILTRASSD--------- 1006
Cdd:cd18544 42 LLALLYLGLLLLSFLLQYLQTYLLQKLGQRIiydlrRDLF-----SHIQRLPLSFFDRTPVGRLVTRVTNDtealnelft 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1007 ---LNVLDYDVPFAFIFVVAPAVELTAALL------IMTYVTWqviiiallalAATKVVQDYYLAsARELI-RINGttka 1076
Cdd:cd18544 117 sglVTLIGDLLLLIGILIAMFLLNWRLALIsllvlpLLLLATY----------LFRKKSRKAYRE-VREKLsRLNA---- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1077 pvmnYAAETSLGVVTIRAFGTAERFFKNYLNLVDAdavlFFLSNAAMEWV--ILR--IETLQNVTLftcALLL----ILI 1148
Cdd:cd18544 182 ----FLQESISGMSVIQLFNREKREFEEFDEINQE----YRKANLKSIKLfaLFRplVELLSSLAL---ALVLwyggGQV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1063712898 1149 PKGYIAPGLVglslsYALTLTQTQVF-----LTRWYCTLSNSIISVERI 1192
Cdd:cd18544 251 LSGAVTLGVL-----YAFIQYIQRFFrpirdLAEKFNILQSAMASAERI 294
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1238-1453 |
2.01e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIS-KIGLKDLRMKLSIIPQEPTLFRGciRTNL 1316
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQ--RSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1317 DP--LGVYSDDEIWKALEKCQLKTtiSNLPNKLDSSVS--DEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSAT 1392
Cdd:PRK10982 92 DNmwLGRYPTKGMFVDQDKMYRDT--KAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712898 1393 DAIIQRIIRE-EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEyNEPSKLMETDSYFSKLV 1453
Cdd:PRK10982 170 VNHLFTIIRKlKERGCGIVYISHKMEEIFQlCDEITILRDGQWIA-TQPLAGLTMDKIIAMMV 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1237-1397 |
2.57e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 44.42 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLK---DLR-MKLSIIPQEPTLFRGCi 1312
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRnQKLGFIYQFHHLLPDF- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1313 rTNLD----PL---GVYSDDEIWKALEKCQ---LKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLD 1382
Cdd:PRK11629 103 -TALEnvamPLligKKKPAEINSRALEMLAavgLEHRANHRPSEL-----------SGGERQRVAIARALVNNPRLVLAD 170
|
170
....*....|....*.
gi 1063712898 1383 EATASIDSAT-DAIIQ 1397
Cdd:PRK11629 171 EPTGNLDARNaDSIFQ 186
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
615-803 |
2.87e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 615 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHA---------VLGEIpKVSGTVKV---FGSIA-YVSQTSwIQSG 681
Cdd:PLN03140 889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVlagrktggyIEGDI-RISGFPKKqetFARISgYCEQND-IHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 --TIRDNILYGK----PMESRRYNaaiKACALDKDMNGFGHGDLTE--IGQRGIN-LSGGQKQRIQLARAVYADADVYLL 752
Cdd:PLN03140 967 qvTVRESLIYSAflrlPKEVSKEE---KMMFVDEVMELVELDNLKDaiVGLPGVTgLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 753 DDPFSAVDAHTAGVLFhKCVEDSLKE-KTVILVTHQ--VEFLSEVDQILVMEEG 803
Cdd:PLN03140 1044 DEPTSGLDARAAAIVM-RTVRNTVDTgRTVVCTIHQpsIDIFEAFDELLLMKRG 1096
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
730-760 |
3.41e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.57 E-value: 3.41e-04
10 20 30
....*....|....*....|....*....|.
gi 1063712898 730 SGGQKQRIQLARAVYADADVYLLDDPFSAVD 760
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
679-843 |
3.60e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 679 QSGTIRDNI-LYGKPMESRRYNAAIKAcalDKDMNGFghgDLTEI-GQRGINLSGGQKQRIQLARAVYADADVYLLDDPF 756
Cdd:NF000106 99 ESFSGRENLyMIGR*LDLSRKDARARA---DELLERF---SLTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 757 SAVDAHTAGVLFHKcVEDSLKEKTVILVTHQveFLSEVDQ----ILVMEEGTITQSGKYEEL------------------ 814
Cdd:NF000106 173 TGLDPRTRNEVWDE-VRSMVRDGATVLLTTQ--YMEEAEQlaheLTVIDRGRVIADGKVDELktkvggrtlqirpahaae 249
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063712898 815 --LMMGTAFQQLVNA-------HNDAVTVLPLASNESL 843
Cdd:NF000106 250 ldRMVGAIAQAGLDGiagatadHEDGVVNVPIVSDEQL 287
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1237-1414 |
4.53e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 43.61 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKI---GLKDLRMK--------LSIIP--- 1302
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhvgfvfqsFMLIPtln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1303 -----QEPTLFRGCIRTNldplgvySDDEIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNK 1377
Cdd:PRK10584 105 alenvELPALLRGESSRQ-------SRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063712898 1378 ILVLDEATASIDSAT-DAIIQRI--IREEFAdCTVITVAH 1414
Cdd:PRK10584 167 VLFADEPTGNLDRQTgDKIADLLfsLNREHG-TTLILVTH 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
729-842 |
5.61e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.46 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 729 LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQVEFLSEV-DQILVMEEGTITQ 807
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEIsDAVYVLRQGQILT 216
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1063712898 808 SGKYEELLMMGTAFQQ-------LVNAHndAVTVLPLASNES 842
Cdd:PRK13638 217 HGAPGEVFACTEAMEQagltqpwLVKLH--TQLGLPLCKTET 256
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
629-786 |
5.91e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 629 IKHGQKVAVCGPVGAGKSSLLHAVLGE-IP----------------KVSGT-------------VKVFGSIAYVSQTSWI 678
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGElIPnlgdyeeepswdevlkRFRGTelqnyfkklyngeIKVVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 679 QSGTIRDniLYGKPMESRRYNAAIKACALDKDMNgfghgdlteigqRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFS 757
Cdd:PRK13409 176 FKGKVRE--LLKKVDERGKLDEVVERLGLENILD------------RDIsELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063712898 758 AVD-------AhtagvlfhKCVEDSLKEKTVILVTH 786
Cdd:PRK13409 242 YLDirqrlnvA--------RLIRELAEGKYVLVVEH 269
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1238-1452 |
1.32e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.11 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1238 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPA---SGCILIDGIdisKIGLKDLRMKLSIIPQE----PTL--- 1307
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM---PIDAKEMRAISAYVQQDdlfiPTLtvr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1308 ----FRGCIRTnldPLGVYSD------DEIWKA--LEKCQlkTTISNLPNKLDSsvsdegenWSVGQRQLFCLGRVLLKR 1375
Cdd:TIGR00955 118 ehlmFQAHLRM---PRRVTKKekrervDEVLQAlgLRKCA--NTRIGVPGRVKG--------LSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 1376 NKILVLDEATASIDSATDAIIQRIIReEFAD--CTVITVAHRVPTVIDS--DMVMVLSFGDLVEYNEPSKLMEtdsYFSK 1451
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLK-GLAQkgKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVP---FFSD 260
|
.
gi 1063712898 1452 L 1452
Cdd:TIGR00955 261 L 261
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
622-798 |
1.61e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.22 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 622 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVL---------------GEIPKVSGTVKVfGSIAYVSQ-----TSWIQSG 681
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEGLEHI-DKVIVIDQspigrTPRSNPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 682 T-------IRDniLYGKPMESRRYNA---AIK------ACALD--------------------KDMNGFGHGDLTeIGQR 725
Cdd:cd03271 90 TytgvfdeIRE--LFCEVCKGKRYNRetlEVRykgksiADVLDmtveealeffenipkiarklQTLCDVGLGYIK-LGQP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 726 GINLSGGQKQRIQLARAVYADAD---VYLLDDPfsavdahTAGVLFH---KCVE--DSLKEK--TVILVTHQVEFLSEVD 795
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKRSTgktLYILDEP-------TTGLHFHdvkKLLEvlQRLVDKgnTVVVIEHNLDVIKCAD 239
|
...
gi 1063712898 796 QIL 798
Cdd:cd03271 240 WII 242
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1237-1285 |
1.90e-03 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 42.06 E-value: 1.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGID 1285
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD 65
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1250-1270 |
2.31e-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: 2.31e-03
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
639-798 |
3.36e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.67 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 639 GPVGAGKSSLLHAVL----GEIPKvsgtvkvfGSIAYVSQTSWIQSGTIRDNI------LYGKPMESRRYNAAIKACAld 708
Cdd:cd03240 29 GQNGAGKTTIIEALKyaltGELPP--------NSKGGAHDPKLIREGEVRAQVklafenANGKKYTITRSLAILENVI-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 709 kdmngFGH-GDLTEIGQRGI-NLSGGQKQ------RIQLARAVYADADVYLLDDPFSAVDA-HTAGVLfHKCVEDSLKEK 779
Cdd:cd03240 99 -----FCHqGESNWPLLDMRgRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESL-AEIIEERKSQK 172
|
170 180
....*....|....*....|.
gi 1063712898 780 T--VILVTHQVEFLSEVDQIL 798
Cdd:cd03240 173 NfqLIVITHDEELVDAADHIY 193
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1237-1307 |
4.71e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 4.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712898 1237 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASG-CILIDGIdisKIGlkdlrmklsIIPQEPTL 1307
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGI---KVG---------YLPQEPQL 81
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
630-760 |
4.82e-03 |
|
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: 41.31 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 630 KHGQKVAVCGPVGAGKSSLLHAVLGE-IP----------------------------KVS-GTVKVFGSIAYVSQTSWIQ 679
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGElKPnlgdydeepswdevlkrfrgtelqdyfkKLAnGEIKVAHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 680 SGTIRDniLYGKPMESRRYNAAIKACALDKDMNgfghgdlteigqRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSA 758
Cdd:COG1245 177 KGTVRE--LLEKVDERGKLDELAEKLGLENILD------------RDIsELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
..
gi 1063712898 759 VD 760
Cdd:COG1245 243 LD 244
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
1252-1271 |
6.34e-03 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 38.48 E-value: 6.34e-03
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
929-1005 |
7.66e-03 |
|
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: 40.19 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712898 929 AFAIGIPKIT-----NTMLIGVYSIISTLSAG----------FVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDS 993
Cdd:cd18555 16 LLTLLIPILTqyvidNVIVPGNLNLLNVLGIGililfllyglFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFEN 95
|
90
....*....|..
gi 1063712898 994 TPVGRILTRASS 1005
Cdd:cd18555 96 RSSGDLLFRANS 107
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
939-1002 |
9.97e-03 |
|
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: 39.74 E-value: 9.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712898 939 NTMLIGVySIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTR 1002
Cdd:cd18570 42 NIISIGL-ILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISR 104
|
|
| |
