|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
187-1432 |
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: 813.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 187 LSDPLLTKNPRKESarlaTAGFFSILSFSWMNPLLSLGFKKPLSPEDIPSVVPEDEAQLAYKKFSQAW------------ 254
Cdd:TIGR00957 192 FSETNHDPNPCPES----SASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWkkeckktrkqpv 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 255 ------------------------DTLLGdESSTKERN-LVFRAVVKVYFKENIFIAVFAFLRTFAVVSLPLMLYVFVDY 309
Cdd:TIGR00957 268 savygkkdpskpkgssqldaneevEALIV-KSPHKPRKpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRF 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 310 ANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYKKQLKLSSLGRKRHSSGEIVNYIAVDAY 389
Cdd:TIGR00957 347 VNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 390 RMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKMLQNCQTQFMIAQDKRLRSTSEILNSM 469
Cdd:TIGR00957 427 RFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGI 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 470 KVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVF-LGCALLKSAPLNASTIFTVLATLRVM 548
Cdd:TIGR00957 507 KVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFaVYVTVDENNILDAEKAFVSLALFNIL 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 549 SEPVKIIPDAISAIIQGNVSFQRLNNFLLDDELKMDEIERSGL-DASGTAVDIQVGNFGWePETKIPTLRNIHLEIKHGQ 627
Cdd:TIGR00957 587 RFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIkPGEGNSITVHNATFTW-ARDLPPTLNGITFSIPEGA 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 628 KVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNG 707
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEI 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 708 FGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCV--EDSLKEKTVILVTHQ---- 781
Cdd:TIGR00957 746 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGisyl 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 782 -------VMEEGTITQSGKYEELLMMGTAFQQLVNAHndavtvlplASNESLGDLRKEGKDREIRNMTVVEKIEEEIEKT 854
Cdd:TIGR00957 826 pqvdviiVMSGGKISEMGSYQELLQRDGAFAEFLRTY---------APDEQQGHLEDSWTALVSGEGKEAKLIENGMLVT 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 855 DIPGVQ------------------------------------LTQEEEKESGYVGMKPFLDYIGvSRGWCLLWSSVLGQV 898
Cdd:TIGR00957 897 DVVGKQlqrqlsasssdsgdqsrhhgssaelqkaeakeetwkLMEADKAQTGQVELSVYWDYMK-AIGLFITFLSIFLFV 975
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 899 GFVVFQAASTYWLAFAIGIPKITNT-----MLIGVYSIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLF 973
Cdd:TIGR00957 976 CNHVSALASNYWLSLWTDDPMVNGTqnntsLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSF 1055
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 974 FDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQDYYLASARELIRI 1053
Cdd:TIGR00957 1056 FERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRL 1135
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1054 NGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQN-VTLFtcALLLILIP 1132
Cdd:TIGR00957 1136 ESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNcIVLF--AALFAVIS 1213
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1133 KGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYMNIPEEPPAIIDDKRPPSSWPSNGTIHLQELKIR 1212
Cdd:TIGR00957 1214 RHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLR 1293
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1213 YRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFR 1292
Cdd:TIGR00957 1294 YREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFS 1373
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1293 GCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASID 1372
Cdd:TIGR00957 1374 GSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1373 SATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYF 1432
Cdd:TIGR00957 1454 LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-1436 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 788.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 27 IAFVNLLFLCIFYLFLIASCVSTH-FIVRGRKKGWIFVAVAICCAITSFIFLGVGLNSL-IHGGNDVTEISWVACFVEGI 104
Cdd:PLN03130 41 ISHLVLLGLCLYRIWLIKKDHKVQrFCLRSKWYNYFLALLAAYCTAEPLFRLVMGISVLnLDGQTSLPPFEIVSLIVEAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 105 IWVSLAVSLLVNGSKWVNILVsvWWVSFALLDLVAKSGILLQ---------GNGIRILDILTLPMSLLLLLCSWMNLRS- 174
Cdd:PLN03130 121 TWCSMLVMIGVETKIYIREFR--WYVRFAVIYVLVGDAVMLNlvlsvkeyySSFVLYLYISEVAAQVLFGILLLVYFPNl 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 175 -----SSAAAQDCSVTGLSDPLLTKN---PRKEsarlatAGFFSILSFSWMNPLLSLGFKKPLSPEDIPSVVPEDEAQLA 246
Cdd:PLN03130 199 dpypgYTPIGSESVDDYEYEELPGGEqicPERH------ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 247 YKKFSQAWDtllgdESSTKERNLVFRAVVKVYFKENIFIAVFAFLRTFAVVSLPLMLyvfvdyaNSDHRDLRNG-----F 321
Cdd:PLN03130 273 YRSFQKCWD-----EELKKPKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLL-------NLLLESMQNGepawiG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 322 FNLACLVMLKLVESLTMRHWYFAS-RRSGMRIRSALMVAAYKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHS 400
Cdd:PLN03130 341 YIYAFSIFVGVVLGVLCEAQYFQNvMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 401 GWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDE 480
Cdd:PLN03130 421 LWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENS 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 481 FKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVFlGCALLKSAPLNASTIFTVLATLRVMSEPVKIIPDAIS 560
Cdd:PLN03130 501 FQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSF-GVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLIT 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 561 AIIQGNVSFQRLNNFLLDDELKMdeIERSGLDASGTAVDIQVGNFGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKS 640
Cdd:PLN03130 580 QAVNANVSLKRLEELLLAEERVL--LPNPPLEPGLPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKT 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 641 SLLHAVLGEIPKVS-GTVKVFGSIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQR 719
Cdd:PLN03130 658 SLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGER 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 720 GINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQV-----------MEEGTI 788
Cdd:PLN03130 738 GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLhflsqvdriilVHEGMI 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 789 TQSGKYEELLMMGTAFQQLV-NAHNDAVTVlplASNESLGDLRKEGKDREIRNMTVVEKIEEEIEKTDIPGVQLTQEEEK 867
Cdd:PLN03130 818 KEEGTYEELSNNGPLFQKLMeNAGKMEEYV---EENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEER 894
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 868 ESGYVGMKPFLDYIGVSRGWCLLWSSVLGQVGFVVFQAASTYWLAFAI--GIPKITNTML-IGVYSIIS------TLSAG 938
Cdd:PLN03130 895 ETGVVSWKVLERYKNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTdqGTPKTHGPLFyNLIYALLSfgqvlvTLLNS 974
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 939 FVYaraITTAhlgLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDV-PFAFIFVVAPAVELTAALLI 1017
Cdd:PLN03130 975 YWL---IMSS---LYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVaVFVNMFLGQIFQLLSTFVLI 1048
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1018 ---MTYVTWQVIIIALLALaatkVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDA 1094
Cdd:PLN03130 1049 givSTISLWAIMPLLVLFY----GAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDN 1124
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1095 DAVLFFLSNAAMEWVILRIETLQNVTLFTCALLLILI------PKGYiAPgLVGLSLSYALTLTQTQVFLTRWYCTLSNS 1168
Cdd:PLN03130 1125 NIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQngraenQAAF-AS-TMGLLLSYALNITSLLTAVLRLASLAENS 1202
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1169 IISVERIKQYMNIPEEPPAIIDDKRPPSSWPSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLI 1248
Cdd:PLN03130 1203 LNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSML 1282
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1249 SALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPN 1328
Cdd:PLN03130 1283 NALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSL 1362
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1329 KLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMV 1408
Cdd:PLN03130 1363 GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRI 1442
|
1450 1460
....*....|....*....|....*....
gi 334185504 1409 MVLSFGDLVEYNEPSKLMETD-SYFSKLV 1436
Cdd:PLN03130 1443 LVLDAGRVVEFDTPENLLSNEgSAFSKMV 1471
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-1436 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 757.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 32 LLFLCIFYLFLIASCVS-THFIVRGRKKGWIFVAVAICCAITSF--IFLGVGLNSLiHGGNDVTEISWVACFVEGIIWVS 108
Cdd:PLN03232 46 LLGLCFYRIWIILDNAKaQIYVLRKKYYNCVLGILACYCVVEPVlrLVMGISLFDM-DEETDLPPFEVASLMVEAFAWFS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 109 LAVSLLVNGSKWVNILVsvWWVSFALLDLVAKSGILLQgngiRILDILTLPMSLLLLLCswMNLRSSSA----------- 177
Cdd:PLN03232 125 MLVLIGLETKQYVKEFR--WYVRFGVVYVLVADAVLLD----LVLPLKNSINRTALYLC--ISSRCCQAlfgilllvyip 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 178 AAQDCSVTGLSDPLLTKNPRKESARLAT-------AGFFSILSFSWMNPLLSLGFKKPLSPEDIPSVVPEDEAQLAYKKF 250
Cdd:PLN03232 197 ELDPYPGYHILNNESLDNVEYDALRGGEnicperyASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 251 SQAWDtllgdESSTKERNLVFRAVVKVYFKENIFIAVFAFLRTFAVVSLPLMLYVFVdyansdhRDLRNG-----FFNLA 325
Cdd:PLN03232 277 QRCWT-----EESRRPKPWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLL-------QSMQEGdpawvGYVYA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 326 CLVMLKLVESLTMRHWYFAS-RRSGMRIRSALMVAAYKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSL 404
Cdd:PLN03232 345 FLIFFGVTFGVLCESQYFQNvGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 405 SLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKK 484
Cdd:PLN03232 425 PFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESR 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 485 IESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVFlGCALLKSAPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQ 564
Cdd:PLN03232 505 IQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSF-GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVN 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 565 GNVSFQRLNNFLLDDELKMdeIERSGLDASGTAVDIQVGNFGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLH 644
Cdd:PLN03232 584 ANVSLQRIEELLLSEERIL--AQNPPLQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLIS 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 645 AVLGEIPKVSGT-VKVFGSIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINL 723
Cdd:PLN03232 662 AMLGELSHAETSsVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNI 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 724 SGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQV-----------MEEGTITQSG 792
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLhflplmdriilVSEGMIKEEG 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 793 KYEELLMMGTAFQQL------------VNAHNDAV-----TVLPLASNESLGDLRKEGKDREIrnmtvvekieeeiektd 855
Cdd:PLN03232 822 TFAELSKSGSLFKKLmenagkmdatqeVNTNDENIlklgpTVTIDVSERNLGSTKQGKRGRSV----------------- 884
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 856 ipgvqLTQEEEKESGYVGMKPFLDYIGVSRGwclLWSSVLGQVGFV---VFQAASTYWLAFAIGIPKITN---TMLIGVY 929
Cdd:PLN03232 885 -----LVKQEERETGIISWNVLMRYNKAVGG---LWVVMILLVCYLtteVLRVSSSTWLSIWTDQSTPKSyspGFYIVVY 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 930 SIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVP----------- 998
Cdd:PLN03232 957 ALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVAnlmnmfmnqlw 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 999 -----FAFIFVVApAVELTA--ALLIMTYVTWQviiiallalaatkvvqdYYLASARELIRINGTTKAPVMNYAAETSLG 1071
Cdd:PLN03232 1037 qllstFALIGTVS-TISLWAimPLLILFYAAYL-----------------YYQSTSREVRRLDSVTRSPIYAQFGEALNG 1098
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1072 VVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQNVTLFTCALLLIL----IPKGYIAPGLVGLSLSY 1147
Cdd:PLN03232 1099 LSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLrngnAENQAGFASTMGLLLSY 1178
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1148 ALTLTQTQVFLTRWYCTLSNSIISVERIKQYMNIPEEPPAIIDDKRPPSSWPSNGTIHLQELKIRYRPNAPLVLKGISCT 1227
Cdd:PLN03232 1179 TLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFF 1258
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1228 FREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDPLGVYSD 1307
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHND 1338
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1308 DEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEF 1387
Cdd:PLN03232 1339 ADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEF 1418
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|
gi 334185504 1388 ADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETD-SYFSKLV 1436
Cdd:PLN03232 1419 KSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDtSAFFRMV 1468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
288-1436 |
7.25e-179 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 575.19 E-value: 7.25e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 288 FAFLRTFAVVSLPLMLYVFVDYANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYKKQLKL 367
Cdd:PTZ00243 252 FKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCGLQYRSALNALIFEKCFTI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 368 S--SLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKMLQ 445
Cdd:PTZ00243 332 SskSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQM 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 446 NCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVFLGC 525
Cdd:PTZ00243 412 AARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVFTVY 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 526 ALLKSApLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRLNNFLLDDEL------KMDEIERSGLDASGTA-- 597
Cdd:PTZ00243 492 YLLGHE-LTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNAtcstvqDMEEYWREQREHSTACql 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 598 ------VDIQV------------------------------------------------------------GNFGWEPET 611
Cdd:PTZ00243 571 aavlenVDVTAfvpvklprapkvktsllsralrmlcceqcrptkrhpspsvvvedtdygspssasrhivegGTGGGHEAT 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPT---------------------LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTS 670
Cdd:PTZ00243 651 PTSErsaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQA 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 671 WIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPF 750
Cdd:PTZ00243 731 WIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 751 SAVDAHTAGVLFHKCVEDSLKEKTVILVTHQV-----------MEEGTITQSGKYEElLMMGTAFQQL------------ 807
Cdd:PTZ00243 811 SALDAHVGERVVEECFLGALAGKTRVLATHQVhvvpradyvvaLGDGRVEFSGSSAD-FMRTSLYATLaaelkenkdske 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 808 --VNAHNDAVTVLP-----LASNESLGDLRKEGKDreirnmtvvekieeeIEKTDIPGVQLTQEEEKESGYVGMKPFLDY 880
Cdd:PTZ00243 890 gdADAEVAEVDAAPggavdHEPPVAKQEGNAEGGD---------------GAALDAAAGRLMTREEKASGSVPWSTYVAY 954
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 881 IGVSRGWClLWSSVLgqVGFVV---FQAASTYWLA-FAIGIPKITNTMLIGVYSIISTLSAGFVYARAITTAHLGLKASK 956
Cdd:PTZ00243 955 LRFCGGLH-AAGFVL--ATFAVtelVTVSSGVWLSmWSTRSFKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSR 1031
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 957 AFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAAT 1036
Cdd:PTZ00243 1032 NMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLY 1111
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1037 KVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETL 1116
Cdd:PTZ00243 1112 YRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFL 1191
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1117 QNVTLFTCALLLI---LIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM-NIPEEP------- 1185
Cdd:PTZ00243 1192 SNIVVTVIALIGVigtMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDmpeldee 1271
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1186 ----------------PAIIDDKRPPSSWPSN---GTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKST 1246
Cdd:PTZ00243 1272 vdalerrtgmaadvtgTVVIEPASPTSAAPHPvqaGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKST 1351
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1247 LISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNL 1326
Cdd:PTZ00243 1352 LLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASE 1431
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1327 PNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVL-DEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDS 1405
Cdd:PTZ00243 1432 SEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQY 1511
|
1290 1300 1310
....*....|....*....|....*....|..
gi 334185504 1406 DMVMVLSFGDLVEYNEPSKL-METDSYFSKLV 1436
Cdd:PTZ00243 1512 DKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
203-1449 |
1.39e-144 |
|
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: 480.18 E-value: 1.39e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 203 LATAGFFSILSFSWMNPLLSLGFKKPLSPEDIPSVVPEDEAQLAYKKFSQAWDTLLgdeSSTKERNLVFRAVVKVYFKEN 282
Cdd:TIGR01271 6 VEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDREL---ASAKKNPKLLNALRRCFFWRF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 283 IFIAVFAFLRTFAVVSLPLMLYVFVDYANSDHRDLRNGFFNLAC-LVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAY 361
Cdd:TIGR01271 83 VFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALgLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 362 KKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFA 441
Cdd:TIGR01271 163 KKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 442 KMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVV 521
Cdd:TIGR01271 243 QKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 522 FLGCALLKSAPLNasTIFTVLATLRVMSEPV-KIIPDAISAIIQGNVSFQRLNNFLLDDELKM-------DEIERSGLDA 593
Cdd:TIGR01271 323 VVPYALIKGIILR--RIFTTISYCIVLRMTVtRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTleynlttTEVEMVNVTA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 594 S-------------------GTA---VDIQVGNFGWEpetKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIP 651
Cdd:TIGR01271 401 SwdegigelfekikqnnkarKQPngdDGLFFSNFSLY---VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 652 KVSGTVKVFGSIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRI 731
Cdd:TIGR01271 478 PSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARI 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 732 QLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEEL--- 797
Cdd:TIGR01271 558 SLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKlehlkkadkilLLHEGVCYFYGTFSELqak 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 798 ------LMMGT---------------------------------------AFQQ-------------LVNAHN------- 812
Cdd:TIGR01271 638 rpdfssLLLGLeafdnfsaerrnsiltetlrrvsidgdstvfsgpetikqSFKQpppefaekrkqsiILNPIAsarkfsf 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 813 --------------DAV---------------------------------------TVLPLASNESLGDLRKEGKDREIR 839
Cdd:TIGR01271 718 vqmgpqkaqattieDAVrepserkfslvpedeqgeeslprgnqyhhglqhqaqrrqSVLQLMTHSNRGENRREQLQTSFR 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 840 NMTVVEKIEEEIEKTDIPGVQLTQE-------------------EEKESGYV--GMKPFLDYIGVSRG--WCLLWSSVLg 896
Cdd:TIGR01271 798 KKSSITQQNELASELDIYSRRLSKDsvyeiseeineedlkecfaDERENVFEttTWNTYLRYITTNRNlvFVLIFCLVI- 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 897 qvgFVVFQAASTYWLAFAIGIPKITNTM---------LIGVYSIIST------------------LSAGFVyaRAITTAH 949
Cdd:TIGR01271 877 ---FLAEVAASLLGLWLITDNPSAPNYVdqqhanassPDVQKPVIITptsayyifyiyvgtadsvLALGFF--RGLPLVH 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 950 LGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAF-------------IFVVA---PAVELTA 1013
Cdd:TIGR01271 952 TLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLfdfiqltlivlgaIFVVSvlqPYIFIAA 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1014 ALLIMTYVtwqviiiallalaatkVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTA---ERFFKNYLN 1090
Cdd:TIGR01271 1032 IPVAVIFI----------------MLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQsyfETLFHKALN 1095
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1091 LVDADavlFFLSNAAMEWVILRIETLqnVTLFTCALLLILIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSII 1170
Cdd:TIGR01271 1096 LHTAN---WFLYLSTLRWFQMRIDII--FVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMR 1170
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1171 SVERIKQYMNIPEEPPA--------------IIDDKRPPSSWPSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGV 1236
Cdd:TIGR01271 1171 SVSRVFKFIDLPQEEPRpsggggkyqlstvlVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGL 1250
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1237 VGRTGSGKSTLISALFRLVEpASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEK 1316
Cdd:TIGR01271 1251 LGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEE 1329
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1317 CQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVA 1396
Cdd:TIGR01271 1330 VGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSE 1409
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 1397 HRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLV-----AEYWASCRGNSSQ 1449
Cdd:TIGR01271 1410 HRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMsaadrLKLFPLHRRNSSK 1467
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1202-1422 |
1.68e-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: 1.68e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1202 GTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1281
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKI 1361
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 1362 LVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEP 1422
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
598-782 |
6.69e-99 |
|
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: 315.18 E-value: 6.69e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 598 VDIQVGNFGWEPE--TKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQSG 675
Cdd:cd03250 1 ISVEDASFTWDSGeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180
....*....|....*....|....*...
gi 334185504 756 HTAGVLFHKCVEDSLKE-KTVILVTHQV 782
Cdd:cd03250 161 HVGRHIFENCILGLLLNnKTRILVTHQL 188
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1198-1422 |
2.26e-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: 2.26e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1198 WPSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDL 1277
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1278 RMKLSIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALekcqlkttisnlpnkldsSVSDEGENWSVGQRQLFCLGRVLLK 1357
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1358 RNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEP 1422
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
874-1437 |
2.33e-88 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 299.77 E-value: 2.33e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 874 MKPFLDYIGVSRGWCLLwsSVLGQVGFVVFQAASTYWLAFAI--GIPKITNT---MLIGVYSIISTLSAGFVYARAITTA 948
Cdd:COG1132 9 LRRLLRYLRPYRGLLIL--ALLLLLLSALLELLLPLLLGRIIdaLLAGGDLSallLLLLLLLGLALLRALLSYLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 949 HLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQ---- 1024
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRlali 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1025 ----VIIIALLALAATKVVQDYYLASARELIRINGttkapvmnYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFF 1100
Cdd:COG1132 167 vllvLPLLLLVLRLFGRRLRKLFRRVQEALAELNG--------RLQESLSGIRVVKAFGREERELERFREANEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1101 LSNAAMEWVILRIETLQNV-TLFTCALLLILIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1179
Cdd:COG1132 239 RAARLSALFFPLMELLGNLgLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1180 nipEEPPAIIDDKRPPSSWPSNGTIHLQELKIRYRPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPAS 1259
Cdd:COG1132 319 ---DEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1260 GCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDpLGV--YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDE 1337
Cdd:COG1132 395 GRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR-YGRpdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1338 GENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLV 1417
Cdd:COG1132 474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
570 580
....*....|....*....|
gi 334185504 1418 EYNEPSKLMETDSYFSKLVA 1437
Cdd:COG1132 554 EQGTHEELLARGGLYARLYR 573
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
898-1438 |
2.12e-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: 289.43 E-value: 2.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 898 VGFVVFQAASTYWLAFAIGIpkitntmligvySIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDST 977
Cdd:COG2274 183 IDRVLPNQDLSTLWVLAIGL------------LLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 978 PVGRILTRASSDLNVLD----------YDVPFAFIFVV-----APAVELTAALLIMTYVTWqviiiallalaaTKVVQDY 1042
Cdd:COG2274 251 SVGDLASRFRDVESIREfltgslltalLDLLFVLIFLIvlffySPPLALVVLLLIPLYVLL------------GLLFQPR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1043 YLASARELIRINGTtkapVMNYAAETSLGVVTIRAFGTAERFFKNYLNL----VDADAVLFFLSNAAMEWVILrIETLQN 1118
Cdd:COG2274 319 LRRLSREESEASAK----RQSLLVETLRGIETIKALGAESRFRRRWENLlakyLNARFKLRRLSNLLSTLSGL-LQQLAT 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1119 VTLFTCALLLILipKGYIAPG-------LVGLSLSYALTLTQtqvFLTRWYctlsNSIISVERIKQYMNIPEEPPAIIDD 1191
Cdd:COG2274 394 VALLWLGAYLVI--DGQLTLGqliafniLSGRFLAPVAQLIG---LLQRFQ----DAKIALERLDDILDLPPEREEGRSK 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1192 KRPPsswPSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISK 1271
Cdd:COG2274 465 LSLP---RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1272 IGLKDLRMKLSIIPQEPTLFRGCIRTNL---DPLgvYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQL 1348
Cdd:COG2274 542 IDPASLRRQIGVVLQDVFLFSGTIRENItlgDPD--ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1349 FCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMET 1428
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
570
....*....|
gi 334185504 1429 DSYFSKLVAE 1438
Cdd:COG2274 700 KGLYAELVQQ 709
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1202-1436 |
1.31e-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: 1.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1202 GTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1281
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKI 1361
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 1362 LVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLM-ETDSYFSKLV 1436
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
284-572 |
3.21e-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: 3.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 284 FIAVFAFLRTFAVVSLPLMLYVFVDYANSDHR-DLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYK 362
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDePLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 363 KQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAK 442
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 443 MLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVF 522
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 334185504 523 LGCALLKSaPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 572
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 ... |
886-1179 |
2.48e-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: 235.09 E-value: 2.48e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 886 GWCLLWSSVLGQVGFVVFQAASTYWLAFAIGIPKITNTMLIGVYSIISTL-SAGFVYARAITTAHLGLKASKAFFSGFTN 964
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLaSVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 965 AVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQDYYL 1044
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1045 ASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQNVTLFTC 1124
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1125 ALLLILIPkGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1179
Cdd:cd18580 241 ALLAVLLR-SSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
271-811 |
2.71e-64 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 230.05 E-value: 2.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 271 FRAVVKVYFKENIFIAVFAFLRTFAVVSLPLMLYVFVDYAnSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGM 350
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDAL-LAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 351 RIRSALMVAAYKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWW-FHSGWSLSLQLLLSTAVLF------GVVGAGA 423
Cdd:COG1132 91 RVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLFvidwrlALIVLLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 424 FPglilllLCGLLNLPFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEF-TWLAKAQLT 502
Cdd:COG1132 171 LP------LLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRrANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 503 KAFGSFLYWMSPTIVSSVVFLGCALLKSAPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRLNNfLLDDELK 582
Cdd:COG1132 245 ALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE-LLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 583 MDEIERsGLDASGTAVDIQVGN--FGWEPETkiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVF 660
Cdd:COG1132 324 IPDPPG-AVPLPPVRGEIEFENvsFSYPGDR--PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 661 G-------------SIAYVSQTSWIQSGTIRDNILYGKPMESR-RYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGG 726
Cdd:COG1132 401 GvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPDATDeEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 727 QKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKcVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYE 795
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-LERLMKGRTTIVIAHRlstirnadrilVLDDGRIVEQGTHE 559
|
570
....*....|....*.
gi 334185504 796 ELLMMGTAFQQLVNAH 811
Cdd:COG1132 560 ELLARGGLYARLYRLQ 575
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1071-1429 |
3.50e-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: 220.40 E-value: 3.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1071 GVVTIRAFGTAERffknYLNLVDADA---------VL--FFLSNAAMEW----------VILRIETLQ-NVTLFTCALLL 1128
Cdd:COG4988 206 GLTTLKLFGRAKA----EAERIAEASedfrkrtmkVLrvAFLSSAVLEFfaslsialvaVYIGFRLLGgSLTLFAALFVL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1129 ILIPKGYiAPgLVGLSLSYALTLtqtqvfltrwyctlsNSIISVERIkqyMNIPEEPPAIIDDKRPPSSWPSNGTIHLQE 1208
Cdd:COG4988 282 LLAPEFF-LP-LRDLGSFYHARA---------------NGIAAAEKI---FALLDAPEPAAPAGTAPLPAAGPPSIELED 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1209 LKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEP 1288
Cdd:COG4988 342 VSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNP 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1289 TLFRGCIRTNLDpLG--VYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDE 1366
Cdd:COG4988 421 YLFAGTIRENLR-LGrpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDE 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1367 ATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETD 1429
Cdd:COG4988 500 PTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1202-1427 |
4.95e-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: 4.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1202 GTIHLQELKIRYRPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1281
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEK-CQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNK 1360
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKeAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1361 ILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLME 1427
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1204-1411 |
3.14e-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: 189.52 E-value: 3.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1283
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLFRGCIRTNLdplgvysddeiwkalekcqlkttisnlpnkldssvsdegenWSVGQRQLFCLGRVLLKRNKILV 1363
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 334185504 1364 LDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVL 1411
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVL 167
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
980-1437 |
3.28e-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: 199.99 E-value: 3.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 980 GRILTRASSDLNVLDYdvpfAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQ-------DYYLA--SAREL 1050
Cdd:COG4987 112 GDLLNRLVADVDALDN----LYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAglllpllAARLGrrAGRRL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1051 IRINGTTKApvmnYAAETSLGVVTIRAFGTAERFF-------KNYLNLVDADAVLFFLSNAAMEWVilrietlqnVTLFT 1123
Cdd:COG4987 188 AAARAALRA----RLTDLLQGAAELAAYGALDRALarldaaeARLAAAQRRLARLSALAQALLQLA---------AGLAV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1124 CALLLILIP---KGYIAP------GLVGLSLSYALT-LTQTQVFLTRwyctlsnSIISVERIKQymnIPEEPPAIIDDKR 1193
Cdd:COG4987 255 VAVLWLAAPlvaAGALSGpllallVLAALALFEALApLPAAAQHLGR-------VRAAARRLNE---LLDAPPAVTEPAE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1194 PPSSwPSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG 1273
Cdd:COG4987 325 PAPA-PGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1274 LKDLRMKLSIIPQEPTLFRGCIRTNL---DPLGvySDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFC 1350
Cdd:COG4987 404 EDDLRRRIAVVPQRPHLFDTTLRENLrlaRPDA--TDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLA 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1351 LGRVLLKRNKILVLDEATASIDSAT-DAIIQRiIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETD 1429
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATeQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
....*...
gi 334185504 1430 SYFSKLVA 1437
Cdd:COG4987 561 GRYRQLYQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1213-1435 |
3.41e-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: 3.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1213 YRPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFR 1292
Cdd:cd03253 10 YDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1293 GCIRTNLDplgvY-----SDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEA 1367
Cdd:cd03253 89 DTIGYNIR----YgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 1368 TASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKL 1435
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
890-1435 |
3.13e-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: 197.25 E-value: 3.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 890 LWSSVLGQVGFVVFQAASTYWLAFaigIPKITNTMLIGVY-SIISTLSAGFV-------YARAITTAHLGlKASKAFFSG 961
Cdd:TIGR02203 13 KAGLVLAGVAMILVAATESTLAAL---LKPLLDDGFGGRDrSVLWWVPLVVIglavlrgICSFVSTYLLS-WVSNKVVRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 962 FTNAVF----KAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATK 1037
Cdd:TIGR02203 89 IRVRMFekllGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1038 VVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFG----TAERF-FKNYLNLVDA----------DAVLFFLS 1102
Cdd:TIGR02203 169 ILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGgqayETRRFdAVSNRNRRLAmkmtsagsisSPITQLIA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1103 NAAMEWVIlrietlqnvtlftcALLLILIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYMNIP 1182
Cdd:TIGR02203 249 SLALAVVL--------------FIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1183 EEPPaiiDDKRPPSSwpSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI 1262
Cdd:TIGR02203 315 PEKD---TGTRAIER--ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1263 LIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNL--DPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGEN 1340
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIayGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1341 WSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYN 1420
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
|
570
....*....|....*
gi 334185504 1421 EPSKLMETDSYFSKL 1435
Cdd:TIGR02203 550 THNELLARNGLYAQL 564
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1202-1437 |
8.45e-53 |
|
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: 186.98 E-value: 8.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1202 GTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEpASGCILIDGIDISKIGLKDLRMKL 1281
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKI 1361
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 1362 LVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLVA 1437
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; ... |
887-1179 |
1.23e-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: 187.29 E-value: 1.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 887 WCLLWSSVLGQVGFVVFQaasTYWLAF-------AIGIPKITNTML--IGVYSIISTLSAGFVYARAITTAHLGLKASKA 957
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQ---SWWLGIwasayetSSALPPSEVSVLyyLGIYALISLLSVLLGTLRYLLFFFGSLRASRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 958 FFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATK 1037
Cdd:cd18604 78 LHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1038 VVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQ 1117
Cdd:cd18604 158 YIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLG 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 1118 NVTLFTCALLLILIPKgyIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1179
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, ... |
890-1179 |
3.08e-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: 3.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 890 LWSSVLGQVGFVVFQAASTYWLAF-------AIGIPKITNTMLIGVYSIISTLSAGFVYARAITTAHLGLKASKAFFSGF 962
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEwsddpalNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 963 TNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQDY 1042
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1043 YLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQNVTLF 1122
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1123 TCALLLIlIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1179
Cdd:cd18603 241 FAALFAV-LSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1204-1436 |
5.94e-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: 5.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRY--RPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1281
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPTLFRGCIRTNLDpLGVYS--DDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRN 1359
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIR-YGKPDatDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1360 KILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLV 1436
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1204-1435 |
3.67e-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: 3.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1283
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLFRGCIRTNLdplgVY-----SDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKR 1358
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1359 NKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKL 1435
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
614-782 |
3.97e-51 |
|
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: 182.36 E-value: 3.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQSGTIRDNILYGKPMESRRYN 693
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 694 AAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEK 773
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANK 210
|
....*....
gi 334185504 774 TVILVTHQV 782
Cdd:cd03291 211 TRILVTSKM 219
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
286-572 |
6.21e-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: 6.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 286 AVFAFLRTFAVVSLPLMLYVFVDYANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYKKQL 365
Cdd:cd18595 3 ALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 366 KLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKMLQ 445
Cdd:cd18595 83 RLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 446 NCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVFLGC 525
Cdd:cd18595 163 KLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 334185504 526 ALLKSAP-LNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 572
Cdd:cd18595 243 VLSDPDNvLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
598-782 |
1.97e-50 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 177.91 E-value: 1.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 598 VDIQVGNFGWEPEtkIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTV-----------------KVF 660
Cdd:cd03290 1 VQVTNGYFSWGSG--LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 661 GSIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYAD 740
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 334185504 741 ADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKE--KTVILVTHQV 782
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKL 202
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
964-1418 |
3.81e-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: 3.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 964 NAVFKAPMLFFDSTPVGRILTRASSDLNVLDyDVpfaFIFVVAP---AVELTAALLI-MTYVTWQVIIIALLALAATKVV 1039
Cdd:PRK10790 106 DAALRQPLSAFDTQPVGQLISRVTNDTEVIR-DL---YVTVVATvlrSAALIGAMLVaMFSLDWRMALVAIMIFPAVLVV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1040 QDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNylnlvdadavlffLSNAAMEWVILRIETLQ-- 1117
Cdd:PRK10790 182 MVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGER-------------MGEASRSHYMARMQTLRld 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1118 ------NVTLFT----CALLLILipkGYIAPGLVGLSLSYALT-----LTQTQVFLTRWYCTLSNSIISVERIKQYMNIP 1182
Cdd:PRK10790 249 gfllrpLLSLFSalilCGLLMLF---GFSASGTIEVGVLYAFIsylgrLNEPLIELTTQQSMLQQAVVAGERVFELMDGP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1183 EEPPAiiDDKRPPSSwpsnGTIHLQELKIRYRPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI 1262
Cdd:PRK10790 326 RQQYG--NDDRPLQS----GRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1263 LIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLdPLGV-YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENW 1341
Cdd:PRK10790 399 RLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANV-TLGRdISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNL 477
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1342 SVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVE 1418
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
887-1179 |
7.50e-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: 179.26 E-value: 7.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 887 WCLLWSSVLGQVGfvvfQAASTYWLAFAI--------GIPKITNTMLIGVYSIISTLSAGFVYARAITTAHLGLKASKAF 958
Cdd:cd18605 2 ILILLSLILMQAS----RNLIDFWLSYWVshsnnsffNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 959 FSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKV 1038
Cdd:cd18605 78 HNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1039 VQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQN 1118
Cdd:cd18605 158 IQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1119 VTLFTCAL--LLILIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1179
Cdd:cd18605 238 LIVTFVALtaVVQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
856-1436 |
2.98e-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: 2.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 856 IPGVQLTQEEEKESGY-VGMKPFLDYIGVSRGW-----CLLWSSVLGQVGFVVFQAASTYWLAFAIGIPKITNTM-LIGV 928
Cdd:TIGR00958 130 SAGASEKEAEQGQSETaDLLFRLLGLSGRDWPWlisafVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIfFMCL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 929 YSIISTLSAGFvyaRA----ITTAHLGLKASKAFFSgftnAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFV 1004
Cdd:TIGR00958 210 LSIASSVSAGL---RGgsfnYTMARINLRIREDLFR----SLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1005 VAPAVELTAALLIMTYVTWQVIIIALLAL----AATKVVQDYYLASARELIriNGTTKApvmNYAAETSLGVV-TIRAFG 1079
Cdd:TIGR00958 283 LRNLVMLLGLLGFMLWLSPRLTMVTLINLplvfLAEKVFGKRYQLLSEELQ--EAVAKA---NQVAEEALSGMrTVRSFA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1080 TAERFFKNY---------LNLVDADAVLFFLsnaameWVILRIETLQNVTLFTCALLLILipKGYIAPGLVGLSLSYALT 1150
Cdd:TIGR00958 358 AEEGEASRFkealeetlqLNKRKALAYAGYL------WTTSVLGMLIQVLVLYYGGQLVL--TGKVSSGNLVSFLLYQEQ 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1151 LTQTQVFLTRWYCTLSNSIISVERIKQYMNipeeppaiiddkRPPSSWPS--------NGTIHLQELKIRY--RPNAPlV 1220
Cdd:TIGR00958 430 LGEAVRVLSYVYSGMMQAVGASEKVFEYLD------------RKPNIPLTgtlaplnlEGLIEFQDVSFSYpnRPDVP-V 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLD 1300
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1301 -PLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATasidSATDAII 1379
Cdd:TIGR00958 577 yGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT----SALDAEC 652
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1380 QRIIRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLV 1436
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 ... |
894-1179 |
1.23e-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: 169.58 E-value: 1.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 894 VLGQVGFVVFQAASTYWLAFAIG-IPKITNTMLIGVYSIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPML 972
Cdd:cd18606 5 LLLLILSQFAQVFTNLWLSFWTEdFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 973 FFDSTPVGRILTRASSDLNVLDYDVP----------------FAFIFVVAPAVELTAALLIMTYVtwqviiiallalaat 1036
Cdd:cd18606 85 FFDTTPLGRILNRFSKDTDVLDNELPdslrmflytlssiigtFILIIIYLPWFAIALPPLLVLYY--------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1037 kVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETL 1116
Cdd:cd18606 150 -FIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1117 QNVTLFTCALLLIlIPKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1179
Cdd:cd18606 229 GSLLVLIVALLCV-TRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
557-798 |
4.62e-46 |
|
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: 175.72 E-value: 4.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 557 DAISAiiqgnvsFQRLNNFLLDDELKMDEIERSGLDASGTAVDIQVGNFGWEPETkiPTLRNIHLEIKHGQKVAVCGPVG 636
Cdd:COG4988 303 NGIAA-------AEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 637 AGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDNILYGKPMESR-RYNAAIKACALD 702
Cdd:COG4988 374 AGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRPDASDeELEAALEAAGLD 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 703 KDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKcVEDSLKEKTVILVTHQ- 781
Cdd:COG4988 454 EFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRl 532
|
250 260
....*....|....*....|....*..
gi 334185504 782 ----------VMEEGTITQSGKYEELL 798
Cdd:COG4988 533 allaqadrilVLDDGRIVEQGTHEELL 559
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
530-807 |
5.57e-46 |
|
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: 175.72 E-value: 5.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 530 SAPLNASTIFTVLAtlrvMSEPVKIIPDAISAIIQGNVSFQRLNNfLLDDELKMDEIERSGLDASGTAVDIQVGNFGWeP 609
Cdd:COG4987 271 SGPLLALLVLAALA----LFEALAPLPAAAQHLGRVRAAARRLNE-LLDAPPAVTEPAEPAPAPGGPSLELEDVSFRY-P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 610 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGT 676
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTT 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 677 IRDNILYGKPMES-RRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:COG4987 425 LRENLRLARPDATdEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDA 504
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 756 HTAGVLFHKcVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQL 807
Cdd:COG4987 505 ATEQALLAD-LLEALAGRTVLLITHRlaglermdrilVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1183-1418 |
9.05e-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: 9.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1183 EEPPAIIDDKRPPSSWPSNGTIHLQELKIRYRPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI 1262
Cdd:COG5265 337 DQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1263 LIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLdplgVY-----SDDEIWKALEKCQLKTTISNLPNKLDSSVSDE 1337
Cdd:COG5265 416 LIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGER 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1338 GENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLV 1417
Cdd:COG5265 492 GLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIV 571
|
.
gi 334185504 1418 E 1418
Cdd:COG5265 572 E 572
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
271-809 |
4.62e-45 |
|
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: 175.41 E-value: 4.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 271 FRAVVKVYFKENIFIAVFAFLRTFAVVSLPLMLYVFVDYAnsdhrdLRNGFFNL-----ACLVMLKLVESL--TMRHWYF 343
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRV------LPNQDLSTlwvlaIGLLLALLFEGLlrLLRSYLL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 344 --ASRRSGMRIRSALMvaayKKQLKLSSLGRKRHSSGEIVNYIAvDAYRMGEFLwwfhSGWSLSLQLLLSTAVLFGVV-- 419
Cdd:COG2274 221 lrLGQRIDLRLSSRFF----RHLLRLPLSFFESRSVGDLASRFR-DVESIREFL----TGSLLTALLDLLFVLIFLIVlf 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 420 ---------GAGAFPGLILLLLCgllnlpFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIEScrd 490
Cdd:COG2274 292 fyspplalvVLLLIPLYVLLGLL------FQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWEN--- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 491 deftwLAKAQLTKAFGSFLYWMSPTIVSS---------VVFLGCALLKSAPLN-----ASTIFTVLATLRVMSepvkiIP 556
Cdd:COG2274 363 -----LLAKYLNARFKLRRLSNLLSTLSGllqqlatvaLLWLGAYLVIDGQLTlgqliAFNILSGRFLAPVAQ-----LI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 557 DAISAIIQGNVSFQRLNNFL-LDDElkmDEIERSGLDASGTAVDIQVGN--FGWEPETKiPTLRNIHLEIKHGQKVAVCG 633
Cdd:COG2274 433 GLLQRFQDAKIALERLDDILdLPPE---REEGRSKLSLPRLKGDIELENvsFRYPGDSP-PVLDNISLTIKPGERVAIVG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 634 PVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDNILYGKPMESR-RYNAAIKAC 699
Cdd:COG2274 509 RSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPDATDeEIIEAARLA 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 700 ALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAgvlfhKCVEDSLKE----KTV 775
Cdd:COG2274 589 GLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE-----AIILENLRRllkgRTV 663
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 334185504 776 ILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQLVN 809
Cdd:COG2274 664 IIIAHRlstirladriiVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1204-1437 |
7.23e-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: 7.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1283
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLFRGCIRTNL---DPlgVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNK 1360
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1361 ILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLVA 1437
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; ... |
284-572 |
8.12e-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: 8.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 284 FIAVFAFLRTFAVVSLPLMLYVFVDY-ANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYK 362
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYlEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 363 KQLKL-------------------SSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGA 423
Cdd:cd18596 81 KALRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 424 FPGLILLLLCGLLNLPFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTK 503
Cdd:cd18596 161 LVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLD 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 504 AFGSFLYWMSPTIVSSVVFLGCALLKSAPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 572
Cdd:cd18596 241 LLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1202-1417 |
7.82e-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: 7.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1202 GTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1281
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPTLFRGCIRTNLDPLGVYSDDE-IWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNK 1360
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDErILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 1361 ILVLDEATASIDSATDA-IIQRiIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLV 1417
Cdd:cd03245 161 ILLLDEPTSAMDMNSEErLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1071-1437 |
5.99e-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: 5.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1071 GVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQnvtLFTCALLLILIPKGYIAPGL-VGLSLSYAL 1149
Cdd:TIGR03797 323 GISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLP---VLTSAALFAAAISLLGGAGLsLGSFLAFNT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1150 TLTQTQVFLTRwyctLSNSIISV-------ERIKQymnIPEEPPAIIDDKRPPSswPSNGTIHLQELKIRYRPNAPLVLK 1222
Cdd:TIGR03797 400 AFGSFSGAVTQ----LSNTLISIlaviplwERAKP---ILEALPEVDEAKTDPG--KLSGAIEVDRVTFRYRPDGPLILD 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1223 GISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDPL 1302
Cdd:TIGR03797 471 DVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGG 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1303 GVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATasidSATDAIIQRI 1382
Cdd:TIGR03797 551 APLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEAT----SALDNRTQAI 626
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1383 IREEFA--DCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLVA 1437
Cdd:TIGR03797 627 VSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
604-786 |
2.56e-39 |
|
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: 144.06 E-value: 2.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 604 NFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTS 670
Cdd:cd03228 7 SFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 671 WIQSGTIRDNIlygkpmesrrynaaikacaldkdmngfghgdlteigqrginLSGGQKQRIQLARAVYADADVYLLDDPF 750
Cdd:cd03228 86 FLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 334185504 751 SAVDAHTAgVLFHKCVEDSLKEKTVILVTHQ-----------VMEEG 786
Cdd:cd03228 125 SALDPETE-ALILEALRALAKGKTVIVIAHRlstirdadriiVLDDG 170
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
894-1179 |
2.63e-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: 2.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 894 VLGQVGFVVFQAASTYWLA-------------FAIGIPKITN---TMLIGVYSIISTLSAGFVYARAITTAHLGLKASKA 957
Cdd:cd18602 5 LALALLKQGLRVATDFWLAdwteanhdvasvvFNITSSSLEDdevSYYISVYAGLSLGAVILSLVTNLAGELAGLRAARR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 958 FFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATK 1037
Cdd:cd18602 85 LHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1038 VVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQ 1117
Cdd:cd18602 165 FLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLG 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1118 NVTLFTCALLLILIPK-GYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1179
Cdd:cd18602 245 AVIVFLAALSSLTAALaGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1183-1411 |
6.85e-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: 6.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1183 EEPPAIIDDKRPpSSWPSNGTIHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI 1262
Cdd:TIGR02857 302 DAAPRPLAGKAP-VTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1263 LIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLD-PLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENW 1341
Cdd:TIGR02857 380 AVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRlARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGL 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1342 SVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVL 1411
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
284-572 |
1.62e-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: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 284 FIAVFAFLRTFAVVSLPLMLYVFVD-----YANSDHRDLRNGF-FNLACLVMLkLVESLTMRHWYFASRRSGMRIRSALM 357
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINfvedaYLGGPPPSIGYGIgYAIGLFLLQ-LLSSLLLNHFFYRSMLTGAQVRAALT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 358 VAAYKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLN 437
Cdd:cd18597 80 KAIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 438 LPFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTK----AFGSFLywms 513
Cdd:cd18597 160 GFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRsiltAVAFSL---- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 514 PTIVSSVVFLGCALLKSaPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 572
Cdd:cd18597 236 PVLASMLSFITYYATGH-TLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
886-1179 |
5.40e-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: 145.40 E-value: 5.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 886 GWCLLWSSVLGQVGFVVFQAASTYWLAF----------------AIGIPKITNTMLIGVYSIISTLSAGFVY----ARAI 945
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYwlkqgsgnttnnvdnsTVDSGNISDNPDLNFYQLVYGGSILVILllslIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 946 TTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQV 1025
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1026 IIIALLALAATKVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAA 1105
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 1106 MEWVILRIETLQNVTLFTCALLLILIpKGYIAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1179
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLL-KGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1183-1436 |
1.12e-37 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 150.88 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1183 EEPPAIIDDKRppsswpSNGTIHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI 1262
Cdd:PRK13657 320 RDPPGAIDLGR------VKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1263 LIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDpLGV--YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGEN 1340
Cdd:PRK13657 393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR-VGRpdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQ 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1341 WSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYN 1420
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
250
....*....|....*.
gi 334185504 1421 EPSKLMETDSYFSKLV 1436
Cdd:PRK13657 552 SFDELVARGGRFAALL 567
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
609-792 |
1.34e-37 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 141.19 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 609 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSG 675
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDNILYGKPM-ESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 754
Cdd:cd03245 93 TLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334185504 755 AHTAGVLFHKcVEDSLKEKTVILVTHQ-----------VMEEGTITQSG 792
Cdd:cd03245 173 MNSEERLKER-LRQLLGDKTLIIITHRpslldlvdriiVMDSGRIVADG 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
598-807 |
6.79e-37 |
|
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: 139.67 E-value: 6.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 598 VDIQVGNFGWePETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAvlgeIPKV----SGTVKVFG------------ 661
Cdd:cd03251 1 VEFKNVTFRY-PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNL----IPRFydvdSGRILIDGhdvrdytlaslr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 662 -SIAYVSQTSWIQSGTIRDNILYGKPMESRR--YNAAIKACALDKDMNgFGHGDLTEIGQRGINLSGGQKQRIQLARAVY 738
Cdd:cd03251 76 rQIGLVSQDVFLFNDTVAENIAYGRPGATREevEEAARAANAHEFIME-LPEGYDTVIGERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 739 ADADVYLLDDPFSAVDAHTagvlfHKCVEDSL----KEKTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTA 803
Cdd:cd03251 155 KDPPILILDEATSALDTES-----ERLVQAALerlmKNRTTFVIAHRlstienadrivVLEDGKIVERGTHEELLAQGGV 229
|
....
gi 334185504 804 FQQL 807
Cdd:cd03251 230 YAKL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
604-798 |
1.64e-36 |
|
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: 138.13 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 604 NFGWEPetKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTS 670
Cdd:cd03254 9 NFSYDE--KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 671 WIQSGTIRDNILYGKPMESR-RYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDP 749
Cdd:cd03254 87 FLFSGTIMENIRLGRPNATDeEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 750 FSAVDAHTAgVLFHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEELL 798
Cdd:cd03254 167 TSNIDTETE-KLIQEALEKLMKGRTSIIIAHRlstiknadkilVLDDGKIIEEGTHDELL 225
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
284-573 |
4.10e-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: 139.31 E-value: 4.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 284 FIAVFAFLRTFAVVSLPLMLYVFVDYANSDHR-DLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYK 362
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVAYFVPDSTvTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 363 KQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAK 442
Cdd:cd18594 81 KTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 443 MLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVF 522
Cdd:cd18594 161 LFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 334185504 523 LGCALLKSApLNASTIFTVLATLRVMSEPVKI-IPDAISAIIQGNVSFQRLN 573
Cdd:cd18594 241 VPYVLTGNT-LTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
605-807 |
1.60e-35 |
|
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: 135.44 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 605 FGWEPETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSW 671
Cdd:cd03253 8 FAYDPGRPV--LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 672 IQSGTIRDNILYGKP--MESRRYNAAIKACALDKDMNgFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDP 749
Cdd:cd03253 86 LFNDTIGYNIRYGRPdaTDEEVIEAAKAAQIHDKIMR-FPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 750 FSAVDAHTAGVLFhKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQL 807
Cdd:cd03253 165 TSALDTHTEREIQ-AALRDVSKGRTTIVIAHRlstivnadkiiVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1202-1416 |
2.07e-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: 2.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1202 GTIHLQELKIRYrPNAP--LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM 1279
Cdd:cd03248 10 GIVKFQNVTFAY-PTRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1280 KLSIIPQEPTLFRGCIRTNLD-PLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKR 1358
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 1359 NKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDL 1416
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
614-781 |
5.07e-35 |
|
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: 141.66 E-value: 5.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDN 680
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 ILYGKP----MESRRynaAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 756
Cdd:TIGR02857 416 IRLARPdasdAEIRE---ALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180
....*....|....*....|....*
gi 334185504 757 TAgVLFHKCVEDSLKEKTVILVTHQ 781
Cdd:TIGR02857 493 TE-AEVLEALRALAQGRTVLLVTHR 516
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1071-1398 |
8.08e-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: 141.34 E-value: 8.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1071 GVVTIRAFGTAERFFKNYlnlVDADAVLFFLSNAAMEWVILRietlQNVTLFTCAL---LLILIPKGYIAPGLVGLSLSY 1147
Cdd:TIGR02868 202 GAAELVASGALPAALAQV---EEADRELTRAERRAAAATALG----AALTLLAAGLavlGALWAGGPAVADGRLAPVTLA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1148 ALTLTQTQVF-----LTRWYCTLSNSIISVERIKQYMNiPEEPPAIIDDKRPPSSWPSNGTIHLQELKIRYrPNAPLVLK 1222
Cdd:TIGR02868 275 VLVLLPLAAFeafaaLPAAAQQLTRVRAAAERIVEVLD-AAGPVAEGSAPAAGAVGLGKPTLELRDLSAGY-PGAPPVLD 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1223 GISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDpL 1302
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLR-L 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1303 GV--YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQ 1380
Cdd:TIGR02868 432 ARpdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL 511
|
330
....*....|....*...
gi 334185504 1381 RIIREEFADCTVITVAHR 1398
Cdd:TIGR02868 512 EDLLAALSGRTVVLITHH 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1173-1438 |
1.31e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 141.52 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1173 ERIKQYMNIPEEPPAiidDKRPPSSWPSNGTIHLQELKIrYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALF 1252
Cdd:PRK11174 322 ESLVTFLETPLAHPQ---QGEKELASNDPVTIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1253 RLVePASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNL---DPLgvYSDDEIWKALEKCQLKTTISNLPNK 1329
Cdd:PRK11174 398 GFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPD--ASDEQLQQALENAWVSEFLPLLPQG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1330 LDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVM 1409
Cdd:PRK11174 475 LDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIW 554
|
250 260
....*....|....*....|....*....
gi 334185504 1410 VLSFGDLVEYNEPSKLMETDSYFSKLVAE 1438
Cdd:PRK11174 555 VMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
614-780 |
1.50e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.29 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--------SIAYVSQTSWIQSG---TIRDNI- 681
Cdd:COG1121 20 PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQRAEVDWDfpiTVRDVVl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 --LYGKPMESRRYNAAIKAC---ALDK-DMNGFGHgdlTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:COG1121 100 mgRYGRRGLFRRPSRADREAvdeALERvGLEDLAD---RPIGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190
....*....|....*....|....*....|
gi 334185504 756 HTAGVLFhkcveDSLKE-----KTVILVTH 780
Cdd:COG1121 173 ATEEALY-----ELLRElrregKTILVVTH 197
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1211-1397 |
2.11e-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: 2.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1211 IRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTL 1290
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1291 FRGCIRTNLD-PLG----VYSDDEIWKALEKCQLKTTIsnlpnkLDSSVsdegENWSVGQRQLFCLGRVLLKRNKILVLD 1365
Cdd:COG4619 86 WGGTVRDNLPfPFQlrerKFDRERALELLERLGLPPDI------LDKPV----ERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190
....*....|....*....|....*....|....
gi 334185504 1366 EATASIDSATDAIIQRIIREEFADC--TVITVAH 1397
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEgrAVLWVSH 189
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
917-1178 |
3.47e-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: 134.37 E-value: 3.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 917 IPKITNTMLIGVYSIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYD 996
Cdd:cd18601 53 IEDLDRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 997 VPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIR 1076
Cdd:cd18601 133 LPLTFLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1077 AFGTAERF---FKNYLNLvDADAVLFFLsnAAMEWVILRIETLqnVTLFTCALLLI-LIPKGYIAPGLVGLSLSYALTLT 1152
Cdd:cd18601 213 AYSAQERFqeeFDAHQDL-HSEAWFLFL--ATSRWLAVRLDAL--CALFVTVVAFGsLFLAESLDAGLVGLSLSYALTLM 287
|
250 260
....*....|....*....|....*.
gi 334185504 1153 QTQVFLTRWYCTLSNSIISVERIKQY 1178
Cdd:cd18601 288 GTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
287-572 |
1.30e-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: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 287 VFAFLRTFAVV---SLPLMLYVFVDYANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYKK 363
Cdd:cd18598 1 PLGLLKLLADVlgfAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 364 QLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKM 443
Cdd:cd18598 81 ALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 444 LQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVFL 523
Cdd:cd18598 161 IGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 334185504 524 GCALLKSaPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 572
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 ... |
300-572 |
1.80e-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: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 300 PLMLYVFVDYANSDHRD------------------LRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAY 361
Cdd:cd18591 17 PLCISGIVDYVEENTYSssnstdklsvsyvtveefFSNGYVLAVILFLALLLQATFSQASYHIVIREGIRLKTALQAMIY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 362 KKQLKLSS--LGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLP 439
Cdd:cd18591 97 EKALRLSSwnLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIGAALILVMTPLQYL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 440 FAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSS 519
Cdd:cd18591 177 IARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLMTFLTQASPILVTL 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 334185504 520 VVFLGCALLKSAPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 572
Cdd:cd18591 257 VTFGLYPYLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
618-815 |
4.54e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 136.90 E-value: 4.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 618 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPkVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDNILYG 684
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 685 KP-MESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAgvlfh 763
Cdd:PRK11174 447 NPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE----- 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 764 KCVEDSLKE----KTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQLVNAHNDAV 815
Cdd:PRK11174 522 QLVMQALNAasrrQTTLMVTHQledlaqwdqiwVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEEI 588
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1199-1435 |
4.57e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 136.69 E-value: 4.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1199 PSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLR 1278
Cdd:PRK11176 337 RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1279 MKLSIIPQEPTLFRGCIRTNL--DPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLL 1356
Cdd:PRK11176 417 NQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1357 KRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKL 1435
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
614-780 |
5.18e-33 |
|
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: 127.65 E-value: 5.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--------SIAYVSQTSWIQSG---TIRDNI- 681
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRSIDRDfpiSVRDVVl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 --LYGKPMESRRYNAAIKAC---ALDKdmngfghGDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:cd03235 93 mgLYGHKGLFRRLSKADKAKvdeALER-------VGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180
....*....|....*....|....*
gi 334185504 756 HTAGVLFHKCVEDSLKEKTVILVTH 780
Cdd:cd03235 166 KTQEDIYELLRELRREGMTILVVTH 190
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
609-810 |
1.13e-32 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 127.66 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 609 PETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQTSWIQSG 675
Cdd:cd03249 14 PDVPI--LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDNILYGKP---MESRRynAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSA 752
Cdd:cd03249 92 TIAENIRYGKPdatDEEVE--EAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 753 VDAHTAGVLfHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQLVNA 810
Cdd:cd03249 170 LDAESEKLV-QEALDRAMKGRTTIVIAHRlstirnadliaVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1221-1369 |
1.31e-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: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRG-CIRTNL 1299
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1300 -------DPLGVYSDDEIWKALEKCqlkttisNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATA 1369
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1204-1411 |
1.04e-31 |
|
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: 122.32 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1283
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLFRGCIRTNLdplgvysddeiwkalekcqlkttisnlpnkldssvsdegenWSVGQRQLFCLGRVLLKRNKILV 1363
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 334185504 1364 LDEATASIDSATDAIIQRIIRE-EFADCTVITVAHRvPTVIDS-DMVMVL 1411
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHR-PETLASaDRILVL 168
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1204-1425 |
9.76e-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: 9.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVE-----PASGCILIDGIDISKIGLKD-- 1276
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1277 LRMKLSIIPQEPTLFRGCIRTNLDpLGV----YSDDEIWKALEKCQLKTTisnlpnKLDSSVSDE--GENWSVGQRQLFC 1350
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA-YGLrlhgIKLKEELDERVEEALRKA------ALWDEVKDRlhALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1351 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAH------RVptvidSDMVMVLSFGDLVEYNEPSK 1424
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 334185504 1425 L 1425
Cdd:cd03260 227 I 227
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
604-808 |
1.94e-30 |
|
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: 128.66 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 604 NFGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTS 670
Cdd:TIGR02204 344 NFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlrqldpaelraRMALVPQDP 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 671 WIQSGTIRDNILYGKPMESRR--YNAAIKACAlDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDD 748
Cdd:TIGR02204 424 VLFAASVMENIRYGRPDATDEevEAAARAAHA-HEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDE 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 749 PFSAVDAHTAgVLFHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQLV 808
Cdd:TIGR02204 503 ATSALDAESE-QLVQQALETLMKGRTTLIIAHRlatvlkadrivVMDQGRIVAQGTHAELIAKGGLYARLA 572
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
564-798 |
3.77e-30 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 127.52 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 564 QGNVSFQRLNNfLLDDELKMDEIERSGLDASGT-AVDIQVGNFgwePETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSL 642
Cdd:PRK10789 282 RGSAAYSRIRA-MLAEAPVVKDGSEPVPEGRGElDVNIRQFTY---PQTDHPALENVNFTLKPGQMLGICGPTGSGKSTL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 643 LHAVLGEIPKVSGTVKVF-------------GSIAYVSQTSWIQSGTIRDNILYGKPMESRRY--NAAIKACALDkDMNG 707
Cdd:PRK10789 358 LSLIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSDTVANNIALGRPDATQQEieHVARLASVHD-DILR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 708 FGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSlKEKTVILVTHQ------ 781
Cdd:PRK10789 437 LPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRlsalte 515
|
250 260
....*....|....*....|..
gi 334185504 782 -----VMEEGTITQSGKYEELL 798
Cdd:PRK10789 516 aseilVMQHGHIAQRGNHDQLA 537
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1165-1435 |
8.55e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 126.48 E-value: 8.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1165 LSNSIISVERIKQymnIPEEPPAIIDDKRPPSSwPSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGK 1244
Cdd:PRK11160 304 LGQVIASARRINE---ITEQKPEVTFPTTSTAA-ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1245 STLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNL---DPLGvySDDEIWKALEKCQLKT 1321
Cdd:PRK11160 380 STLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLEK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1322 TISNlPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVpT 1401
Cdd:PRK11160 458 LLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRL-T 535
|
250 260 270
....*....|....*....|....*....|....*
gi 334185504 1402 VIDS-DMVMVLSFGDLVEYNEPSKLMETDSYFSKL 1435
Cdd:PRK11160 536 GLEQfDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
609-798 |
1.40e-29 |
|
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: 125.54 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 609 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKV------------FG-SIAYVSQTSWIQSG 675
Cdd:TIGR01842 327 PGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLdgadlkqwdretFGkHIGYLPQDVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDNIL-YGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 754
Cdd:TIGR01842 407 TVAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 755 AHTAGVLFHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEELL 798
Cdd:TIGR01842 487 EEGEQALANAIKALKARGITVVVITHRpsllgcvdkilVLQDGRIARFGERDEVL 541
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1201-1415 |
2.95e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 127.45 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1201 NGTIHLQELKIRY--RPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRL------------------------ 1254
Cdd:PTZ00265 1163 KGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1255 ------------------------------VEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDpLGV 1304
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGK 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1305 --YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRI 1382
Cdd:PTZ00265 1321 edATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270
....*....|....*....|....*....|....*
gi 334185504 1383 IRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGD 1415
Cdd:PTZ00265 1401 IVDikDKADKTIITIAHRIASIKRSDKIVVFNNPD 1435
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
616-784 |
3.85e-29 |
|
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: 116.80 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--------SIAYVSQTS----WIqsgTIRDNILY 683
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQQDallpWL---TVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 684 G------KPMESRRY-NAAIKACALDkdmnGFGHgdlteigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 756
Cdd:cd03293 97 GlelqgvPKAEARERaEELLELVGLS----GFEN-------AYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180 190
....*....|....*....|....*....|
gi 334185504 757 TAGVLfHKCVEDSLKE--KTVILVTHQVME 784
Cdd:cd03293 166 TREQL-QEELLDIWREtgKTVLLVTHDIDE 194
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
464-810 |
7.77e-29 |
|
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: 124.85 E-value: 7.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 464 EILNSMKVIKLQSWEDEFKKKIescrDDEF-TWLAKA---QLTKAFGSFLYWMSPTIVSSVV-FLGCALLKSAPLNASTI 538
Cdd:TIGR01193 339 EDLNGIETIKSLTSEAERYSKI----DSEFgDYLNKSfkyQKADQGQQAIKAVTKLILNVVIlWTGAYLVMRGKLTLGQL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 539 FTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRLNNFLLDDelkmDEIERSGLDASGTAV--DIQVGNFGWEPETKIPTL 616
Cdd:TIGR01193 415 ITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVD----SEFINKKKRTELNNLngDIVINDVSYSYGYGSNIL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 617 RNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDNILY 683
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhtlrqFINYLPQEPYIFSGSILENLLL 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 684 G-KP-MESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAgvl 761
Cdd:TIGR01193 571 GaKEnVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE--- 647
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 762 fHKCVED--SLKEKTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQLVNA 810
Cdd:TIGR01193 648 -KKIVNNllNLQDKTIIFVAHRlsvakqsdkiiVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1183-1427 |
1.00e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 122.32 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1183 EEPPAIIDDKRPPSSWPSNGT--IHLQELKIRY---RPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEP 1257
Cdd:COG1123 238 AAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1258 ASGCILIDGIDISKIG---LKDLRMKLSIIPQEPT--LF-RGCIRTNL-DPL---GVYSDDEIWK----ALEKCQLKTTI 1323
Cdd:COG1123 318 TSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYssLNpRMTVGDIIaEPLrlhGLLSRAERRErvaeLLERVGLPPDL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1324 SN-LPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE---EFaDCTVITVAHRV 1399
Cdd:COG1123 398 ADrYPHEL-----------SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqrEL-GLTYLFISHDL 465
|
250 260
....*....|....*....|....*....
gi 334185504 1400 PTVID-SDMVMVLSFGDLVEYNEPSKLME 1427
Cdd:COG1123 466 AVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1204-1428 |
1.05e-28 |
|
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: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRP--NAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1281
Cdd:COG1124 2 LEVRNLSVSYGQggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPtlfrgciRTNLDP--------------LGV-YSDDEIWKALEKCQLKTTI-SNLPNKLdssvsdegenwSVGQ 1345
Cdd:COG1124 82 QMVFQDP-------YASLHPrhtvdrilaeplriHGLpDREERIAELLEQVGLPPSFlDRYPHQL-----------SGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1346 RQLFCLGRVLLKRNKILVLDEATASIDSATDAII----QRIIREEfaDCTVITVAHRVPtVID--SDMVMVLSFGDLVEY 1419
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEIlnllKDLREER--GLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEE 220
|
....*....
gi 334185504 1420 NEPSKLMET 1428
Cdd:COG1124 221 LTVADLLAG 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1211-1414 |
1.16e-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: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1211 IRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQeptL 1290
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1291 frgcirtnldplgvysddeiwkalekcqlkttisnlpnkldssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATAS 1370
Cdd:cd00267 82 ---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 334185504 1371 IDSATDAIIQRIIREEFAD-CTVITVAHRVPTVID-SDMVMVLSFG 1414
Cdd:cd00267 111 LDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
284-572 |
1.60e-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: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 284 FIAVFAFLrTFAVVSLPLMLYVFVDYANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYKK 363
Cdd:cd18559 2 FLLIKLVL-CNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 364 QLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPFAKM 443
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 444 LQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSVVFL 523
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 334185504 524 GCALLKS-APLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 572
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, ... |
285-572 |
2.21e-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: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 285 IAVFAFLRTFAVVSLPLMLYVFVDYANSDHRDLRNGFFNLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAAYKKQ 364
Cdd:cd18592 3 ILLLLISLIFGFIGPTILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 365 LKLSSLGRKrhSSGEIVNYIAVDAYRMGE---FLWWFHSGWSLSLQLLLSTAVLFG---VVGAGAFPglillllcglLNL 438
Cdd:cd18592 83 LRLRSLGDK--SVGELINIFSNDGQRLFDaavFGPLVIGGPVVLILGIVYSTYLLGpwaLLGMLVFL----------LFY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 439 PFAKMLQNCQTQF----MIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSP 514
Cdd:cd18592 151 PLQAFIAKLTGKFrrkaIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVP 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 515 TIVSSVVFLGCALLKSApLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 572
Cdd:cd18592 231 VIASVVTFLAHVALGND-LTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
616-751 |
3.34e-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: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSG-TIRDNI 681
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 682 LYGKPMEsrRYNAAIKACALDKDMNGFGHGDL--TEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFS 751
Cdd:pfam00005 81 RLGLLLK--GLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
541-781 |
4.29e-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: 120.93 E-value: 4.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 541 VLATLRVMsEPVKIIPDAISAIIQGNVSFQRLNNfLLDDELKMDEIErsgLDASGTAVDIQVG------NFGWEPETkiP 614
Cdd:TIGR02868 277 VLLPLAAF-EAFAALPAAAQQLTRVRAAAERIVE-VLDAAGPVAEGS---APAAGAVGLGKPTlelrdlSAGYPGAP--P 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 615 TLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQTSWIQSGTIRDNI 681
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 LYGKPMES-RRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGV 760
Cdd:TIGR02868 430 RLARPDATdEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
250 260
....*....|....*....|.
gi 334185504 761 LFHKcVEDSLKEKTVILVTHQ 781
Cdd:TIGR02868 510 LLED-LLAALSGRTVVLITHH 529
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
616-784 |
5.87e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 114.42 E-value: 5.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--------SIAYVSQTS----WIqsgTIRDNILY 683
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQEPallpWL---TVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 684 G-----KPMESRRYNA--AIKACALDKDMNGFGHgdlteigqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 756
Cdd:COG1116 104 GlelrgVPKAERRERAreLLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDAL 172
|
170 180 190
....*....|....*....|....*....|
gi 334185504 757 TAGVLfHKCVEDSLKE--KTVILVTHQVME 784
Cdd:COG1116 173 TRERL-QDELLRLWQEtgKTVLFVTHDVDE 201
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1204-1418 |
1.33e-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: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGlKDLRMKLSI 1283
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLFRGCIRTNLdplgvysddeiwkalekcqlkttisnlpnkldssvsdeGENWSVGQRQLFCLGRVLLKRNKILV 1363
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1364 LDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVE 1418
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1204-1427 |
2.09e-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: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1283
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPT--LFRGCIR-------TNldpLGVySDDEIWKALEKCqLKTTisNLPNKLDSSVSDegenWSVGQRQLFCLGRV 1354
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpEN---LGL-PREEIRERVEEA-LELV--GLEHLADRPPHE----LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1355 LLKRNKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLME 1427
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFS 223
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1166-1421 |
3.88e-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: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1166 SNSIISVERIKQYMNipEEPPaiiddKRPPSSWPS-NGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGK 1244
Cdd:TIGR01842 285 SGARQAYKRLNELLA--NYPS-----RDPAMPLPEpEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGK 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1245 STLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLDPLGVYSDDE-IWKALEKCQLKTTI 1323
Cdd:TIGR01842 358 STLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEkIIEAAKLAGVHELI 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1324 SNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATD-AIIQRIIREEFADCTVITVAHRVPTV 1402
Cdd:TIGR01842 438 LRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEqALANAIKALKARGITVVVITHRPSLL 517
|
250
....*....|....*....
gi 334185504 1403 IDSDMVMVLSFGDLVEYNE 1421
Cdd:TIGR01842 518 GCVDKILVLQDGRIARFGE 536
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1209-1420 |
8.10e-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: 8.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1209 LKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG---LKDLRMKLSI 1283
Cdd:cd03257 7 LSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPtlfrgciRTNLDPL--------------GVYSDDE-----IWKALEKCQLKTTISN-LPNKLdssvsdegenwSV 1343
Cdd:cd03257 87 VFQDP-------MSSLNPRmtigeqiaeplrihGKLSKKEarkeaVLLLLVGVGLPEEVLNrYPHEL-----------SG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1344 GQRQLFCLGRVLLKRNKILVLDEATASIDSATDA-IIQRI--IREEFaDCTVITVAHRVPTV-IDSDMVMVLSFGDLVEY 1419
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAqILDLLkkLQEEL-GLTLLFITHDLGVVaKIADRVAVMYAGKIVEE 227
|
.
gi 334185504 1420 N 1420
Cdd:cd03257 228 G 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
600-780 |
9.31e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.52 E-value: 9.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 600 IQVGNFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYV 666
Cdd:COG4619 1 LELEGLSFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 667 SQTSWIQSGTIRDNILYGKPMESRRYNAAikacALDKDMN--GFGHGDLTeigQRGINLSGGQKQRIQLARAVYADADVY 744
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRERKFDRE----RALELLErlGLPPDILD---KPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 334185504 745 LLDDPFSAVDAHTAGvLFHKCVEDSLKEK--TVILVTH 780
Cdd:COG4619 153 LLDEPTSALDPENTR-RVEELLREYLAEEgrAVLWVSH 189
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1200-1438 |
1.15e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.24 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1200 SNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM 1279
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1280 KLSIIPQEP-TLFrgcirtnldpLGVYSDDEIWKALE-KC----QLKTTISNLPNK--LDSSVSDEGENWSVGQRQLFCL 1351
Cdd:PRK13632 84 KIGIIFQNPdNQF----------IGATVEDDIAFGLEnKKvppkKMKDIIDDLAKKvgMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1352 GRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPS------ 1423
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKeilnnk 233
|
250
....*....|....*...
gi 334185504 1424 ---KLMETDSYFSKLVAE 1438
Cdd:PRK13632 234 eilEKAKIDSPFIYKLSK 251
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
616-808 |
2.24e-26 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 109.11 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDNIL 682
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 683 YGKP-MESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVL 761
Cdd:cd03252 98 LADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 762 FHKcVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQLV 808
Cdd:cd03252 178 MRN-MHDICAGRTVIIIAHRlstvknadriiVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
284-572 |
3.29e-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: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 284 FIAVFAFLRTFAVVSLPLMLYVFVDY--ANSDHRDLRNGFFNLACLVMLKLVESLTmRHWYF-ASRRSGMRIRSALMVAA 360
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYfeGNGSSISLTEAYLYAGGVSLCSFLFIIT-HHPYFfGMQRIGMRLRVACSSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 361 YKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAGAFPGLILLLLCGLLNLPF 440
Cdd:cd18593 80 YRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 441 AKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSSV 520
Cdd:cd18593 160 GKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 521 VFLGCALLkSAPLNASTIFTVLAtlrvMSEPVKII-----PDAISAIIQGNVSFQRL 572
Cdd:cd18593 240 TFLAYILL-GNILTAERVFVTMA----LYNAVRLTmtlffPFAIQFGSELSVSIRRI 291
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
599-792 |
3.59e-26 |
|
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: 107.96 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 599 DIQVGNFG--WEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SI 663
Cdd:cd03244 2 DIEFKNVSlrYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 664 AYVSQTSWIQSGTIRDNI-LYGKPMESRRYNaAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADAD 742
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 743 VYLLDDPFSAVDAHTAGVLfHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSG 792
Cdd:cd03244 160 ILVLDEATASVDPETDALI-QKTIREAFKDCTVLTIAHRldtiidsdrilVLDKGRVVEFD 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
609-798 |
5.78e-26 |
|
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: 114.46 E-value: 5.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 609 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKV------------FG-SIAYVSQTSWIQSG 675
Cdd:COG4618 341 PGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlsqwdreeLGrHIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDNI-LYGKPMESRRYNAAIKACAldKDM-----NGFGhgdlTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDP 749
Cdd:COG4618 421 TIAENIaRFGDADPEKVVAAAKLAGV--HEMilrlpDGYD----TRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 750 FSAVDAhtAGvlfhkcvEDSLKE---------KTVILVTHQ-----------VMEEGTITQSGKYEELL 798
Cdd:COG4618 495 NSNLDD--EG-------EAALAAairalkargATVVVITHRpsllaavdkllVLRDGRVQAFGPRDEVL 554
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1204-1427 |
9.37e-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: 9.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRmKLSI 1283
Cdd:COG4555 2 IEVENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLF-RGCIRTNLDPLGvysddEIWKaLEKCQLKTTISN------LPNKLDSSVSDegenWSVGQRQLFCLGRVLL 1356
Cdd:COG4555 79 LPDERGLYdRLTVRENIRYFA-----ELYG-LFDEELKKRIEEliellgLEEFLDRRVGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1357 KRNKILVLDEATASIdsatDAIIQRIIREEFADC-----TVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLME 1427
Cdd:COG4555 149 HDPKVLLLDEPTNGL----DVMARRLLREILRALkkegkTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1204-1427 |
1.10e-25 |
|
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: 113.07 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPA---SGCILIDGIDISKIGLKDLRMK 1280
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1281 LSIIPQEPTlfrgcirTNLDPLGV------------YSDDEIWK----ALEKCQLKTTISNLPNKLdssvsdegenwSVG 1344
Cdd:COG1123 85 IGMVFQDPM-------TQLNPVTVgdqiaealenlgLSRAEARArvleLLEAVGLERRLDRYPHQL-----------SGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1345 QRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNE 1421
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGP 226
|
....*.
gi 334185504 1422 PSKLME 1427
Cdd:COG1123 227 PEEILA 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
616-792 |
2.13e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 104.44 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQtswiqsgtirdnil 682
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 683 ygkpmesrrynaAIKACaldkdmngfghgDLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVD-AHTAGV 760
Cdd:cd03214 81 ------------ALELL------------GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDiAHQIEL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 334185504 761 LfhkcveDSLKE------KTVILVTHQ------------VMEEGTITQSG 792
Cdd:cd03214 137 L------ELLRRlarergKTVVMVLHDlnlaaryadrviLLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
612-784 |
2.76e-25 |
|
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: 103.48 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSiayvsQTSWIQSGTIRDNILYgkpmesrr 691
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRIGY-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 692 ynaaikacaldkdmngfghgdlteIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLK 771
Cdd:cd00267 78 ------------------------VPQ----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE 129
|
170
....*....|...
gi 334185504 772 EKTVILVTHQVME 784
Cdd:cd00267 130 GRTVIIVTHDPEL 142
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1204-1397 |
6.25e-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: 105.51 E-value: 6.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1283
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTL-F---------RGciRTN-LDPLGVYSDDE---IWKALEKCQlkttISNLPNKLDSSVSDegenwsvGQRQLF 1349
Cdd:COG1120 80 VPQEPPApFgltvrelvaLG--RYPhLGLFGRPSAEDreaVEEALERTG----LEHLADRPVDELSG-------GERQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334185504 1350 CLGRVLLKRNKILVLDEATASID----SATDAIIQRIIREEfaDCTVITVAH 1397
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARER--GRTVVMVLH 196
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
598-782 |
6.31e-25 |
|
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: 104.86 E-value: 6.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 598 VDIQVGNFGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IA 664
Cdd:cd03248 12 VKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 665 YVSQTSWIQSGTIRDNILYG---KPMESRRyNAAIKACAlDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADA 741
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGlqsCSFECVK-EAAQKAHA-HSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 334185504 742 DVYLLDDPFSAVDAHTAGVLfHKCVEDSLKEKTVILVTHQV 782
Cdd:cd03248 170 QVLILDEATSALDAESEQQV-QQALYDWPERRTVLVIAHRL 209
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1171-1404 |
1.82e-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: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1171 SVERI---KQYMNIPEEPPAIIDDKRPPSSwpsnGTIHLQELKIRyRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTL 1247
Cdd:COG4178 331 TVDRLagfEEALEAADALPEAASRIETSED----GALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1248 ISALFRLVEPASGCILIDGIDiskiglkdlrmKLSIIPQEPTLFRGCIRTNL---DPLGVYSDDEIWKALEKCQLkttiS 1324
Cdd:COG4178 406 LRAIAGLWPYGSGRIARPAGA-----------RVLFLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL----G 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1325 NLPNKLDssvsdEGENW----SVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRvP 1400
Cdd:COG4178 471 HLAERLD-----EEADWdqvlSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-S 544
|
....
gi 334185504 1401 TVID 1404
Cdd:COG4178 545 TLAA 548
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
612-792 |
2.59e-24 |
|
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: 102.60 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------SIAYVSQT----SWIqsgT 676
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDyalfPHL---T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 677 IRDNILYG-------KPMESRRYNAAIKACALDKDMNGFGHGdlteigqrginLSGGQKQRIQLARAVYADADVYLLDDP 749
Cdd:cd03259 89 VAENIAFGlklrgvpKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 750 FSAVDAHTAGVLFHKcVEDSLKE--KTVILVTH------------QVMEEGTITQSG 792
Cdd:cd03259 158 LSALDAKLREELREE-LKELQRElgITTIYVTHdqeealaladriAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
616-809 |
2.94e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 103.22 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------------SIAYVSQTSWIQSG-TIRDNI- 681
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 ----LYGKPMESR--RYNAAIKACALDKDMNgfghgdlteigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:COG1131 96 ffarLYGLPRKEAreRIDELLELFGLTDAAD-----------RKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 756 HTAGVLFHKCVEDSLKEKTVILVTHQ------------VMEEGTITQSGKYEELL--MMGTAFQQLVN 809
Cdd:COG1131 165 EARRELWELLRELAAEGKTVLLSTHYleeaerlcdrvaIIDKGRIVADGTPDELKarLLEDVFLELTG 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
616-784 |
3.15e-24 |
|
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: 102.17 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS------IAYVSQTSWI--QSG-----TIRDNI- 681
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdarEDYRRRLAYLghADGlkpelTVRENLr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 ----LYGKPMESRRYNAAIKACALDkdmngfGHGDLtEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAht 757
Cdd:COG4133 98 fwaaLYGLRADREAIDEALEAVGLA------GLADL-PVRQ----LSAGQKRRVALARLLLSPAPLWLLDEPFTALDA-- 164
|
170 180
....*....|....*....|....*....
gi 334185504 758 AGV-LFHKCVEDSLKE-KTVILVTHQVME 784
Cdd:COG4133 165 AGVaLLAELIAAHLARgGAVLLTTHQPLE 193
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
592-807 |
3.29e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.14 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 592 DASGTAVDIQVGN--FGWePETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------- 661
Cdd:PRK11160 331 TAAADQVSLTLNNvsFTY-PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyse 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 662 -----SIAYVSQTSWIQSGTIRDNILYGKPMES-RRYNAAIKACALDKDMNGfGHGDLTEIGQRGINLSGGQKQRIQLAR 735
Cdd:PRK11160 410 aalrqAISVVSQRVHLFSATLRDNLLLAAPNASdEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 736 AVYADADVYLLDDPFSAVDAHTA----GVLFHKCvedslKEKTVILVTHQ-----------VMEEGTITQSGKYEELLMM 800
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETErqilELLAEHA-----QNKTVLMITHRltgleqfdricVMDNGQIIEQGTHQELLAQ 563
|
....*..
gi 334185504 801 GTAFQQL 807
Cdd:PRK11160 564 QGRYYQL 570
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1206-1414 |
4.09e-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: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1206 LQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIP 1285
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1286 QEP-------TLFR----GCIRTNLDPlgvysdDEIWKALEKCqLKTTisNLPNKLDSSVSDegenWSVGQRQLFCLGRV 1354
Cdd:cd03225 82 QNPddqffgpTVEEevafGLENLGLPE------EEIEERVEEA-LELV--GLEGLRDRSPFT----LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1355 LLKRNKILVLDEATASIDSATDAIIQRIIReEFADC--TVITVAHRVPTVID-SDMVMVLSFG 1414
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
604-807 |
5.14e-24 |
|
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: 109.45 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 604 NFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTS 670
Cdd:TIGR01846 462 RFRYAPDSP-EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGvdlaiadpawlrrQMGVVLQEN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 671 WIQSGTIRDNILYGKP---MESRRYnAAIKACALDKdMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLD 747
Cdd:TIGR01846 541 VLFSRSIRDNIALCNPgapFEHVIH-AAKLAGAHDF-ISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFD 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 748 DPFSAVDAHTAGVLFHKCVEDSlKEKTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQL 807
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREIC-RGRTVIIIAHRlstvracdriiVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
612-808 |
5.17e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 109.43 E-value: 5.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIR 678
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 679 DNILYG---KPMESRRyNAAIKACALDKDMnGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:TIGR00958 573 ENIAYGltdTPDEEIM-AAAKAANAHDFIM-EFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 756 HTAGVLFHkcvEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQLV 808
Cdd:TIGR00958 651 ECEQLLQE---SRSRASRTVLLIAHRlstveradqilVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1202-1411 |
6.08e-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: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1202 GTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKL 1281
Cdd:COG4618 329 GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPTLFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKI 1361
Cdd:COG4618 409 GYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334185504 1362 LVLDEATASIDSATDAIIQRIIREEFAD-CTVITVAHRvPTVIDS-DMVMVL 1411
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHR-PSLLAAvDKLLVL 539
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1174-1433 |
7.38e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 107.88 E-value: 7.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1174 RIKQYMnipEEPPAIIDDKRPPSSWPSNGTIHLQELkiRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFR 1253
Cdd:PRK10789 289 RIRAML---AEAPVVKDGSEPVPEGRGELDVNIRQF--TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1254 LVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNLdPLGV--YSDDEIWKALEKCQLKTTISNLPNKLD 1331
Cdd:PRK10789 364 HFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI-ALGRpdATQQEIEHVARLASVHDDILRLPQGYD 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1332 SSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVL 1411
Cdd:PRK10789 443 TEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVM 522
|
250 260
....*....|....*....|..
gi 334185504 1412 SFGDLVEYNEPSKLMETDSYFS 1433
Cdd:PRK10789 523 QHGHIAQRGNHDQLAQQSGWYR 544
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
616-798 |
1.01e-23 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 102.04 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSG-TIRDNI 681
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEPPAPFGlTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 LYG-KP------MESRRYNAAIKAcALDK-DMNGFGHGDLTEigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAV 753
Cdd:COG1120 97 ALGrYPhlglfgRPSAEDREAVEE-ALERtGLEHLADRPVDE-------LSGGERQRVLIARALAQEPPLLLLDEPTSHL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 754 D-AHTAGVLfhkcveDSLKE------KTVILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:COG1120 169 DlAHQLEVL------ELLRRlarergRTVVMVLHDlnlaaryadrlvLLKDGRIVAQGPPEEVL 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
533-807 |
1.22e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.41 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 533 LNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRLnnF-LLDDELKMDEIERSGLDASGtavDIQVGN--FGWeP 609
Cdd:PRK11176 279 LTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTL--FaILDLEQEKDEGKRVIERAKG---DIEFRNvtFTY-P 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 610 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGT 676
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQNVHLFNDT 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 677 IRDNILYGKPMESRRY---NAAIKACALDKdMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAV 753
Cdd:PRK11176 433 IANNIAYARTEQYSREqieEAARMAYAMDF-INKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 754 DAHTAGVLfHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQL 807
Cdd:PRK11176 512 DTESERAI-QAALDELQKNRTSLVIAHRlstiekadeilVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1206-1397 |
1.37e-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: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1206 LQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIP 1285
Cdd:cd03214 2 VENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1286 QeptlfrgcirtnldplgvysddeiwkALEKCQlkttISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLD 1365
Cdd:cd03214 80 Q--------------------------ALELLG----LAHLADRPFNELSG-------GERQRVLLARALAQEPPILLLD 122
|
170 180 190
....*....|....*....|....*....|....*.
gi 334185504 1366 EATASID----SATDAIIQRIIREEfaDCTVITVAH 1397
Cdd:cd03214 123 EPTSHLDiahqIELLELLRRLARER--GKTVVMVLH 156
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
605-807 |
2.15e-23 |
|
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: 106.83 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 605 FGWEPETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWIQS-G------- 675
Cdd:COG5265 365 FGYDPERPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqDIRDVTQASLRAAiGivpqdtv 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 ----TIRDNILYGKPMESRR-YNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPF 750
Cdd:COG5265 443 lfndTIAYNIAYGRPDASEEeVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 751 SAVDAHTagvlfHKCVEDSLKE----KTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQL 807
Cdd:COG5265 523 SALDSRT-----ERAIQAALREvargRTTLVIAHRlstivdadeilVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
604-792 |
2.25e-23 |
|
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: 98.54 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 604 NFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS------------IAYVSQTSW 671
Cdd:cd03247 7 SFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 672 IQSGTIRDNIlygkpmesrrynaaikacaldkdmngfghgdlteigqrGINLSGGQKQRIQLARAVYADADVYLLDDPFS 751
Cdd:cd03247 86 LFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334185504 752 AVDAHTAGVLFhKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSG 792
Cdd:cd03247 128 GLDPITERQLL-SLIFEVLKDKTLIWITHHltgiehmdkilFLENGKIIMQG 178
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
614-780 |
2.75e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.85 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--SIAYVSQTS---WIQSGTIRDNI---LYGK 685
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSevpDSLPLTVRDLVamgRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 686 PMESRRYNAAIKAcALDKDMNGFGhgdLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHK 764
Cdd:NF040873 86 RGLWRRLTRDDRA-AVDDALERVG---LADLAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAL 161
|
170
....*....|....*.
gi 334185504 765 CVEDSLKEKTVILVTH 780
Cdd:NF040873 162 LAEEHARGATVVVVTH 177
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
587-810 |
4.19e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.81 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 587 ERSGL-DASGTAVDIQVGNFGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKS---SLLHAVLGeiPKvSGTVKVFG- 661
Cdd:PRK13657 321 DPPGAiDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKStliNLLQRVFD--PQ-SGRILIDGt 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 662 ------------SIAYVSQTSWIQSGTIRDNILYGKP--MESRRYNAAIKACALD---KDMNGFGhgdlTEIGQRGINLS 724
Cdd:PRK13657 398 dirtvtraslrrNIAVVFQDAGLFNRSIEDNIRVGRPdaTDEEMRAAAERAQAHDfieRKPDGYD----TVVGERGRQLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 725 GGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLfHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSGK 793
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKV-KAALDELMKGRTTFIIAHRlstvrnadrilVFDNGRVVESGS 552
|
250
....*....|....*..
gi 334185504 794 YEELLMMGTAFQQLVNA 810
Cdd:PRK13657 553 FDELVARGGRFAALLRA 569
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
609-788 |
5.52e-23 |
|
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: 97.29 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 609 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQTSWIQSG 675
Cdd:cd03246 11 PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDNIlygkpmesrrynaaikacaldkdmngfghgdlteigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:cd03246 91 SIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 334185504 756 HTAGVLFHKCVEDSLKEKTVILVTHQ-----------VMEEGTI 788
Cdd:cd03246 130 EGERALNQAIAALKAAGATRIVIAHRpetlasadrilVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
609-787 |
1.12e-22 |
|
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: 97.54 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 609 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQ--TSWIQ 673
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLVFQnpDDQFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 674 SGTIRDNILYG-------KPMESRRYNAAIKACaldkdmngfghgDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYL 745
Cdd:cd03225 90 GPTVEEEVAFGlenlglpEEEIEERVEEALELV------------GLEGLRDRSPfTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 746 LDDPFSAVDAHTAGVLFHKcVEDsLKE--KTVILVTHQ------------VMEEGT 787
Cdd:cd03225 158 LDEPTAGLDPAGRRELLEL-LKK-LKAegKTIIIVTHDldllleladrviVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
605-799 |
1.63e-22 |
|
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: 97.79 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 605 FGWEPETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSW 671
Cdd:COG1122 8 FSYPGGTPA--LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 672 IQ--SGTIRDNILYGkPMESRRYNAAIKAC---ALDKdmngFGhgdLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYL 745
Cdd:COG1122 86 DQlfAPTVEEDVAFG-PENLGLPREEIRERveeALEL----VG---LEHLADRPPhELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 746 LDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQ------------VMEEGTITQSGKYEELLM 799
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDldlvaeladrviVLDDGRIVADGTPREVFS 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1217-1411 |
2.94e-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: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1217 APLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGidiskiglkdlrmKLSIIPQEPTLFRGCIR 1296
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEPWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1297 TNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSAT- 1375
Cdd:cd03250 84 ENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVg 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 334185504 1376 DAIIQRIIREEFADC-TVITVAHRVPTVIDSDMVMVL 1411
Cdd:cd03250 164 RHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVL 200
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1205-1411 |
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 334185504 1205 HLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGidiskiglKDLRMKLSII 1284
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPLEKERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1285 ---PQE-------PTLFRGCIRTNLDP----LGVYSDDEIWKALEKcqLKTT-ISNLPNKLDSSVSdeGenwsvGQRQLF 1349
Cdd:cd03235 71 gyvPQRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADKAKVDEA--LERVgLSELADRQIGELS--G-----GQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 1350 CLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFAD-CTVITVAHRVPTVIDS-DMVMVL 1411
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYfDRVLLL 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
612-785 |
1.52e-21 |
|
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: 95.31 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------------SIAYVSQTSWIQSG-TIR 678
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRlTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 679 DNILY---GKPMESRRYNAAIKAcaLDKDMngfghgDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 754
Cdd:COG4555 93 ENIRYfaeLYGLFDEELKKRIEE--LIELL------GLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190
....*....|....*....|....*....|...
gi 334185504 755 AHTAGvLFHKCVEdSLKE--KTVILVTHQvMEE 785
Cdd:COG4555 165 VMARR-LLREILR-ALKKegKTVLFSSHI-MQE 194
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
616-785 |
3.38e-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: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGsiayvsQTSWIQSGTIRDNILYgKPMESRrynaa 695
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRIGY-LPEEPS----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 696 ikacaLDKDMNGFGHgdlteigqrgINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTV 775
Cdd:cd03230 84 -----LYENLTVREN----------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTI 148
|
170
....*....|
gi 334185504 776 ILVTHqVMEE 785
Cdd:cd03230 149 LLSSH-ILEE 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1204-1397 |
3.73e-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: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGlKDLRMKLSI 1283
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLFRgcirtNLdplgvysddeiwkalekcqlkTTISNLpnKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILV 1363
Cdd:cd03230 78 LPEEPSLYE-----NL---------------------TVRENL--KL-----------SGGMKQRLALAQALLHDPELLI 118
|
170 180 190
....*....|....*....|....*....|....*
gi 334185504 1364 LDEATASIDSATDAIIQRIIREEFAD-CTVITVAH 1397
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEgKTILLSSH 153
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1204-1414 |
3.99e-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: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG--LKDLRMKL 1281
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPTLFRGcirtnldplgvysddeiwkalekcqlKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKI 1361
Cdd:cd03229 79 GMVFQDFALFPH--------------------------LTVLENIALGL-----------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 1362 LVLDEATASIDSATDAIIQRIIREEFAD--CTVITVAHRVPTVID-SDMVMVLSFG 1414
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
616-798 |
4.20e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 96.75 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTV----KVFGS--------IAYVSQ--------Tswiqs 674
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPD-SGRIvlngRDLFTnlpprerrVGFVFQhyalfphmT----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 675 gtIRDNILYGkpMESRRYN-AAIKACA---LDK-DMNGFGHgdlteigQRGINLSGGQKQRIQLARAVYADADVYLLDDP 749
Cdd:COG1118 92 --VAENIAFG--LRVRPPSkAEIRARVeelLELvQLEGLAD-------RYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 750 FSAVDAHTAGVLfhkcvEDSLKE------KTVILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:COG1118 161 FGALDAKVRKEL-----RRWLRRlhdelgGTTVFVTHDqeealeladrvvVMNQGRIEQVGTPDEVY 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
610-780 |
4.70e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 93.32 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 610 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHaVLGEIPKV-SGTVKVFG-----------------SIAYVSQT-S 670
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGtdisklsekelaafrrrHIGFVFQSfN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 671 WIQSGTIRDNI-----LYGKPMESRRYNA--AIKACALDKDMNGFGHgdlteigqrgiNLSGGQKQRIQLARAVYADADV 743
Cdd:cd03255 93 LLPDLTALENVelpllLAGVPKKERRERAeeLLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 334185504 744 YLLDDPFSAVDAHTAGV---LFHKCVEDslKEKTVILVTH 780
Cdd:cd03255 162 ILADEPTGNLDSETGKEvmeLLRELNKE--AGTTIVVVTH 199
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
616-784 |
1.05e-20 |
|
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: 91.09 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG---------------SIAYVSQTSWIQSG-TIRD 679
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 680 NILYGkpmesrrynaaikacaldkdmngfghgdlteigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAG 759
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190
....*....|....*....|....*....|.
gi 334185504 760 VlfhkcVEDSLKE------KTVILVTHQVME 784
Cdd:cd03229 138 E-----VRALLKSlqaqlgITVVLVTHDLDE 163
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1204-1429 |
1.06e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 92.84 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKiglkdLRMKLSI 1283
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQeptlfrgciRTNLDP-----------LGVYSD------------DEIWKALEKCQL----KTTISNLpnkldssvsd 1336
Cdd:COG1121 80 VPQ---------RAEVDWdfpitvrdvvlMGRYGRrglfrrpsradrEAVDEALERVGLedlaDRPIGEL---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1337 egenwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFA-DCTVITVAHRVPTVID-SDMVMVLSfG 1414
Cdd:COG1121 141 -----SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREyFDRVLLLN-R 214
|
250
....*....|....*
gi 334185504 1415 DLVEYNEPSKLMETD 1429
Cdd:COG1121 215 GLVAHGPPEEVLTPE 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
610-809 |
1.47e-20 |
|
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: 92.84 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 610 ETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSG-TVKVFG-------------SIAYVS---QTSWI 672
Cdd:COG1119 15 GKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGerrggedvwelrkRIGLVSpalQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 673 QSGTIRDNIL---YGKPMESRRYNAAIKACALDKdMNGFGhgdLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDD 748
Cdd:COG1119 93 RDETVLDVVLsgfFDSIGLYREPTDEQRERAREL-LELLG---LAHLADRPFGtLSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 749 PFSAVDAHtAGVLFHKCVED--SLKEKTVILVTHQV------------MEEGTITQSGKYEELL---MMGTAFQQLVN 809
Cdd:COG1119 169 PTAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVeeippgithvllLKDGRVVAAGPKEEVLtseNLSEAFGLPVE 245
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
614-798 |
3.07e-20 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 91.59 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQtswiQSG----- 675
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQ----QIGlfphm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDNI-----LYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEigqrginLSGGQKQRIQLARAVYADADVYLLDDPF 750
Cdd:cd03295 91 TVEENIalvpkLLKWPKEKIRERADELLALVGLDPAEFADRYPHE-------LSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 751 SAVDAHTagvlfhkcvEDSLKE----------KTVILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:cd03295 164 GALDPIT---------RDQLQEefkrlqqelgKTIVFVTHDideafrladriaIMKNGEIVQVGTPDEIL 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
616-797 |
3.41e-20 |
|
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: 91.09 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-----LGEIPKVSGTVKVFGSIAYVSQTSWIQ---------------SG 675
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDVLElrrrvgmvfqkpnpfPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDNILYGKP---MESRRYNAAIKACALDKdmngfghGDLT-EIGQR--GINLSGGQKQRIQLARAVYADADVYLLDDP 749
Cdd:cd03260 96 SIYDNVAYGLRlhgIKLKEELDERVEEALRK-------AALWdEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 750 FSAVDAHTAGVlfhkcVEDSLKE----KTVILVTH---QV---------MEEGTITQSGKYEEL 797
Cdd:cd03260 169 TSALDPISTAK-----IEELIAElkkeYTIVIVTHnmqQAarvadrtafLLNGRLVEFGPTEQI 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1204-1438 |
5.00e-20 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 90.89 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKiGLKDLRMKLSI 1283
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLFRG-CIRTNLDPLGVY-------SDDEIWKALEKCqlkttisNLPNKLDSSVSdegeNWSVGQRQLFCLGRVL 1355
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFARLyglprkeARERIDELLELF-------GLTDAADRKVG----TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1356 LKRNKILVLDEATASIDSATDAIIQRIIREEFAD-CTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMET--DSY 1431
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARllEDV 226
|
....*..
gi 334185504 1432 FSKLVAE 1438
Cdd:COG1131 227 FLELTGE 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1203-1409 |
5.23e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.03 E-value: 5.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1203 TIHLQELKIRYRPNAPL---VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIS--KIGLKDL 1277
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1278 RMKLSIIPQEP--TLFRGCIRTNLD--P--LGVySDDEIWKALEKCqLKTTISNLPNKLDSSVSDegenWSVGQRQLFCL 1351
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIEKDIAfgPinLGL-SEEEIENRVKRA-MNIVGLDYEDYKDKSPFE----LSGGQKRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 1352 GRVLLKRNKILVLDEATASID-SATDAIIQRI--IREEFaDCTVITVAHR---VPTVIDSDMVM 1409
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDpKGRDEILNKIkeLHKEY-NMTIILVSHSmedVAKLADRIIVM 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
612-797 |
7.68e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.83 E-value: 7.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG-----------SIAYVSQtSWI--QSGTI 677
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPT-SGEILIGGrdvtdlppkdrNIAMVFQ-SYAlyPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 678 RDNILYgkPMESRRYNAAikacaldkdmngfghgdltEIGQR--------GI---------NLSGGQKQRIQLARAVYAD 740
Cdd:COG3839 93 YENIAF--PLKLRKVPKA-------------------EIDRRvreaaellGLedlldrkpkQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 741 ADVYLLDDPFSAVDAHTAGVL------FHKcvedSLKeKTVILVTH-Q-----------VMEEGTITQSGKYEEL 797
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMraeikrLHR----RLG-TTTIYVTHdQveamtladriaVMNDGRIQQVGTPEEL 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1204-1399 |
1.22e-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: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM---K 1280
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1281 LSIIPQEPTL--------------------FRGCirtnldpLGVYSDDEIWKA---LEKCQLKTTISNLPNKLdssvsde 1337
Cdd:cd03256 80 IGMIFQQFNLierlsvlenvlsgrlgrrstWRSL-------FGLFPKEEKQRAlaaLERVGLLDKAYQRADQL------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1338 genwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE---EFADcTVITVAHRV 1399
Cdd:cd03256 146 ----SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinrEEGI-TVIVSLHQV 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1204-1419 |
1.46e-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: 89.18 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI---SKIGLKDLR 1278
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1279 MKLSIIPQEPTLFRGciRTNLD----PLgvysddEIWKaLEKCQLKTTISNLPNKLDssVSDEGENW----SVGQRQLFC 1350
Cdd:cd03258 82 RRIGMIFQHFNLLSS--RTVFEnvalPL------EIAG-VPKAEIEERVLELLELVG--LEDKADAYpaqlSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1351 LGRVLLKRNKILVLDEATASIDSA-TDAIIQRI--IREEFaDCTVITVAHRVPTVID-SDMVMVLSFGDLVEY 1419
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPEtTQSILALLrdINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1204-1430 |
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 334185504 1204 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI---SKIGLKDLRMK 1280
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1281 LSIIPQEPTLFrgcirTNLD-------PL---GVYSDDEIWK-ALEKCQ---LKTTISNLPNKLdssvsdegenwSVGQR 1346
Cdd:cd03261 79 MGMLFQSGALF-----DSLTvfenvafPLrehTRLSEEEIREiVLEKLEavgLRGAEDLYPAEL-----------SGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1347 QLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPS 1423
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPE 222
|
....*..
gi 334185504 1424 KLMETDS 1430
Cdd:cd03261 223 ELRASDD 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
616-782 |
1.79e-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: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWI----------QSG------TIR 678
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGeDISGLSEAELYrlrrrmgmlfQSGalfdslTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 679 DNILYgkPM-ESRRYNAA-IKACALDKdmngfghgdLTEIGQRGI------NLSGGQKQRIQLARAVYADADVYLLDDPF 750
Cdd:cd03261 96 ENVAF--PLrEHTRLSEEeIREIVLEK---------LEAVGLRGAedlypaELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 334185504 751 SAVDAHTAGVlfhkcVED---SLKEK---TVILVTHQV 782
Cdd:cd03261 165 AGLDPIASGV-----IDDlirSLKKElglTSIMVTHDL 197
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
618-798 |
1.80e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.04 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 618 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVkvfgSIAYVSQT---------SWI-QSG------TIRDNI 681
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI----LWNGQDLTalppaerpvSMLfQENnlfphlTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 LYG-KPmeSRRYNAAIKA---CALDKdmngFGhgdLTEIGQR--GInLSGGQKQRIQLARAVYADADVYLLDDPFSAVD- 754
Cdd:COG3840 93 GLGlRP--GLKLTAEQRAqveQALER----VG---LAGLLDRlpGQ-LSGGQRQRVALARCLVRKRPILLLDEPFSALDp 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 755 AHTAGVLfhKCVEDSLKEK--TVILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:COG3840 163 ALRQEML--DLVDELCRERglTVLMVTHDpedaariadrvlLVADGRIAADGPTAALL 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
616-782 |
2.59e-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: 88.78 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGsiayVSQTSWI---------QSGTI--------R 678
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDG----TDINKLKgkalrqlrrQIGMIfqqfnlieR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 679 ----DNILYG--------KPMESRRYNAAIKAC--ALDK-DMNGFGHgdlteigQRGINLSGGQKQRIQLARAVYADADV 743
Cdd:cd03256 93 lsvlENVLSGrlgrrstwRSLFGLFPKEEKQRAlaALERvGLLDKAY-------QRADQLSGGQQQRVAIARALMQQPKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334185504 744 YLLDDPFSAVDAHTA----GVLFHKCVEdslKEKTVILVTHQV 782
Cdd:cd03256 166 ILADEPVASLDPASSrqvmDLLKRINRE---EGITVIVSLHQV 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1220-1412 |
3.10e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 94.71 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILI-DGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTN 1298
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1299 ----------LDPLGVYS------------------------------------------------DDEIWKALEKCQLK 1320
Cdd:PTZ00265 480 ikyslyslkdLEALSNYYnedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIH 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1321 TTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVIT--VAHR 1398
Cdd:PTZ00265 560 DFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITiiIAHR 639
|
250
....*....|....
gi 334185504 1399 VPTVIDSDMVMVLS 1412
Cdd:PTZ00265 640 LSTIRYANTIFVLS 653
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1204-1397 |
3.64e-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: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAP--LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDL---- 1277
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1278 RMKLSIIPQEPTLFRGciRTNLD----PL------GVYSDDEIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQ 1347
Cdd:cd03255 81 RRHIGFVFQSFNLLPD--LTALEnvelPLllagvpKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334185504 1348 LFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAH 1397
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTH 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
614-797 |
4.17e-19 |
|
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: 88.17 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG-----------SIAYVSQT-SWIQSGTIRDN 680
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERPD-SGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 ILYG---KPMESRRYNAAIKAcaldKDMNGFGHGDLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 756
Cdd:cd03296 95 VAFGlrvKPRSERPPEAEIRA----KVHELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 757 TAGVL--FHKCVEDSLKEKTViLVTHQ------------VMEEGTITQSGKYEEL 797
Cdd:cd03296 171 VRKELrrWLRRLHDELHVTTV-FVTHDqeealevadrvvVMNKGRIEQVGTPDEV 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1204-1397 |
5.90e-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: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKiGLKDLRMKLSI 1283
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLFrgcirTNLDPL----------GVYSDDEIwkalEKCQLKTTISNLPNKLDSSVSDegenWSVGQRQLFCLGR 1353
Cdd:cd03263 80 CPQFDALF-----DELTVRehlrfyarlkGLPKSEIK----EEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 334185504 1354 VLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAH 1397
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
616-797 |
6.27e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.16 E-value: 6.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG-----------SIAYVSQtswiqSG------TI 677
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPD-SGRILLDGrdvtglppekrNVGMVFQ-----DYalfphlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 678 RDNILYGkpMESRRYNAA-IKAC---ALDK-DMNGFGHgdlTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSA 752
Cdd:COG3842 95 AENVAFG--LRMRGVPKAeIRARvaeLLELvGLEGLAD---RYPHQ----LSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 753 VDAHTAGVLfhkcvEDSLKE------KTVILVTH-Q-----------VMEEGTITQSGKYEEL 797
Cdd:COG3842 166 LDAKLREEM-----REELRRlqrelgITFIYVTHdQeealaladriaVMNDGRIEQVGTPEEI 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1204-1397 |
7.53e-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: 7.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYR--PNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDL---- 1277
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1278 RMKLSIIPQE---------------PTLFRGCIRTNldplgvySDDEIWKALEKCQLKTTISNLPNKLdssvsdegenwS 1342
Cdd:COG1136 85 RRHIGFVFQFfnllpeltalenvalPLLLAGVSRKE-------RRERARELLERVGLGDRLDHRPSQL-----------S 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 1343 VGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE---EFaDCTVITVAH 1397
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnrEL-GTTIVMVTH 203
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
610-780 |
1.18e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 86.64 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 610 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHaVLGEIPKV-SGTVKVFG-----------------SIAYVSQTS- 670
Cdd:COG1136 18 EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdisslserelarlrrrHIGFVFQFFn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 671 WIQSGTIRDNILY-----GKPMESRRynAAIKAcALDKdmngFGhgdLTEIGQRGIN-LSGGQKQRIQLARAVYADADVY 744
Cdd:COG1136 97 LLPELTALENVALplllaGVSRKERR--ERARE-LLER----VG---LGDRLDHRPSqLSGGQQQRVAIARALVNRPKLI 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 334185504 745 LLDDPFSAVDAHTAGV---LFHKCVEDSlkEKTVILVTH 780
Cdd:COG1136 167 LADEPTGNLDSKTGEEvleLLRELNREL--GTTIVMVTH 203
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1204-1385 |
1.30e-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: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLkDLRMKLSI 1283
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLFRGC-IRTNLD------PLGVySDDEIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLL 1356
Cdd:COG4133 80 LGHADGLKPELtVRENLRfwaalyGLRA-DREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLLL 147
|
170 180
....*....|....*....|....*....
gi 334185504 1357 KRNKILVLDEATASIDSATDAIIQRIIRE 1385
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1204-1418 |
1.30e-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: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD---LRMK 1280
Cdd:COG2884 2 IRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1281 LSIIPQEPTLFRGciRTNLD----PLGV--YSDDEIWK----ALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFC 1350
Cdd:COG2884 81 IGVVFQDFRLLPD--RTVYEnvalPLRVtgKSRKEIRRrvreVLDLVGLSDKAKALPHEL-----------SGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1351 LGRVLLKRNKILVLDEATASIDSATdaiIQRIIR--EEFAD--CTVITVAHrvptviDSDM-------VMVLSFGDLVE 1418
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPET---SWEIMEllEEINRrgTTVLIATH------DLELvdrmpkrVLELEDGRLVR 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
609-798 |
1.30e-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: 91.12 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 609 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIP---KVSGTVKVFG-------------SIAYVSQTSWI 672
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGrdllelsealrgrRIGMVFQDPMT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 673 Q--SGTIRDNIlygkpMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDP 749
Cdd:COG1123 95 QlnPVTVGDQI-----AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 750 FSAVDAHTAgvlfhKCVEDSLKE------KTVILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:COG1123 170 TTALDVTTQ-----AEILDLLRElqrergTTVLLITHDlgvvaeiadrvvVMDDGRIVEDGPPEEIL 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
612-792 |
1.39e-18 |
|
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: 86.41 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG----------------SIAYVSQ---TSWI 672
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQdpmSSLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 673 QSGTIRDNILygKPMESRRYN---AAIKACALDKDMngfGHGDLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDD 748
Cdd:cd03257 97 PRMTIGEQIA--EPLRIHGKLskkEARKEAVLLLLV---GVGLPEEVLNRYPHeLSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 749 PFSAVDAHT-AGV--LFHKcvedsLKEK---TVILVTHQ------------VMEEGTITQSG 792
Cdd:cd03257 172 PTSALDVSVqAQIldLLKK-----LQEElglTLLFITHDlgvvakiadrvaVMYAGKIVEEG 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
612-798 |
2.23e-18 |
|
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: 85.71 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG----------------SIAYVSQT-SWIQ 673
Cdd:cd03258 17 KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPT-SGSVLVDGtdltllsgkelrkarrRIGMIFQHfNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 674 SGTIRDNILYgkPMESRRYNAAIKACALDKDMNGFGHGDLTEIgqRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAV 753
Cdd:cd03258 96 SRTVFENVAL--PLEIAGVPKAEIEERVLELLELVGLEDKADA--YPAQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 754 D-AHTAGVLfhkcveDSLKEK------TVILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:cd03258 172 DpETTQSIL------ALLRDInrelglTIVLITHEmevvkricdrvaVMEKGEVVEEGTVEEVF 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
604-780 |
2.68e-18 |
|
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: 85.00 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 604 NFGWEPETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKV----------FGSIAYVSQTSWIQ 673
Cdd:cd03226 6 SFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLngkpikakerRKSIGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 674 --SGTIRDNILYGKPMESRRYNAAikACALdKDMNGFGHGDlteigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFS 751
Cdd:cd03226 84 lfTDSVREELLLGLKELDAGNEQA--ETVL-KDLDLYALKE-----RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190
....*....|....*....|....*....|..
gi 334185504 752 AVDAHTA---GVLFHKCvedSLKEKTVILVTH 780
Cdd:cd03226 156 GLDYKNMervGELIREL---AAQGKAVIVITH 184
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
616-798 |
3.33e-18 |
|
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: 85.47 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-----------IAYVSQT-SWIQSGTIRDNILY 683
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 684 GkpMESRRYN-AAIKACALD-KDMNGFGHgdltEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVL 761
Cdd:cd03299 95 G--LKKRKVDkKEIERKVLEiAEMLGIDH----LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 334185504 762 FH--KCVEDSLkEKTVILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:cd03299 169 REelKKIRKEF-GVTVLHVTHDfeeawaladkvaIMLNGKLIQVGKPEEVF 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
612-810 |
3.38e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 85.63 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQ---TS----W 671
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrVQMVFQdpyASlhprH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 672 iqsgTIRDNI-----LYGKPMESRRYNAAIKACALDKD-MNGFGHgdlteigQrginLSGGQKQRIQLARAVYADADVYL 745
Cdd:COG1124 97 ----TVDRILaeplrIHGLPDREERIAELLEQVGLPPSfLDRYPH-------Q----LSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 746 LDDPFSAVDAHT-AGV--LFHKcvedsLKEK---TVILVTHQ------------VMEEGTITQSGKYEELLMMGT--AFQ 805
Cdd:COG1124 162 LDEPTSALDVSVqAEIlnLLKD-----LREErglTYLFVSHDlavvahlcdrvaVMQNGRIVEELTVADLLAGPKhpYTR 236
|
....*
gi 334185504 806 QLVNA 810
Cdd:COG1124 237 ELLAA 241
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1204-1427 |
3.98e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 86.22 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1283
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEP------TLFRGCIRTNLDPLGVYSDDEIWK---ALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRV 1354
Cdd:PRK13635 86 VFQNPdnqfvgATVQDDVAFGLENIGVPREEMVERvdqALRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1355 LLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLME 1427
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1204-1417 |
4.96e-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: 85.56 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG-LKDLRMKLS 1282
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1283 IIPQEPtlfrgcirTN--------------LDPLGVySDDEIWK----ALEKCQLKTTISNLPNKLdssvsdegenwSVG 1344
Cdd:TIGR04520 81 MVFQNP--------DNqfvgatveddvafgLENLGV-PREEMRKrvdeALKLVGMEDFRDREPHLL-----------SGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1345 QRQLFCLGRVLLKRNKILVLDEATASIDSATD----AIIQRIIREEfaDCTVITVAHRVPTVIDSDMVMVLSFGDLV 1417
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRkevlETIRKLNKEE--GITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1204-1429 |
5.70e-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: 5.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG---LKDLRMK 1280
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1281 LSIIPQEPTLFrgcirTNLD-------PL---GVYSDDEIWK-ALEKCQ---LKTTISNLPNKLdssvsdegenwSVGQR 1346
Cdd:COG1127 84 IGMLFQGGALF-----DSLTvfenvafPLrehTDLSEAEIRElVLEKLElvgLPGAADKMPSEL-----------SGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1347 QlfclgRVLLKRN-----KILVLDEATASIDSATDAIIQRIIRE---EFaDCTVITVAHRVPTVID-SDMVMVLSFGDLV 1417
Cdd:COG1127 148 K-----RVALARAlaldpEILLYDEPTAGLDPITSAVIDELIRElrdEL-GLTSVVVTHDLDSAFAiADRVAVLADGKII 221
|
250
....*....|..
gi 334185504 1418 EYNEPSKLMETD 1429
Cdd:COG1127 222 AEGTPEELLASD 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1204-1417 |
6.45e-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: 83.78 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNapLVLKGISCTFREGTrVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKdLRMKLSI 1283
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLF-RGCIRTNLDPLGVYS-------DDEIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVL 1355
Cdd:cd03264 77 LPQEFGVYpNFTVREFLDYIAWLKgipskevKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1356 LKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDS-DMVMVLSFGDLV 1417
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLV 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1204-1425 |
6.96e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.67 E-value: 6.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDISKIGLKDLRMKL 1281
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEP--TLFRGCIRTNLDpLGVYS----DDEIWKALEKCQLKTTISNLPNKLDSSVsdegenwSVGQRQLFCLGRVL 1355
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVS-FGAVNlklpEDEVRKRVDNALKRTGIEHLKDKPTHCL-------SFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1356 LKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTV-IDSDMVMVLSFGDLVEYNEPSKL 1425
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1204-1419 |
7.89e-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: 7.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEP---ASGCILIDGIDISKIG---LK 1275
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1276 DLRMK-LSIIPQEPTlfrgcirTNLDPL--------------GVYSDDEIWK----ALEKCQL---KTTISNLPNKLdss 1333
Cdd:COG0444 82 KIRGReIQMIFQDPM-------TSLNPVmtvgdqiaeplrihGGLSKAEAREraieLLERVGLpdpERRLDRYPHEL--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1334 vsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATasidSATDAIIQRII-------REEFaDCTVITVAHRVPTV--Id 1404
Cdd:COG0444 152 --------SGGMRQRVMIARALALEPKLLIADEPT----TALDVTIQAQIlnllkdlQREL-GLAILFITHDLGVVaeI- 217
|
250
....*....|....*
gi 334185504 1405 SDMVMVLSFGDLVEY 1419
Cdd:COG0444 218 ADRVAVMYAGRIVEE 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1204-1418 |
1.74e-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: 82.57 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISkiGLKDLRMKLSI 1283
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLF-----RGCIRTNLDPLGVYSDDEIWKALEKCQLkTTISNLPNKLDSSVSdeGenwsvGQRQLFCLGRVLLKR 1358
Cdd:cd03259 77 VFQDYALFphltvAENIAFGLKLRGVPKAEIRARVRELLEL-VGLEGLLNRYPHELS--G-----GQQQRVALARALARE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1359 NKILVLDEATasidSATDAIIQRIIREEFAD------CTVITVAHrvptviD-------SDMVMVLSFGDLVE 1418
Cdd:cd03259 149 PSLLLLDEPL----SALDAKLREELREELKElqrelgITTIYVTH------DqeealalADRIAVMNEGRIVQ 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1220-1418 |
2.20e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.42 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVE-----PASGCILIDGIDISKIGLKDLRMKLSIIPQEP------ 1288
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1289 TLFRG-CIRTNLDPLgVYSDDEIWK----ALEKCQLKTTISnlpNKLDSSVSdegeNWSVGQRQLFCLGRVLLKRNKILV 1363
Cdd:PRK14247 98 SIFENvALGLKLNRL-VKSKKELQErvrwALEKAQLWDEVK---DRLDAPAG----KLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 1364 LDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVID-SDMVMVLSFGDLVE 1418
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVE 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
614-780 |
2.20e-17 |
|
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: 80.19 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--SIAYVSQtswiqsgtirdnilygkpmesrr 691
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ----------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 692 ynaaikacaldkdmngfghgdlteigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLfhkcvEDSLK 771
Cdd:cd03221 71 -------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL-----EEALK 114
|
170
....*....|.
gi 334185504 772 E--KTVILVTH 780
Cdd:cd03221 115 EypGTVILVSH 125
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
612-798 |
2.25e-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: 82.48 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQTSWIQSG-T 676
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 677 IRDNILYGkpmESRRYNAAIKAcALDK--DMngFghGDLTEI-GQRGINLSGGQKQRIQLARAVYADADVYLLDDPfsav 753
Cdd:cd03224 92 VEENLLLG---AYARRRAKRKA-RLERvyEL--F--PRLKERrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP---- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 754 dahTAGvLFHKCVED------SLKEK--TVILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:cd03224 160 ---SEG-LAPKIVEEifeairELRDEgvTILLVEQNarfaleiadrayVLERGRVVLEGTAAELL 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
616-792 |
2.29e-17 |
|
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: 82.34 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIK---HGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-----------------IAYVSQT-SWIQS 674
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQyALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 675 GTIRDNILYGKPmesRRYNAAIKACAlDKDMNGFGhgdLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAV 753
Cdd:cd03297 90 LNVRENLAFGLK---RKRNREDRISV-DELLDLLG---LDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 334185504 754 DAHTAGVLfHKCVEDSLKE--KTVILVTHQ------------VMEEGTITQSG 792
Cdd:cd03297 163 DRALRLQL-LPELKQIKKNlnIPVIFVTHDlseaeyladrivVMEDGRLQYIG 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
614-802 |
4.83e-17 |
|
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: 81.78 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------------SIAYVSQTSWIQSG-TIRDN 680
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 I-----LYGKPMESRRYNAA--IKACALDKDMNgfghgdlTEIGqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAV 753
Cdd:cd03263 96 LrfyarLKGLPKSEIKEEVEllLRVLGLTDKAN-------KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 754 DAHTAGVLFhKCVEDSLKEKTVILVTHQvMEEG-------TITQSGKyeeLLMMGT 802
Cdd:cd03263 165 DPASRRAIW-DLILEVRKGRSIILTTHS-MDEAealcdriAIMSDGK---LRCIGS 215
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1220-1417 |
9.37e-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: 9.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD-LRMKLSIIPQEPTLFRG-CIRT 1297
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1298 NLDpLGVYsddeiwkALEKCQLKTTISNL----PnKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATA---- 1369
Cdd:cd03224 95 NLL-LGAY-------ARRRAKRKARLERVyelfP-RLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEglap 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334185504 1370 SIDSATDAIIQRIIREEFadcTVITVAHRVPTVID-SDMVMVLSFGDLV 1417
Cdd:cd03224 166 KIVEEIFEAIRELRDEGV---TILLVEQNARFALEiADRAYVLERGRVV 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
616-799 |
9.79e-17 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 81.92 E-value: 9.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWI-----------QS------GTI 677
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqDIAAMSRKELRelrrkkismvfQSfallphRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 678 RDNILYGkpMESR------RYNAAIKACALdKDMNGFGHGDLTEigqrginLSGGQKQRIQLARAVYADADVYLLDDPFS 751
Cdd:cd03294 120 LENVAFG--LEVQgvpraeREERAAEALEL-VGLEGWEHKYPDE-------LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 752 AVDAhtagvLFHKCVEDSL------KEKTVILVTHQ------------VMEEGTITQSGKYEELLM 799
Cdd:cd03294 190 ALDP-----LIRREMQDELlrlqaeLQKTIVFITHDldealrlgdriaIMKDGRLVQVGTPEEILT 250
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1220-1428 |
1.15e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.63 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVE------PASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRG 1293
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1294 C-----IRTNLDPLGVYSDDEIWKALEKCQLKTTI-SNLPNKLDSSVSdegeNWSVGQRQLFCLGRVLLKRNKILVLDEA 1367
Cdd:PRK14246 105 LsiydnIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPAS----QLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 1368 TASIDSATDAIIQRIIREEFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMET 1428
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
614-781 |
1.27e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.24 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKV--FGSIAYVSQTSWIQSGTIRDNILYgkPMESRR 691
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLY--PATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 692 Y-NAAIKAcALDKdmNGFGH--GDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKcVED 768
Cdd:COG4178 455 FsDAELRE-ALEA--VGLGHlaERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LRE 530
|
170
....*....|...
gi 334185504 769 SLKEKTVILVTHQ 781
Cdd:COG4178 531 ELPGTTVISVGHR 543
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1164-1439 |
1.44e-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: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1164 TLSNSIISVERIKQYMNIPE-EPPAIidDKRPPSSWPSNgTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGS 1242
Cdd:TIGR00957 599 SIVQASVSLKRLRIFLSHEElEPDSI--ERRTIKPGEGN-SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGC 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1243 GKSTLISALFRLVEPASGCILIDGidiskiglkdlrmKLSIIPQEPTLFRGCIRTNLdPLGVYSDDEIWKA-LEKCQLKT 1321
Cdd:TIGR00957 676 GKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENI-LFGKALNEKYYQQvLEACALLP 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1322 TISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDS-ATDAIIQRIIREE--FADCTVITVAHR 1398
Cdd:TIGR00957 742 DLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPEgvLKNKTRILVTHG 821
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 334185504 1399 VPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLVAEY 1439
Cdd:TIGR00957 822 ISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTY 862
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1204-1397 |
1.47e-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: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYrPNAPLvlkGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGlKDLRmKLSI 1283
Cdd:COG3840 2 LRLDDLTYRY-GDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-PAER-PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLFRG-CIRTN----LDPLGVYSDDE---IWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVL 1355
Cdd:COG3840 76 LFQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARCL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 334185504 1356 LKRNKILVLDEATASIDSATDA----IIQRIIREEFAdcTVITVAH 1397
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQemldLVDELCRERGL--TVLMVTH 188
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1204-1409 |
1.58e-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: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLkDLRMKL 1281
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPTLF-RGCIRTNLDPLG-VYsddeiwkALEKCQLKTTISNLPNKLD--SSVSDEGENWSVGQRQLFCLGRVLLK 1357
Cdd:cd03266 81 GFVSDSTGLYdRLTARENLEYFAgLY-------GLKGDELTARLEELADRLGmeELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 1358 RNKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHR---VPTVIDSDMVM 1409
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHImqeVERLCDRVVVL 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
611-797 |
1.65e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.82 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 611 TKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-----------IAYVSQT-SWIQSGTIR 678
Cdd:PRK10851 15 TQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 679 DNILYGKPMESRRYN---AAIKAcaldKDMNGFGHGDLTEIGQR-GINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 754
Cdd:PRK10851 93 DNIAFGLTVLPRRERpnaAAIKA----KVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 755 AHTAGVL--FHKCVEDSLKeKTVILVTHQ------------VMEEGTITQSGKYEEL 797
Cdd:PRK10851 169 AQVRKELrrWLRQLHEELK-FTSVFVTHDqeeamevadrvvVMSQGNIEQAGTPDQV 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
616-798 |
2.07e-16 |
|
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: 80.41 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWI----------QSG------TIR 678
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYelrrrigmlfQGGalfdslTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 679 DNILYgkPM-ESRRYNAA-IKACALDKdmngfghgdLTEIGQRGIN------LSGGQKQRIQLARAVYADADVYLLDDPF 750
Cdd:COG1127 101 ENVAF--PLrEHTDLSEAeIRELVLEK---------LELVGLPGAAdkmpseLSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 751 SAVDAHTAGVlFHKCVEDsLKEK---TVILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:COG1127 170 AGLDPITSAV-IDELIRE-LRDElglTSVVVTHDldsafaiadrvaVLADGKIIAEGTPEELL 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
614-784 |
2.62e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSI--------AYVSQTS----WIqsgTIRDNI 681
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNEgllpWR---NVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 -----LYGKPMESRRYNAaikacaldKDMngFGHGDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:PRK11248 92 afglqLAGVEKMQRLEIA--------HQM--LKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190
....*....|....*....|....*....|..
gi 334185504 756 HT---AGVLFHKCVEDSLKEktVILVTHQVME 784
Cdd:PRK11248 162 FTreqMQTLLLKLWQETGKQ--VLLITHDIEE 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
613-825 |
2.77e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 613 IPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQ-TSWIQSGTIR 678
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQdTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 679 DNILYGKPMESRRYNAAIKA--CALDKDMNgfgHGDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:PRK09536 96 QVVEMGRTPHRSRFDTWTETdrAAVERAME---RTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 756 HTAG---VLFHKCVEDSlkeKTVILVTHQ------------VMEEGTITQSGKYEELLMMGT---AF--QQLV--NAHND 813
Cdd:PRK09536 173 NHQVrtlELVRRLVDDG---KTAVAAIHDldlaarycdelvLLADGRVRAAGPPADVLTADTlraAFdaRTAVgtDPATG 249
|
250
....*....|..
gi 334185504 814 AVTVLPLASNES 825
Cdd:PRK09536 250 APTVTPLPDPDR 261
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
614-802 |
3.95e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.91 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSI--------AYVSQTS----WIqsgTIRDNI 681
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKDallpWL---NVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 -----LYGKPMESRRynaAIKACALDKdmngfghGDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:COG4525 98 afglrLRGVPKAERR---ARAEELLAL-------VGLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 756 HTagvlfhkcvEDSLKE----------KTVILVTHQVmeegtitqsgkyEELLMMGT 802
Cdd:COG4525 168 LT---------REQMQEllldvwqrtgKGVFLITHSV------------EEALFLAT 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1201-1428 |
4.16e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.52 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1201 NGTIHLQELKIRYRPNAPL-VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM 1279
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1280 KLSIIPQEP-TLFRGCIRTNLDPLGVYSD----DEIWKALEKCQLKTTISNLPNKldssvsdEGENWSVGQRQLFCLGRV 1354
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLAVNMLDFKTR-------EPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 1355 LLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMET 1428
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEikEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFAT 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1213-1434 |
4.27e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.64 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1213 YRPNAPLVLKG---ISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI----SKIGLKDLRMKLSIIP 1285
Cdd:PRK13641 12 YSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1286 Q--EPTLFRGCIRTNLD--PLGV-YSDDE----IWKALEKCQLKTT-ISNLPNKLdssvsdegenwSVGQRQLFCLGRVL 1355
Cdd:PRK13641 92 QfpEAQLFENTVLKDVEfgPKNFgFSEDEakekALKWLKKVGLSEDlISKSPFEL-----------SGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1356 LKRNKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMETDSYFS 1433
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKEWLK 240
|
.
gi 334185504 1434 K 1434
Cdd:PRK13641 241 K 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
616-780 |
5.57e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--SIAYVSQ-TSWIQSGTIRDNILYGKP----ME 688
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQePPLDDDLTVLDTVLDGDAelraLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 689 SRRYNAAIKACALDKDMNGFG--HGDLTEIG-----QR--------GI----------NLSGGQKQRIQLARAVYADADV 743
Cdd:COG0488 94 AELEELEAKLAEPDEDLERLAelQEEFEALGgweaeARaeeilsglGFpeedldrpvsELSGGWRRRVALARALLSEPDL 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 334185504 744 YLLDDPFSAVDAHTAGVLfhkcvEDSLK--EKTVILVTH 780
Cdd:COG0488 174 LLLDEPTNHLDLESIEWL-----EEFLKnyPGTVLVVSH 207
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
616-795 |
6.45e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS----------IAYVSQTS---WIQSGTIRDNIL 682
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 683 ---YGKPMESRRYNAAIKAC---ALDK-DMNGFGHgdlTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:PRK15056 103 mgrYGHMGWLRRAKKRDRQIvtaALARvDMVEFRH---RQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 334185504 756 HTAGVLFHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYE 795
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHNlgsvtefcdytVMVKGTVLASGPTE 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1204-1426 |
9.36e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 9.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG-LKDLRMKLS 1282
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1283 IIPQEP-TLFRGciRTNLDPLGVYSDD------EIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVL 1355
Cdd:PRK13644 81 IVFQNPeTQFVG--RTVEEDLAFGPENlclppiEIRKRVDRALAEIGLEKYRHRSPKTLSG-------GQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 1356 LKRNKILVLDEATASID-SATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLM 1426
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDpDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1204-1372 |
9.93e-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: 9.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI--SKIGLKDLRMKL 1281
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPTLFRGciRTNLD-----PLGVY--SDDEI----WKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFC 1350
Cdd:cd03262 79 GMVFQQFNLFPH--LTVLEnitlaPIKVKgmSKAEAeeraLELLEKVGLADKADAYPAQL-----------SGGQQQRVA 145
|
170 180
....*....|....*....|..
gi 334185504 1351 LGRVLLKRNKILVLDEATASID 1372
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALD 167
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
616-788 |
1.07e-15 |
|
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: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFGSIAYVSQTSWI----------QS------GTIR 678
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLlEEPD-SGTIIIDGLKLTDDKKNINelrqkvgmvfQQfnlfphLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 679 DNILYGkPMESRRYN-AAIKACALDKdmngfghgdLTEIG------QRGINLSGGQKQRIQLARAVYADADVYLLDDPFS 751
Cdd:cd03262 95 ENITLA-PIKVKGMSkAEAEERALEL---------LEKVGladkadAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 334185504 752 AVDAHTAG-VLfhKCVEDSLKEK-TVILVTHQV------------MEEGTI 788
Cdd:cd03262 165 ALDPELVGeVL--DVMKDLAEEGmTMVVVTHEMgfarevadrvifMDDGRI 213
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
616-781 |
1.26e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.04 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--IAYVSQTSWIQSGTIRDNILYgkpmesrryn 693
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGedLLFLPQRPYLPLGTLREQLIY---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 694 aaikacALDKdmngfghgdlteigqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLkek 773
Cdd:cd03223 87 ------PWDD------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI--- 139
|
....*...
gi 334185504 774 TVILVTHQ 781
Cdd:cd03223 140 TVISVGHR 147
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
611-780 |
1.39e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.40 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 611 TKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG----------------SIAYVSQTSW-IQ 673
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQDFRlLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 674 SGTIRDNILYgkPME-----SRRYNAAIKAcALDKdmngFGHGDLteIGQRGINLSGGQKQRIQLARAVYADADVYLLDD 748
Cdd:COG2884 93 DRTVYENVAL--PLRvtgksRKEIRRRVRE-VLDL----VGLSDK--AKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 334185504 749 PFSAVDAHTAGVLFhkcveDSLKE-----KTVILVTH 780
Cdd:COG2884 164 PTGNLDPETSWEIM-----ELLEEinrrgTTVLIATH 195
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
605-798 |
1.54e-15 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 81.49 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 605 FGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG----------------SIAYVSQ 668
Cdd:COG1123 270 YPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 669 ---TSWIQSGTIRDNILYG--------KPMESRRYNAAIKACALDKD-MNGFGHGdlteigqrginLSGGQKQRIQLARA 736
Cdd:COG1123 350 dpySSLNPRMTVGDIIAEPlrlhgllsRAERRERVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 737 VYADADVYLLDDPFSAVDAHT-AGVLfhkcveDSLKE------KTVILVTHQ------------VMEEGTITQSGKYEEL 797
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVqAQIL------NLLRDlqrelgLTYLFISHDlavvryiadrvaVMYDGRIVEDGPTEEV 492
|
.
gi 334185504 798 L 798
Cdd:COG1123 493 F 493
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
616-780 |
1.92e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVfGS---IAYVSQTswiQSG-----TIRDNILYGKP- 686
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQH---QEEldpdkTVLDELRDGAPg 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 687 ---MESRRYnaaikacaldkdMNGFG-HGD--LTEIGqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGV 760
Cdd:COG0488 407 gteQEVRGY------------LGRFLfSGDdaFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEA 470
|
170 180
....*....|....*....|..
gi 334185504 761 LfhkcvEDSLK--EKTVILVTH 780
Cdd:COG0488 471 L-----EEALDdfPGTVLLVSH 487
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1203-1426 |
2.24e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1203 TIHLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLS 1282
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1283 IIPQEPTLFRGCIRTNLDPLG----------VYSDDE--IWKALEkcqlKTTISNLPNKLDSSVSDegenwsvGQRQLFC 1350
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGrspwlslwgrLSAEDNarVNQAME----QTRINHLADRRLTDLSG-------GQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1351 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHrvptviD-------SDMVMVLSFGDLVEYNEP 1422
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRElNTQGKTVVTVLH------DlnqasryCDHLVVLANGHVMAQGTP 222
|
....
gi 334185504 1423 SKLM 1426
Cdd:PRK11231 223 EEVM 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
614-780 |
2.73e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.37 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIP---KVSGTVKVFGS-----------IAYVSQTS-----Wiqs 674
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRrltalpaeqrrIGILFQDDllfphL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 675 gTIRDNILYGKPMESRRYN--AAIKAcALDK-DMNGFGHGDLTEigqrginLSGGQKQRIQLARAVYADADVYLLDDPFS 751
Cdd:COG4136 92 -SVGENLAFALPPTIGRAQrrARVEQ-ALEEaGLAGFADRDPAT-------LSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|.
gi 334185504 752 AVDAHTAgVLFHKCVEDSLKEKT--VILVTH 780
Cdd:COG4136 163 KLDAALR-AQFREFVFEQIRQRGipALLVTH 192
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
614-792 |
2.76e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 76.30 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSGTIRDN 680
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 I-LYGKPMESRRYNAaikacaldkdmngfghgdlTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTaG 759
Cdd:cd03369 102 LdPFDEYSDEEIYGA-------------------LRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-D 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 334185504 760 VLFHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSG 792
Cdd:cd03369 162 ALIQKTIREEFTNSTILTIAHRlrtiidydkilVMDAGEVKEYD 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1204-1426 |
3.13e-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: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVlKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1283
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLFRGciRTNLDPLGVYSDDEIWKaleKCQLKTTISNL-------PNKLDSSVSDEgenWSVGQRQLFCLGRVLL 1356
Cdd:cd03295 80 VIQQIGLFPH--MTVEENIALVPKLLKWP---KEKIRERADELlalvgldPAEFADRYPHE---LSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1357 KRNKILVLDEATasidSATDAIIQRIIREEFADC------TVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLM 1426
Cdd:cd03295 152 ADPPLLLMDEPF----GALDPITRDQLQEEFKRLqqelgkTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
606-792 |
3.71e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 76.16 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 606 GWEPETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPK---VSGTVKVFG----------SIAYVSQTS-W 671
Cdd:cd03234 15 NWNKYARI--LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGqprkpdqfqkCVAYVRQDDiL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 672 IQSGTIRDNILYGKPMESRRY--NAAIKACALDKDMNGFGHGDLTeiGQRGINLSGGQKQRIQLARAVYADADVYLLDDP 749
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKssDAIRKKRVEDVLLRDLALTRIG--GNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 750 FSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQ-------------VMEEGTITQSG 792
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQprsdlfrlfdrilLLSSGEIVYSG 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1220-1372 |
3.99e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTL---FRGCI- 1295
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVRQv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1296 --------RTNLDPLGvySDDEiwKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLDEA 1367
Cdd:PRK09536 98 vemgrtphRSRFDTWT--ETDR--AAVERAMERTGVAQFADRPVTSLSG-------GERQRVLLARALAQATPVLLLDEP 166
|
....*
gi 334185504 1368 TASID 1372
Cdd:PRK09536 167 TASLD 171
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
616-785 |
4.33e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 74.39 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGsiayvsqtswiqsgtirdnilygKPMESRRYNAA 695
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------------------KEVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 696 IKAcaldkdmngfghgdlteigqrGIN----LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFhKCVEDsLK 771
Cdd:cd03216 73 RRA---------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF-KVIRR-LR 129
|
170
....*....|....*.
gi 334185504 772 E--KTVILVTHQvMEE 785
Cdd:cd03216 130 AqgVAVIFISHR-LDE 144
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1225-1399 |
4.97e-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: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1225 SCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISkiGLKDLRMKLSIIPQEPTLFRG-CIRTNLDpLG 1303
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVG-LG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1304 VYS----DDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAII 1379
Cdd:cd03298 95 LSPglklTAEDRQAIEVALARVGLAGLEKRLPGELSG-------GERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180
....*....|....*....|..
gi 334185504 1380 QRIIREEFAD--CTVITVAHRV 1399
Cdd:cd03298 168 LDLVLDLHAEtkMTVLMVTHQP 189
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
621-791 |
5.31e-15 |
|
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: 75.67 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 621 LEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKV-----FGSIAYVSQTSWI-QSG------TIRDNILYGkpme 688
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVndqshTGLAPYQRPVSMLfQENnlfahlTVRQNIGLG---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 689 srrYNAAIKACALDKD-----MNGFGHGDLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD----AHTAG 759
Cdd:TIGR01277 95 ---LHPGLKLNAEQQEkvvdaAQQVGIADYLD--RLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllrEEMLA 169
|
170 180 190
....*....|....*....|....*....|...
gi 334185504 760 VLFHKCVEdslKEKTVILVTHQVME-EGTITQS 791
Cdd:TIGR01277 170 LVKQLCSE---RQRTLLMVTHHLSDaRAIASQI 199
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
612-798 |
7.07e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 75.79 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQTSWIQSG-T 676
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 677 IRDNILYGkpMESRRYNAAIKAcaldkdmngfghgDLTEI-----------GQRGINLSGGQKQriQLA--RAVYADADV 743
Cdd:COG0410 95 VEENLLLG--AYARRDRAEVRA-------------DLERVyelfprlkerrRQRAGTLSGGEQQ--MLAigRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 744 YLLDDPfsavdahTAGV-------LFHKCVEdsLKEK--TVILV---THQ---------VMEEGTITQSGKYEELL 798
Cdd:COG0410 158 LLLDEP-------SLGLapliveeIFEIIRR--LNREgvTILLVeqnARFaleiadrayVLERGRIVLEGTAAELL 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
616-792 |
7.54e-15 |
|
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: 75.26 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQtswIQSG-----TIRDNIlygkpmesr 690
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG---LGGGfnpelTGRENI--------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 691 RYNAAIKACaLDKDMNGFGHG--DLTEIGQRgINL-----SGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAgvlfH 763
Cdd:cd03220 106 YLNGRLLGL-SRKEIDEKIDEiiEFSELGDF-IDLpvktySSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ----E 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 334185504 764 KCVE--DSLKE--KTVILVTHQ------------VMEEGTITQSG 792
Cdd:cd03220 180 KCQRrlRELLKqgKTVILVSHDpssikrlcdralVLEKGKIRFDG 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1201-1427 |
7.86e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.03 E-value: 7.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1201 NGTIHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVE-----PASGCILIDGIDI--SKIG 1273
Cdd:PRK14267 2 KFAIETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1274 LKDLRMKLSIIPQEPTLF-------RGCIRTNLDPLgVYSDDEIWKALEKCQLKTTisnLPNKLDSSVSDEGENWSVGQR 1346
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFphltiydNVAIGVKLNGL-VKSKKELDERVEWALKKAA---LWDEVKDRLNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1347 QLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAH------RVptvidSDMVMVLSFGDLVEYN 1420
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaqaaRV-----SDYVAFLYLGKLIEVG 230
|
....*..
gi 334185504 1421 EPSKLME 1427
Cdd:PRK14267 231 PTRKVFE 237
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
616-798 |
7.93e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 75.80 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG--------SIAYVSQtswiQSG----------- 675
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLlEEPD-SGTITVDGedltdskkDINKLRR----KVGmvfqqfnlfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 -TIRDNILYGkPMESRRYN---AAIKACALdkdmngfghgdLTEIG------QRGINLSGGQKQRIQLARAVYADADVYL 745
Cdd:COG1126 92 lTVLENVTLA-PIKVKKMSkaeAEERAMEL-----------LERVGladkadAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 746 LDDPFSAVDAHTAGVlfhkcVEDSLKE-----KTVILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:COG1126 160 FDEPTSALDPELVGE-----VLDVMRDlakegMTMVVVTHEmgfarevadrvvFMDGGRIVEEGPPEEFF 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1208-1425 |
9.18e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.20 E-value: 9.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1208 ELKIRYRpNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDISKIGLKDLRMKLSIIP 1285
Cdd:PRK13638 6 DLWFRYQ-DEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1286 QEP------TLFRGCIRTNLDPLGVySDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRN 1359
Cdd:PRK13638 84 QDPeqqifyTDIDSDIAFSLRNLGV-PEAEITRRVDEALTLVDAQHFRHQPIQCLSH-------GQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 1360 KILVLDEATASIDSATD----AIIQRIIREefaDCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKL 1425
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRtqmiAIIRRIVAQ---GNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEV 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
616-785 |
9.98e-15 |
|
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: 74.62 E-value: 9.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS---------IAYVSQTSWI-QSGTIRDNILY-- 683
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEERGLyPKMKVIDQLVYla 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 684 ---G-KPMESRRynaaikacALDKDMNGFGHGDLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAG 759
Cdd:cd03269 96 qlkGlKKEEARR--------RIDEWLERLELSEYAN--KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180
....*....|....*....|....*.
gi 334185504 760 VLFHKCVEDSLKEKTVILVTHQvMEE 785
Cdd:cd03269 166 LLKDVIRELARAGKTVILSTHQ-MEL 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1204-1397 |
1.01e-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: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISkiGLKD-----LR 1278
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1279 MKLSIIPQEPTLfrgcirtnLDPLGVYSD------------DEIWK----ALEKCQLKTTISNLPNKLdssvsdegenwS 1342
Cdd:cd03292 78 RKIGVVFQDFRL--------LPDRNVYENvafalevtgvppREIRKrvpaALELVGLSHKHRALPAEL-----------S 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 1343 VGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAH 1397
Cdd:cd03292 139 GGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATH 194
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1220-1414 |
1.27e-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: 74.78 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISkiGLK-DLRMKLSIIP--QEPTLFRGC-- 1294
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT--GLPpHEIARLGIGRtfQIPRLFPELtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1295 ---------IRTNLDPLGVYSDDEIWKALEKCQ--LKTTisNLPNKLDSSVSdegeNWSVGQRQLFCLGRVLLKRNKILV 1363
Cdd:cd03219 93 lenvmvaaqARTGSGLLLARARREEREARERAEelLERV--GLADLADRPAG----ELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1364 LDEATASIDSA-TDAIIQRI--IREEfaDCTVITVAHRVPTVID-SDMVMVLSFG 1414
Cdd:cd03219 167 LDEPAAGLNPEeTEELAELIreLRER--GITVLLVEHDMDVVMSlADRVTVLDQG 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1220-1402 |
1.28e-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: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKiglkdlrmkLSIIPQEPTLFRG------ 1293
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE---------QRDEPHENILYLGhlpglk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1294 ---CIRTNLD---PLGVYSDDEIWKALEKCQLkTTISNLP-NKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDE 1366
Cdd:TIGR01189 86 pelSALENLHfwaAIHGGAQRTIEDALAAVGL-TGFEDLPaAQL-----------SAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 334185504 1367 ATASIDSATDAIIQRIIREEFAD--CTVITVAHRVPTV 1402
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARggIVLLTTHQDLGLV 191
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
612-792 |
1.40e-14 |
|
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: 74.21 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------SIAYVSQT-SWIQSGTIRD 679
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 680 NILYgkPMESRRY-NAAIKACALD-KDMNGFGHgdltEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH- 756
Cdd:cd03301 92 NIAF--GLKLRKVpKDEIDERVREvAELLQIEH----LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKl 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 334185504 757 -----TAGVLFHKCVedslkEKTVILVTHQ------------VMEEGTITQSG 792
Cdd:cd03301 166 rvqmrAELKRLQQRL-----GTTTIYVTHDqveamtmadriaVMNDGQIQQIG 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
616-784 |
1.82e-14 |
|
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: 74.42 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS---------IAYVSQTSWIQSGTIRDNILYGKP 686
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqitepgpdrMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 687 MESRRYNAAIKACALDK--DMNGFGHGDLTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVL--- 761
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEhiALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLqee 156
|
170 180
....*....|....*....|...
gi 334185504 762 FHKCVEDSlkEKTVILVTHQVME 784
Cdd:TIGR01184 157 LMQIWEEH--RVTVLMVTHDVDE 177
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1204-1412 |
1.82e-14 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 74.05 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPN--APLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLkdlrmKL 1281
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPTLFRGciRTNLD----PL---GVySDDEIW----KALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFC 1350
Cdd:cd03293 76 GYVFQQDALLPW--LTVLDnvalGLelqGV-PKAEAReraeELLELVGLSGFENAYPHQL-----------SGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 1351 LGRVLLKRNKILVLDEATASIDSATDAIIQ----RIIREEFAdcTVITVAHRvptvID-----SDMVMVLS 1412
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 ... |
1220-1417 |
1.98e-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: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDlrmklsiipqepTLFRGcIRTnl 1299
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD------------ARRAG-IAM-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1300 dplgVYsddeiwkalekcQLkttisnlpnkldssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSA-TDAI 1378
Cdd:cd03216 80 ----VY------------QL----------------------SVGERQMVEIARALARNARLLILDEPTAALTPAeVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334185504 1379 IQRI--IREEfaDCTVITVAHRVPTVID-SDMVMVLSFGDLV 1417
Cdd:cd03216 122 FKVIrrLRAQ--GVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
616-796 |
2.02e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 74.73 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIayvsqtSW---IQSG-----TIRDNI-----L 682
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV------SAlleLGAGfhpelTGRENIylngrL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 683 YGkpMESRRYNAAIKACAldkdmngfghgDLTEIGQRgINL-----SGGQKQRIQLARAVYADADVYLLDDPFSAVDAHt 757
Cdd:COG1134 116 LG--LSRKEIDEKFDEIV-----------EFAELGDF-IDQpvktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAA- 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 758 agvlF-HKCVE--DSLKE--KTVILVTHQ------------VMEEGTITQSGKYEE 796
Cdd:COG1134 181 ----FqKKCLAriRELREsgRTVIFVSHSmgavrrlcdraiWLEKGRLVMDGDPEE 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1199-1427 |
2.15e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.22 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1199 PSNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKST---LISALFRLVEPASGCILIDGIDISKIGLK 1275
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1276 DLRMKLSIIPQEP-TLFRGcirtnldplGVYSDDEIW----KALEKCQLKTTISNLPNKLD--SSVSDEGENWSVGQRQL 1348
Cdd:PRK13640 81 DIREKVGIVFQNPdNQFVG---------ATVGDDVAFglenRAVPRPEMIKIVRDVLADVGmlDYIDSEPANLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1349 FCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLM 1426
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
.
gi 334185504 1427 E 1427
Cdd:PRK13640 232 S 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1200-1427 |
2.22e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.17 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1200 SNGTIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM 1279
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1280 KLSIIPQEP-TLFRGCIRT-----NLDPLGVYSDD---EIWKALEKCqlkttisNLPNKLDSsvsdEGENWSVGQRQLFC 1350
Cdd:PRK13648 84 HIGIVFQNPdNQFVGSIVKydvafGLENHAVPYDEmhrRVSEALKQV-------DMLERADY----EPNALSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1351 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLME 1427
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1204-1425 |
3.44e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.77 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAP-LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLS 1282
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1283 IIPQEP-TLFRGC-----IRTNLDPLGVYSDDEIWKALEKCQLkTTISNLPNKldssvsdEGENWSVGQRQLFCLGRVLL 1356
Cdd:PRK13650 85 MVFQNPdNQFVGAtveddVAFGLENKGIPHEEMKERVNEALEL-VGMQDFKER-------EPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 1357 KRNKILVLDEATASID-SATDAIIQRI--IREEFaDCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKL 1425
Cdd:PRK13650 157 MRPKIIILDEATSMLDpEGRLELIKTIkgIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
283-552 |
3.78e-14 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 74.60 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 283 IFIAVFAFLRTFAVVSLPLMLYVFVDY--ANSDHRDLRNGFFnLACLVMLKLVESLTMRHWYFASRRSGMRIRSALMVAA 360
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVllPDGDPETQALNVY-SLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 361 YKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWWFHSGWSLSLQLLLSTAVLFGVVGAG-AFPGLILLLLCGLLNLP 439
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 440 FAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMSPTIVSS 519
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 334185504 520 VV-FLGCALLKSAPLNASTIFTVLATLRVMSEPV 552
Cdd:pfam00664 241 LAlWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
889-1154 |
4.56e-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: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 889 LLWSSVLGQVGFVVFQAASTYWLAFAIgipkitntmLIGVYSIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFK 968
Cdd:pfam00664 16 PAFPLVLGRILDVLLPDGDPETQALNV---------YSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 969 APMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQDYYLASAR 1048
Cdd:pfam00664 87 QPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1049 ELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERFFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQNVTLFTCALL- 1127
Cdd:pfam00664 167 KLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFg 246
|
250 260
....*....|....*....|....*..
gi 334185504 1128 LILIPKGYIAPGLVGLSLSYALTLTQT 1154
Cdd:pfam00664 247 AYLVISGELSVGDLVAFLSLFAQLFGP 273
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1220-1417 |
4.76e-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: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISAL--FRLVEPASGCILIDGIDISKiglKDLRMKLSIIPQEPTLfrgcirt 1297
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDIL------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1298 nldplgvYSDDEIWKALE---KCQlkttisnlpnkldssvsdegeNWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSA 1374
Cdd:cd03213 94 -------HPTLTVRETLMfaaKLR---------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 334185504 1375 TDAIIQRIIReEFAD--CTVITVAHRVPTVIDS--DMVMVLSFGDLV 1417
Cdd:cd03213 146 SALQVMSLLR-RLADtgRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
616-798 |
5.55e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.11 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-LGEIPkVSGTVKVFG----------------SIAYVSQT-SWIQSGTI 677
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInLLERP-TSGSVLVDGvdltalserelraarrKIGMIFQHfNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 678 RDNILYgkPMESRRYNAAikacaldkdmngfghgdltEIGQR--------GI---------NLSGGQKQRIQLARAVYAD 740
Cdd:COG1135 100 AENVAL--PLEIAGVPKA-------------------EIRKRvaellelvGLsdkadaypsQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 741 ADVYLLDDPFSAVDAH-TAGVLfhkcveDSLKE------KTVILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:COG1135 159 PKVLLCDEATSALDPEtTRSIL------DLLKDinrelgLTIVLITHEmdvvrricdrvaVLENGRIVEQGPVLDVF 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
616-798 |
7.05e-14 |
|
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: 72.58 E-value: 7.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG--------------SIAYVSQTSWIQSG-TIRDN 680
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 ILygKPMESRRYNAAIKACALDKDMNGFGhgdLTEI-GQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAhtag 759
Cdd:cd03218 96 IL--AVLEIRGLSKKEREEKLEELLEEFH---ITHLrKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP---- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 760 vlfhKCVED------SLKEKTV-ILVT-HQVME------------EGTITQSGKYEELL 798
Cdd:cd03218 167 ----IAVQDiqkiikILKDRGIgVLITdHNVREtlsitdrayiiyEGKVLAEGTPEEIA 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
616-820 |
7.40e-14 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 73.74 E-value: 7.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVL------GEIpKVSGTV----------KVFGSIayvSQTSWIQSGTIRD 679
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDI-QIDGVSwnsvplqkwrKAFGVI---PQKVFIFSGTFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 680 NI-LYGKPMESRRYNAAiKACALDKDMNGF-GHGDLTEIgQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHT 757
Cdd:cd03289 96 NLdPYGKWSDEEIWKVA-EEVGLKSVIEQFpGQLDFVLV-DGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 758 AGVLfHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQLVnAHNDAVTVLPL 820
Cdd:cd03289 174 YQVI-RKTLKQAFADCTVILSEHRieamlecqrflVIEENKVRQYDSIQKLLNEKSHFKQAI-SPSDRLKLFPR 245
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
616-780 |
8.23e-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: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLL------HAvlgEIP--KVSGTVKVFG---------------SIAYVSQ---- 668
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLrclnrmND---LIPgaRVEGEILLDGediydpdvdvvelrrRVGMVFQkpnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 669 --TSwiqsgtIRDNILYGkP----MESRRYNAAI-----KACAL-D--KDmngfghgDLteiGQRGINLSGGQKQRIQLA 734
Cdd:COG1117 104 fpKS------IYDNVAYG-LrlhgIKSKSELDEIveeslRKAALwDevKD-------RL---KKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 334185504 735 RAVYADADVYLLDDPFSAVDAHTAGVlfhkcVED---SLKEK-TVILVTH 780
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAK-----IEElilELKKDyTIVIVTH 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
616-756 |
1.06e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 72.84 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQ-SGTIRDNI 681
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQHSSLAfPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 ---LYGKPMESRRYNAAIKAcALDK-DMNGFGHGDLTEigqrginLSGGQKQRIQLARA-------VYADADVYLLDDPF 750
Cdd:COG4559 97 algRAPHGSSAAQDRQIVRE-ALALvGLAHLAGRSYQT-------LSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPT 168
|
....*..
gi 334185504 751 SAVD-AH 756
Cdd:COG4559 169 SALDlAH 175
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
616-781 |
1.18e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVK----------VFGSIAYVSQtswiQSG-----TIRDN 680
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldggdiddpdVAEACHYLGH----RNAmkpalTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 I-----LYGkpmeSRRYNAAIKACAldkdmngFGHGDLTEIgqRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:PRK13539 94 LefwaaFLG----GEELDIAAALEA-------VGLAPLAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*..
gi 334185504 756 HTAGvLFHKCVEDSLKEK-TVILVTHQ 781
Cdd:PRK13539 161 AAVA-LFAELIRAHLAQGgIVIAATHI 186
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1204-1425 |
1.22e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.13 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAP---LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIS----KIGLKD 1276
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1277 LRMKLSIIPQ--EPTLFRGCIRTNL--DPL--GVYSDDEIWKALEKCQLkttiSNLPNK-LDSSVSDegenWSVGQRQLF 1349
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDIcfGPMnfGVSEEDAKQKAREMIEL----VGLPEElLARSPFE----LSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1350 CLGRVLLKRNKILVLDEATASIDSATdaiiQRIIREEFA------DCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEP 1422
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
...
gi 334185504 1423 SKL 1425
Cdd:PRK13634 231 REI 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1206-1412 |
1.30e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1206 LQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIP 1285
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1286 QEPTLFRGCIRTNL-----------DPlgvysdDEIWKALEKCQLKTTIsnlpnkLDSSVSDegenWSVGQRQlfclgRV 1354
Cdd:PRK10247 88 QTPTLFGDTVYDNLifpwqirnqqpDP------AIFLDDLERFALPDTI------LTKNIAE----LSGGEKQ-----RI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1355 LLKRN-----KILVLDEATASIDSAT----DAIIQRIIREEfaDCTVITVAHRVPTVIDSDMVMVLS 1412
Cdd:PRK10247 147 SLIRNlqfmpKVLLLDEITSALDESNkhnvNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITLQ 211
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
622-781 |
1.42e-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: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 622 EIKHGQKVAVCGPVGAGKSSLLHaVLGEIPKVSG---TVKVFGSIAYVSQTSWIQSGTIRDNILYgkPMESrrynaaika 698
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIY--PDSS--------- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 699 caLDKDMNGFGHGDL---------TEIGQRGIN----------LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAG 759
Cdd:TIGR00954 542 --EDMKRRGLSDKDLeqildnvqlTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170 180
....*....|....*....|..
gi 334185504 760 VLFHKCVEDSLkekTVILVTHQ 781
Cdd:TIGR00954 620 YMYRLCREFGI---TLFSVSHR 638
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
616-819 |
2.60e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 71.73 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQ-SGTIRDNI 681
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLSfPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 LYGK-PM-ESRRYNAAIKACALDK-DMNGFGHGDLTEigqrginLSGGQKQRIQLARA---VYADAD---VYLLDDPFSA 752
Cdd:PRK13548 98 AMGRaPHgLSRAEDDALVAAALAQvDLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqLWEPDGpprWLLLDEPTSA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 753 VD-AH---TAGVLFHKCVEDSLkekTVILVTHQ------------VMEEGTITQSGKYEELL---MMGTAFQQ--LVNAH 811
Cdd:PRK13548 171 LDlAHqhhVLRLARQLAHERGL---AVIVVLHDlnlaaryadrivLLHQGRLVADGTPAEVLtpeTLRRVYGAdvLVQPH 247
|
250
....*....|
gi 334185504 812 --NDAVTVLP 819
Cdd:PRK13548 248 peTGAPLVLP 257
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1206-1385 |
2.64e-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: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1206 LQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGL-KDLRMKLSII 1284
Cdd:cd03218 3 AENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1285 PQEPTLFRG-CIRTNLdpLGV-----YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKR 1358
Cdd:cd03218 81 PQEASIFRKlTVEENI--LAVleirgLSKKEREEKLEELLEEFHITHLRKSKASSLSG-------GERRRVEIARALATN 151
|
170 180
....*....|....*....|....*..
gi 334185504 1359 NKILVLDEATASIDSATDAIIQRIIRE 1385
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
610-780 |
2.94e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 610 ETKIptLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQTSWIQSGT 676
Cdd:PRK10247 19 DAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 677 IRDNILYgkPMESRryNAAIKACALDKDMNGFGHGDltEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:PRK10247 97 VYDNLIF--PWQIR--NQQPDPAIFLDDLERFALPD--TILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180
....*....|....*....|....*...
gi 334185504 756 HT---AGVLFHKCVEDslKEKTVILVTH 780
Cdd:PRK10247 171 SNkhnVNEIIHRYVRE--QNIAVLWVTH 196
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
616-796 |
3.26e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTV------------------KVFGSIAYVSQTswiqsgT 676
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfETPD-SGRImldgqdithvpaenrhvnTVFQSYALFPHM------T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 677 IRDNILYGKPMEsRRYNAAIKACALDK-DMNgfghgDLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 754
Cdd:PRK09452 103 VFENVAFGLRMQ-KTPAAEITPRVMEAlRMV-----QLEEFAQRKPhQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 755 AHtagvlFHKCVEDSLKEK------TVILVTHQ------------VMEEGTITQSGK----YEE 796
Cdd:PRK09452 177 YK-----LRKQMQNELKALqrklgiTFVFVTHDqeealtmsdrivVMRDGRIEQDGTpreiYEE 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
618-797 |
3.71e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.83 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 618 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPkVSGTV------------------KVFGSIAYVSQTSwiqsgtIR 678
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKP-TEGQIfidgedvthrsiqqrdicMVFQSYALFPHMS------LG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 679 DNILYGKPMESRRyNAAIK-----ACALdKDMNGFGHGDLTEIgqrginlSGGQKQRIQLARAVYADADVYLLDDPFSAV 753
Cdd:PRK11432 97 ENVGYGLKMLGVP-KEERKqrvkeALEL-VDLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 754 DAHtagvlfhkcVEDSLKEK----------TVILVTHQ------------VMEEGTITQSGKYEEL 797
Cdd:PRK11432 168 DAN---------LRRSMREKirelqqqfniTSLYVTHDqseafavsdtviVMNKGKIMQIGSPQEL 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1221-1433 |
4.65e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.57 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRL--VEP---ASGCILIDGIDI--SKIGLKDLRMKLSIIPQEPTLFRG 1293
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1294 CIRTN----LDPLGVYSDDEIWKALEKCQLKTTISN-LPNKL-DSSVSDEGenwsvGQRQLFCLGRVLLKRNKILVLDEA 1367
Cdd:PRK14239 101 SIYENvvygLRLKGIKDKQVLDEAVEKSLKGASIWDeVKDRLhDSALGLSG-----GQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1368 TASIDSATDAIIQRIIREEFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLM------ETDSYFS 1433
Cdd:PRK14239 176 TSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFmnpkhkETEDYIS 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1221-1418 |
5.06e-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: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVePASGCILIDGIDISKIG---LKDLRMKLSIIPQEPtlFrgcirT 1297
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-----G 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1298 NLDP-----------LGVYS--------DDEIWKALEKCQLK-TTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLK 1357
Cdd:COG4172 374 SLSPrmtvgqiiaegLRVHGpglsaaerRARVAEALEEVGLDpAARHRYPHEF-----------SGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1358 RNKILVLDEATasidSATDAIIQ-------RIIREEFA--------DCTVI-TVAHRvptvidsdmVMVLSFGDLVE 1418
Cdd:COG4172 443 EPKLLVLDEPT----SALDVSVQaqildllRDLQREHGlaylfishDLAVVrALAHR---------VMVMKDGKVVE 506
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
616-798 |
5.73e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.55 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-LGEIPKvSGTVKVF-----GSIAYVSQTSWI-----QSG--------- 675
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQPE-AGTIRVGditidTARSLSQQKGLIrqlrqHVGfvfqnfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 ---TIRDNILYGKPMESRRYNAAikACALDKDMngfghgdLTEIGQRGIN------LSGGQKQRIQLARAVYADADVYLL 746
Cdd:PRK11264 98 phrTVLENIIEGPVIVKGEPKEE--ATARAREL-------LAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 747 DDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQV------------MEEGTITQSGKYEELL 798
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMsfardvadraifMDQGRIVEQGPAKALF 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1204-1418 |
5.95e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.76 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM-- 1279
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1280 -KLSIIPQEPTLFRGciRTnldplgVYsdDEIWKALE-----KCQLKTTISNLpnkLD-SSVSDEGE----NWSVGQRQL 1348
Cdd:PRK11153 82 rQIGMIFQHFNLLSS--RT------VF--DNVALPLElagtpKAEIKARVTEL---LElVGLSDKADrypaQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1349 FCLGRVLLKRNKILVLDEATASIDSA-TDAIIQ--RIIREEFaDCTVITVAHRVpTVIDS--DMVMVLSFGDLVE 1418
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPAtTRSILEllKDINREL-GLTIVLITHEM-DVVKRicDRVAVIDAGRLVE 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1204-1384 |
5.97e-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: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKigLKDLRMKLSI 1283
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLF-----RGCIRTNLDPLGVySDDEIWKALEkcqlkttISNLPNKLDSSVSdegeNWSVGQRQLFCLGRVLLKR 1358
Cdd:cd03268 77 LIEAPGFYpnltaRENLRLLARLLGI-RKKRIDEVLD-------VVGLKDSAKKKVK----GFSLGMKQRLGIALALLGN 144
|
170 180
....*....|....*....|....*.
gi 334185504 1359 NKILVLDEATASIDSATDAIIQRIIR 1384
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIL 170
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
630-798 |
6.19e-13 |
|
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: 72.06 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 630 AVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------------SIAYVSQtswiQSG-----TIRDNILYGkpm 687
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQ----EARlfphlSVRGNLLYG--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 688 eSRRYNAAIKACALDK--DMNGFGHgdLteIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTagvlfhKC 765
Cdd:COG4148 102 -RKRAPRAERRISFDEvvELLGIGH--L--LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR------KA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 334185504 766 vE-----DSLKEKT---VILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:COG4148 171 -EilpylERLRDELdipILYVSHSldevarladhvvLLEQGRVVASGPLAEVL 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1204-1397 |
6.45e-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: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPL---VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKigLKDLR-- 1278
Cdd:COG1101 2 LELKNLSKTFNPGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK--LPEYKra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1279 MKLSIIPQEP---TLFRGCIRTNLD-----------PLGVYSDDeiwKALEKCQLKTTISNLPNKLDSSVsdegENWSVG 1344
Cdd:COG1101 80 KYIGRVFQDPmmgTAPSMTIEENLAlayrrgkrrglRRGLTKKR---RELFRELLATLGLGLENRLDTKV----GLLSGG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1345 QRQLFCLGRVLLKRNKILVLDEATASIDSATDAII----QRIIREEfaDCTVITVAH 1397
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEEN--NLTTLMVTH 207
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
621-784 |
6.56e-13 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 69.44 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 621 LEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKvSGTVKVFG-----------SIAYVSQTSWIQSG-TIRDNILYGKpM 687
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQ-SGRVLINGvdvtaappadrPVSMLFQENNLFAHlTVEQNVGLGL-S 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 688 ESRRYNA----AIKACALDKDMNGFghgDLTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVD-AHTAGVLf 762
Cdd:cd03298 97 PGLKLTAedrqAIEVALARVGLAGL---EKRLPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDpALRAEML- 168
|
170 180
....*....|....*....|....
gi 334185504 763 hKCVEDSLKEK--TVILVTHQVME 784
Cdd:cd03298 169 -DLVLDLHAETkmTVLMVTHQPED 191
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1220-1439 |
6.87e-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: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISkiGLKDLRMKLSIIPQEPTLFrgcirtnl 1299
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALF-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1300 dP-LGVYSDDE---IWKALEKCQLKTTISNLPNKL--DSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDS 1373
Cdd:cd03299 84 -PhMTVYKNIAyglKKRKVDKKEIERKVLEIAEMLgiDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1374 ATDAIIQ---RIIREEFaDCTVITVAHRVPTV-IDSDMVMVLSFGDLVEYNEPSKLMETDSyfSKLVAEY 1439
Cdd:cd03299 163 RTKEKLReelKKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPK--NEFVAEF 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1204-1404 |
7.67e-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: 7.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM-- 1279
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1280 -KLSIIPQEPTLFRGciRTNLD----PLgvysddEIWKaLEKCQLKTTISNLpnkLDsSV--SDEGENW----SVGQRQl 1348
Cdd:COG1135 82 rKIGMIFQHFNLLSS--RTVAEnvalPL------EIAG-VPKAEIRKRVAEL---LE-LVglSDKADAYpsqlSGGQKQ- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 1349 fclgRV-----LLKRNKILVLDEATASIDSA-TDAIIQRI--IREEFaDCTV--IT--------VAHRVpTVID 1404
Cdd:COG1135 148 ----RVgiaraLANNPKVLLCDEATSALDPEtTRSILDLLkdINREL-GLTIvlIThemdvvrrICDRV-AVLE 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1220-1411 |
7.95e-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: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD-LRMKLSIIPQEPTLF------- 1291
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVpnlsvae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1292 ----------RGCIRtnldplgvysddeiWKALEK------CQLKTTISnlpnkLDSSVSDegenWSVGQRQLFCLGRVL 1355
Cdd:COG1129 99 niflgreprrGGLID--------------WRAMRRrarellARLGLDID-----PDTPVGD----LSVAQQQLVEIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1356 LKRNKILVLDEATASIDSATDAIIQRIIReEFAD--CTVITVAHRVPTVID-SDMVMVL 1411
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIR-RLKAqgVAIIYISHRLDEVFEiADRVTVL 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
614-781 |
8.46e-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: 8.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQsgtirdNILYG------KP- 686
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE------NILYLghlpglKPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 687 ---MESRRYNAAIKACAlDKDMngfgHGDLTEIGQRGIN------LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAht 757
Cdd:TIGR01189 88 lsaLENLHFWAAIHGGA-QRTI----EDALAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-- 160
|
170 180
....*....|....*....|....*.
gi 334185504 758 AGV-LFHKCVEDSL-KEKTVILVTHQ 781
Cdd:TIGR01189 161 AGVaLLAGLLRAHLaRGGIVLLTTHQ 186
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1229-1397 |
1.05e-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: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1229 REGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDL----RMKLSIIPQEPTLFRGciRTNLD---- 1300
Cdd:cd03294 48 REGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPH--RTVLEnvaf 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1301 PL---GVYSDDEIWKALEKCQ---LKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATasidSA 1374
Cdd:cd03294 126 GLevqGVPRAEREERAAEALElvgLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF----SA 190
|
170 180
....*....|....*....|....*....
gi 334185504 1375 TDAIIQRIIREEFADC------TVITVAH 1397
Cdd:cd03294 191 LDPLIRREMQDELLRLqaelqkTIVFITH 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1211-1425 |
1.39e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 69.72 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1211 IRYR-PNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDISKIGLKDLRMKLSIIPQE 1287
Cdd:PRK13639 7 LKYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1288 P--TLFRGCIRTNL--DPLGV-YSDDEIWK----ALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKR 1358
Cdd:PRK13639 87 PddQLFAPTVEEDVafGPLNLgLSKEEVEKrvkeALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1359 NKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHRVPTV-IDSDMVMVLSFGDLVEYNEPSKL 1425
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 ... |
1204-1427 |
1.52e-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: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVLK---GISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASG--CILI--DGIDISKIGLkD 1276
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVgdEWVDMTKPGP-D 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1277 LRMK----LSIIPQEPTLF--RGCIRTNLDPLGVYSDDEIWKALEKCQLKTT------ISNLPNKLDSSVsdegenwSVG 1344
Cdd:TIGR03269 359 GRGRakryIGILHQEYDLYphRTVLDNLTEAIGLELPDELARMKAVITLKMVgfdeekAEEILDKYPDEL-------SEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1345 QRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRII---REEFADcTVITVAHRVPTVID-SDMVMVLSFGDLVEYN 1420
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDvCDRAALMRDGKIVKIG 510
|
....*..
gi 334185504 1421 EPSKLME 1427
Cdd:TIGR03269 511 DPEEIVE 517
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
616-792 |
1.52e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-LGEIPKvSGTVKVFGSIAYVSQTSWIQSG-TIRDNIlygkPMESRRYN 693
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNHFDFSKTPSDKAIrELRRNV----GMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 694 -------------AAIKACALDKD------MNGFGHGDLTEIGQR-GINLSGGQKQRIQLARAVYADADVYLLDDPFSAV 753
Cdd:PRK11124 93 lwphltvqqnlieAPCRVLGLSKDqalaraEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 754 DAH-TAGVLfhkcveDSLKEK-----TVILVTHQV------------MEEGTITQSG 792
Cdd:PRK11124 173 DPEiTAQIV------SIIRELaetgiTQVIVTHEVevarktasrvvyMENGHIVEQG 223
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1220-1436 |
1.70e-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: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGidiskiglkdlrmKLSIIPQEPTLFRGCIRTNL 1299
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1300 dPLGVYSDDEIWKALEK-CQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDA- 1377
Cdd:cd03291 119 -IFGVSYDEYRYKSVVKaCQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKe 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1378 IIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETDSYFSKLV 1436
Cdd:cd03291 198 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
589-811 |
1.98e-12 |
|
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: 69.17 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 589 SGLDASGTAVDIQVGNFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------- 661
Cdd:cd03288 11 SGLVGLGGEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 662 ------SIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLAR 735
Cdd:cd03288 90 lhtlrsRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 736 AVYADADVYLLDDPFSAVDAHTAGVLfHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEELLMM-GTA 803
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENIL-QKVVMTAFADRTVVTIAHRvstildadlvlVLSRGILVECDTPENLLAQeDGV 248
|
....*...
gi 334185504 804 FQQLVNAH 811
Cdd:cd03288 249 FASLVRTD 256
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
616-798 |
2.11e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.52 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQTSWIQSG-TIRDN 680
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlTVEDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 ILygKPMESRRYNAAIKACALDKDMNGFGhgdLTEI-GQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD--Aht 757
Cdd:COG1137 99 IL--AVLELRKLSKKEREERLEELLEEFG---ITHLrKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiA-- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 758 agvlfhkcVED------SLKEKTV-ILVT-HQVME------------EGTITQSGKYEELL 798
Cdd:COG1137 172 --------VADiqkiirHLKERGIgVLITdHNVREtlgicdrayiisEGKVLAEGTPEEIL 224
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
933-1179 |
2.45e-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: 69.83 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 933 STLSAGFVyaRAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELT 1012
Cdd:cd18600 82 SLLAMGFF--RGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1013 AALLIMTYVTWQVIIIALLALAATKVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERF---FKNYL 1089
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFetlFHKAL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1090 NLVDADavlFFLSNAAMEWVILRIETLqNVTLFTCALLLILIPKGYiAPGLVGLSLSYALTLTQTQVFLTRWYCTLSNSI 1169
Cdd:cd18600 240 NLHTAN---WFLYLSTLRWFQMRIEMI-FVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLM 314
|
250
....*....|
gi 334185504 1170 ISVERIKQYM 1179
Cdd:cd18600 315 RSVSRIFKFI 324
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
616-781 |
2.54e-12 |
|
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: 67.19 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG--EIPKVSGTVKVFG----------SIAYVSQtswiqsgtirDNILY 683
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGrpldkrsfrkIIGYVPQ----------DDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 684 GK--PMESRRYNAAIKacaldkdmngfghgdlteigqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAgvl 761
Cdd:cd03213 95 PTltVRETLMFAAKLR------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA--- 147
|
170 180
....*....|....*....|....*
gi 334185504 762 FHkcVEDSLKE-----KTVILVTHQ 781
Cdd:cd03213 148 LQ--VMSLLRRladtgRTIICSIHQ 170
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
616-782 |
2.83e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.50 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIP--KVSG--------TVKVFGSIAYVSQTSWIQSG---------- 675
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGshiellgrTVQREGRLARDIRKSRANTGyifqqfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 --TIRDNILYGKPMES-------RRYNAAIKACALDK----DMNGFGHgdlteigQRGINLSGGQKQRIQLARAVYADAD 742
Cdd:PRK09984 100 rlSVLENVLIGALGSTpfwrtcfSWFTREQKQRALQAltrvGMVHFAH-------QRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 334185504 743 VYLLDDPFSAVDAHTAgvlfhKCVEDSLKE------KTVILVTHQV 782
Cdd:PRK09984 173 VILADEPIASLDPESA-----RIVMDTLRDinqndgITVVVTLHQV 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
616-797 |
3.24e-12 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 67.65 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSI-----AYVSQTSWI-QSG------TIRDNILY 683
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpPHKRPVNTVfQNYalfphlTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 684 GKPMEsRRYNAAIK---ACALDK-DMNGFGHGDLTEigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAhtag 759
Cdd:cd03300 96 GLRLK-KLPKAEIKervAEALDLvQLEGYANRKPSQ-------LSGGQQQRVAIARALVNEPKVLLLDEPLGALDL---- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 760 vlfhKCVEDSLKE---------KTVILVTHQ------------VMEEGTITQSGKYEEL 797
Cdd:cd03300 164 ----KLRKDMQLElkrlqkelgITFVFVTHDqeealtmsdriaVMNKGKIQQIGTPEEI 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
612-790 |
3.34e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 68.26 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV--LGE-IPKVS--GTVKVFGSIAYVSQTSWIQ------------- 673
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDlNPEVTitGSIVYNGHNIYSPRTDTVDlrkeigmvfqqpn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 674 --SGTIRDNILYGKPMESRRYNAAIKAcALDKDMNGFGHGDltEIGQR----GINLSGGQKQRIQLARAVYADADVYLLD 747
Cdd:PRK14239 97 pfPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWD--EVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 334185504 748 DPFSAVDAHTAGVlfhkcVEDSL----KEKTVILVTHQVMEEGTITQ 790
Cdd:PRK14239 174 EPTSALDPISAGK-----IEETLlglkDDYTMLLVTRSMQQASRISD 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1219-1426 |
3.40e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.06 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1219 LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG---LKDLRMK--------LSIIPQE 1287
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKkiamvfqsFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1288 PTLFRGCIRTNLdpLGVYSDDEIWKALEKCQ---LKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVL 1364
Cdd:PRK10070 122 TVLDNTAFGMEL--AGINAEERREKALDALRqvgLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1365 DEATasidSATDAIIQRIIREEFADC------TVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLM 1426
Cdd:PRK10070 189 DEAF----SALDPLIRTEMQDELVKLqakhqrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1220-1446 |
3.62e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGC-----ILIDGIDISKI-GLKDLRMKLSIIPQEPTLFRG 1293
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1294 CIRTNLdPLGVYSDDEIWKALEK--CQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASI 1371
Cdd:PRK14271 116 SIMDNV-LAGVRAHKLVPRKEFRgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1372 DSATDAIIQRIIREEFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLM------ETDSYFSKLVAEYWASCR 1444
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFsspkhaETARYVAGLSGDVKDAKR 274
|
..
gi 334185504 1445 GN 1446
Cdd:PRK14271 275 GN 276
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1216-1417 |
3.69e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 68.58 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1216 NAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG-LKDLRMKLSIIPQEP------ 1288
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqiva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1289 TLFRGCIRTNLDPLGVYSdDEIWKALEKCQLKTTISNL----PNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVL 1364
Cdd:PRK13633 101 TIVEEDVAFGPENLGIPP-EEIRERVDESLKKVGMYEYrrhaPHLL-----------SGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 1365 DEATASID-SATDAIIQRI--IREEFAdCTVITVAHRVPTVIDSDMVMVLSFGDLV 1417
Cdd:PRK13633 169 DEPTAMLDpSGRREVVNTIkeLNKKYG-ITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
616-782 |
3.73e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.61 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQ---------------SGTIRDN 680
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRskvglvfqdpddqvfSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 ILYG------KPME-SRRYNAAIKACaldkDMNGFGHgdlteigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAV 753
Cdd:PRK13647 101 VAFGpvnmglDKDEvERRVEEALKAV----RMWDFRD-------KPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180
....*....|....*....|....*....
gi 334185504 754 DAHTAGVLFHKCVEDSLKEKTVILVTHQV 782
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDV 198
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1204-1398 |
3.79e-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: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIrYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGidiskiglkdlRMKLSI 1283
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLFRGCIRTNLdplgVYSddeiWkalekcqlkttisnlpnkldssvsdeGENWSVGQRQLFCLGRVLLKRNKILV 1363
Cdd:cd03223 69 LPQRPYLPLGTLREQL----IYP----W--------------------------DDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 334185504 1364 LDEATASIDSATDAIIQRIIREEFAdcTVITVAHR 1398
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
609-807 |
5.30e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.12 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 609 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGsIAYVSQTSW---------IQS----- 674
Cdd:PRK13635 16 PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrrqvgmvFQNpdnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 675 --GTIRDNILY-----GKPMES--RRYNAAIKACaldkDMNGFGHgdlteigQRGINLSGGQKQRIQLARAVYADADVYL 745
Cdd:PRK13635 95 vgATVQDDVAFgleniGVPREEmvERVDQALRQV----GMEDFLN-------REPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 746 LDDPFSAVD-AHTAGVLfhKCVEDsLKEK---TVILVTHQ-----------VMEEGTITQSGKYEELLMMGTAFQQL 807
Cdd:PRK13635 164 LDEATSMLDpRGRREVL--ETVRQ-LKEQkgiTVLSITHDldeaaqadrviVMNKGEILEEGTPEEIFKSGHMLQEI 237
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
614-785 |
5.41e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.09 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS------------IAYVSQTSWI-QSGTIRDN 680
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIGVVPQFDNLdLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 IL-YGK--PMESRRYNAAIKA----CALDKDMNGfghgdlteigqRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAV 753
Cdd:PRK13536 135 LLvFGRyfGMSTREIEAVIPSllefARLESKADA-----------RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190
....*....|....*....|....*....|..
gi 334185504 754 DAHTAGVLFHKCVEDSLKEKTVILVTHqVMEE 785
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGKTILLTTH-FMEE 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
616-820 |
6.16e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.35 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSG-TIRDNI 681
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 LYGK-PMESR--RYNAAIKAcALDKDMNGFGHGDLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTA 758
Cdd:PRK11231 98 AYGRsPWLSLwgRLSAEDNA-RVNQAMEQTRINHLAD--RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 759 GVLFHKCVEDSLKEKTVILVTHQ------------VMEEGTITQSGKYEELL---MMGTAFQQLVNAHNDAVTVLPL 820
Cdd:PRK11231 175 VELMRLMRELNTQGKTVVTVLHDlnqasrycdhlvVLANGHVMAQGTPEEVMtpgLLRTVFDVEAEIHPEPVSGTPM 251
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
616-797 |
6.21e-12 |
|
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: 66.62 E-value: 6.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------------SIAYVSQTSWIQSG-TIRDNI- 681
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 ----LYGKPMESRRYNAaikacalDKDMNGFGhgdLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 756
Cdd:cd03265 96 iharLYGVPGAERRERI-------DELLDFVG---LLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 757 T-AGVLFHkcVEDSLKEK--TVILVTH------------QVMEEGTITQSGKYEEL 797
Cdd:cd03265 166 TrAHVWEY--IEKLKEEFgmTILLTTHymeeaeqlcdrvAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1215-1422 |
6.91e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.34 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1215 PNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIS---------------KI-GLKDLR 1278
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGdkknnhelitnpyskKIkNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1279 MKLSIIPQEP--TLFRGCIRTNL--DP--LGVYSDDEIWKA---LEKCQLKTTIsnlpnkLDSSVSDegenWSVGQRQLF 1349
Cdd:PRK13631 116 RRVSMVFQFPeyQLFKDTIEKDImfGPvaLGVKKSEAKKLAkfyLNKMGLDDSY------LERSPFG----LSGGQKRRV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1350 CLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADC-TVITVAHRVPTVID-SDMVMVLSFGDLVEYNEP 1422
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1221-1436 |
7.17e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 7.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRlVEPA---SGCILIDGIDISKIGLKDLRMK-LSIIPQEPTL------ 1290
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNIRDTERAgIAIIHQELALvkelsv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1291 ----FRGCirtNLDPLGVYSDDEIWKALEKC--QLKTTIS-NLPnkldssVSDEGenwsVGQRQLFCLGRVLLKRNKILV 1363
Cdd:PRK13549 100 leniFLGN---EITPGGIMDYDAMYLRAQKLlaQLKLDINpATP------VGNLG----LGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1364 LDEATASIDSATDAIIQRIIREEFA-DCTVITVAHRVPTVID-SDMVMVLSFGDLVEyNEPSKLMETDSYFSKLV 1436
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAhGIACIYISHKLNEVKAiSDTICVIRDGRHIG-TRPAAGMTEDDIITMMV 240
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
612-798 |
7.25e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.04 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV--LGEIPK----VSGtVKVFGSIAYVSQTSwIQSG---------- 675
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSgdliVDG-LKVNDPKVDERLIR-QEAGmvfqqfylfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 --TIRDNILYGkPMESRRynaAIKACALDKDMNGFGHGDLTE-IGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSA 752
Cdd:PRK09493 91 hlTALENVMFG-PLRVRG---ASKEEAEKQARELLAKVGLAErAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 753 VDAHtagvLFHKC--VEDSLKEK--TVILVTHQV------------MEEGTITQSGKYEELL 798
Cdd:PRK09493 167 LDPE----LRHEVlkVMQDLAEEgmTMVIVTHEIgfaekvasrlifIDKGRIAEDGDPQVLI 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
617-784 |
8.15e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.98 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 617 RNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SI-----AYVSQTSWI--QSGtIRDNIlygKPME 688
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGePIrrqrdEYHQDLLYLghQPG-IKTEL---TALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 689 SRRYNAAIKACALDKDMngfgHGDLTEIGQRGI------NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDahTAGVlf 762
Cdd:PRK13538 94 NLRFYQRLHGPGDDEAL----WEALAQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID--KQGV-- 165
|
170 180
....*....|....*....|....*..
gi 334185504 763 hKCVEDSLKEKT-----VILVTHQVME 784
Cdd:PRK13538 166 -ARLEALLAQHAeqggmVILTTHQDLP 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
616-792 |
9.30e-12 |
|
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: 66.06 E-value: 9.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQkVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS------------IAYVSQT-SWIQSGTIRDNIL 682
Cdd:cd03264 16 LDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQEfGVYPNFTVREFLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 683 YG---KPMESRRYNAAIkaCALDKDMNGFGHGDlTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPfsavdahTAG 759
Cdd:cd03264 95 YIawlKGIPSKEVKARV--DEVLELVNLGDRAK-KKIGS----LSGGMRRRVGIAQALVGDPSILIVDEP-------TAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 334185504 760 ------VLFHKCVEDSLKEKTVILVTHQV------------MEEGTITQSG 792
Cdd:cd03264 161 ldpeerIRFRNLLSELGEDRIVILSTHIVedveslcnqvavLNKGKLVFEG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1204-1402 |
9.44e-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: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDISKiglkdlRMKL 1281
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAA------RNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1282 SIIPQEPTLFRGciRTNLDPLgVYSDDeiWKALEKCQLKTTISNLPNKLDSSVSDEG--ENWSVGQRQLFCLGRVLLKRN 1359
Cdd:cd03269 73 GYLPEERGLYPK--MKVIDQL-VYLAQ--LKGLKKEEARRRIDEWLERLELSEYANKrvEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 334185504 1360 KILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHRVPTV 1402
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELV 191
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
609-798 |
1.06e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.94 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 609 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQS-------------- 674
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKkigiifqnpdnqfi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 675 -GTIRDNILYGkpMESRRYN-----AAIKACALDKDMNGFghgdlteIGQRGINLSGGQKQRIQLARAVYADADVYLLDD 748
Cdd:PRK13632 98 gATVEDDIAFG--LENKKVPpkkmkDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 749 PFSAVDA---HTAGVLFHKCVEDslKEKTVILVTHQ-----------VMEEGTITQSGKYEELL 798
Cdd:PRK13632 169 STSMLDPkgkREIKKIMVDLRKT--RKKTLISITHDmdeailadkviVFSEGKLIAQGKPKEIL 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1220-1397 |
1.07e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 65.33 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGidisKIGLKDLRMKLSIIPQEPTLFRGCI---- 1295
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPLTVRDLVamgr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1296 ---RTNLDPLGVYSDDEIWKALEKCQLkTTISNLPnkLDSsvsdegenWSVGQRQLFCLGRVLLKRNKILVLDEATASID 1372
Cdd:NF040873 83 warRGLWRRLTRDDRAAVDDALERVGL-ADLAGRQ--LGE--------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180
....*....|....*....|....*.
gi 334185504 1373 SATDAIIQRIIREEFAD-CTVITVAH 1397
Cdd:NF040873 152 AESRERIIALLAEEHARgATVVVVTH 177
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1220-1429 |
1.10e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGCIRTNL 1299
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1300 DPLGVY-----------SDDE-IWKALEKCQLKTtisnLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLDEA 1367
Cdd:PRK10575 106 VAIGRYpwhgalgrfgaADREkVEEAISLVGLKP----LAHRLVDSLSG-------GERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1368 TASIDSATD----AIIQRIIREEfaDCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMETD 1429
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 ... |
1221-1414 |
1.23e-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: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDL----RMKLSIIPQEPTLFRGCIR 1296
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1297 TNLdPLGVYSDDEIWKAL-EKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASID-SA 1374
Cdd:cd03290 97 ENI-TFGSPFNKQRYKAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334185504 1375 TDAIIQRIIREEFAD--CTVITVAHRVPTVIDSDMVMVLSFG 1414
Cdd:cd03290 176 SDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
951-1179 |
1.26e-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: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 951 GLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQVIIIAL 1030
Cdd:cd18559 66 GIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1031 LALAATKVvQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAERfFKNYLNLVDADAVLFFLSNAAMEWVI 1110
Cdd:cd18559 146 LGLLYVPV-NRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEA-FIRQVDAKRDNELAYLPSIVYLRALA 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1111 LRIETLQNVtLFTCALLLILIPKGYIApGLVGLSLSYALTLTQTQVFLTRWYCTLSNSIISVERIKQYM 1179
Cdd:cd18559 224 VRLWCVGPC-IVLFASFFAYVSRHSLA-GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
607-780 |
1.37e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 66.20 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 607 WEPETK-IPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------SIAYVSQTSWI--QSGTI 677
Cdd:cd03267 27 FKRKYReVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkrRKKFLRRIGVVfgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 678 RDNIlygKPMESRRYNAAI---KACALDKDMNGFGhgDLTEIG----QRGINLSGGQKQRIQLARAVYADADVYLLDDPF 750
Cdd:cd03267 107 WWDL---PVIDSFYLLAAIydlPPARFKKRLDELS--ELLDLEelldTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190
....*....|....*....|....*....|..
gi 334185504 751 SAVDAHTAGVLfHKCVEDSLKEK--TVILVTH 780
Cdd:cd03267 182 IGLDVVAQENI-RNFLKEYNRERgtTVLLTSH 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
600-782 |
1.43e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.60 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 600 IQVGNFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAvLGEIPKVSGTVKVFGSIAYVSQTSW-------- 671
Cdd:PRK14258 8 IKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYerrvnlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 672 -------------IQSGTIRDNILYGKPMESRR--------YNAAIKACALDKDMNgfghgdlTEIGQRGINLSGGQKQR 730
Cdd:PRK14258 86 lrrqvsmvhpkpnLFPMSVYDNVAYGVKIVGWRpkleiddiVESALKDADLWDEIK-------HKIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 334185504 731 IQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLK-EKTVILVTHQV 782
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRsELTMVIVSHNL 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
614-798 |
1.50e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.26 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-------------SIAYVSQTSWIQSG-TIRD 679
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQENHINSRlTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 680 NILYGKPMESR-RYNAAIKAcALDKDMNGFghgDLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVD-AH 756
Cdd:COG4604 95 LVAFGRFPYSKgRLTAEDRE-IIDEAIAYL---DLEDLADRYLDeLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKH 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 757 TAGV--LFHKCVEDslKEKTVILVTHQV------------MEEGTITQSGKYEELL 798
Cdd:COG4604 171 SVQMmkLLRRLADE--LGKTVVIVLHDInfascyadhivaMKDGRVVAQGTPEEII 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
616-779 |
1.56e-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: 64.76 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVkvfgsiayvsqtswiqsgtirdnILYGKPMESRRYNAA 695
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEI-----------------------TLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 696 IKAcaldkdmnGFGHgdLTE-------IGQRGIN--------LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGV 760
Cdd:cd03215 73 IRA--------GIAY--VPEdrkreglVLDLSVAenialsslLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170
....*....|....*....
gi 334185504 761 LFHKCVEDSLKEKTVILVT 779
Cdd:cd03215 143 IYRLIRELADAGKAVLLIS 161
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
616-789 |
1.61e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.34 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-----LGEIPKVSGTVKVFGSIAYVSQTSWIQ---------------SG 675
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPDVDPVEvrrrigmvfqkpnpfPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDNILYGKpmesrrynaaikacaldkDMNGFgHGDLTEIGQR------------------GINLSGGQKQRIQLARAV 737
Cdd:PRK14243 106 SIYDNIAYGA------------------RINGY-KGDMDELVERslrqaalwdevkdklkqsGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 738 YADADVYLLDDPFSAVDA-HTAGV--LFHKcvedsLKEK-TVILVTHQVMEEGTIT 789
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPiSTLRIeeLMHE-----LKEQyTIIIVTHNMQQAARVS 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
613-780 |
1.64e-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: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 613 IPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG----------------SIAYVSQTS-WIQSG 675
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDFrLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDN------ILYGKPME-SRRYNAAIKACALDKDMNGFGHGdlteigqrginLSGGQKQRIQLARAVYADADVYLLDD 748
Cdd:cd03292 94 NVYENvafaleVTGVPPREiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 334185504 749 PFSAVDA-HTAGV--LFHKCvedSLKEKTVILVTH 780
Cdd:cd03292 163 PTGNLDPdTTWEImnLLKKI---NKAGTTVVVATH 194
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
616-780 |
1.92e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.02 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-----LGEIPKVSGTVKVFGSIAYVSQTSWIQSG--------------- 675
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEVRrevgmvfqypnpfph 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 -TIRDNILYG-------KPMES--RRYNAAIKACALDKDMNgfghgdlTEIGQRGINLSGGQKQRIQLARAVYADADVYL 745
Cdd:PRK14267 100 lTIYDNVAIGvklnglvKSKKEldERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 334185504 746 LDDPFSAVDAHTAgvlfhKCVEDSL----KEKTVILVTH 780
Cdd:PRK14267 173 MDEPTANIDPVGT-----AKIEELLfelkKEYTIVLVTH 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
620-798 |
2.20e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.37 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 620 HLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-----------IAYVSQTSWIQSG-TIRDNILYGkpm 687
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQENNLFSHlTVAQNIGLG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 688 esrrYNAAIKacaldkdMNGFGHGDLTEIGQR-GIN---------LSGGQKQRIQLARAVYADADVYLLDDPFSAVD-AH 756
Cdd:PRK10771 96 ----LNPGLK-------LNAAQREKLHAIARQmGIEdllarlpgqLSGGQRQRVALARCLVREQPILLLDEPFSALDpAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 757 TAGVLfhKCVEDSLKEK--TVILVTHQ------------VMEEGTITQSGKYEELL 798
Cdd:PRK10771 165 RQEML--TLVSQVCQERqlTLLMVSHSledaariaprslVVADGRIAWDGPTDELL 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1217-1416 |
2.62e-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: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1217 APLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI----------SKIGL--KDlRMKLSII 1284
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrrsprdairAGIAYvpED-RKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1285 PQEPtlfrgcIRTNLdplgvysddeiwkalekcqlkttisNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVL 1364
Cdd:cd03215 91 LDLS------VAENI-------------------------ALSSLL-----------SGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1365 DEATASIDSATDAIIQRIIReEFAD--CTVITVAHRVPTVID-SDMVMVLSFGDL 1416
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIR-ELADagKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
593-798 |
2.72e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 593 ASGTaVDIQVGNFGWEPETkiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG----------- 661
Cdd:PRK10790 337 QSGR-IDIDNVSFAYRDDN--LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvl 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 662 --SIAYVSQTSWIQSGTIRDNILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYA 739
Cdd:PRK10790 414 rqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 740 DADVYLLDDPFSAVDAHTagvlfHKCVEDSL----KEKTVILVTHQ-----------VMEEGTITQSGKYEELL 798
Cdd:PRK10790 494 TPQILILDEATANIDSGT-----EQAIQQALaavrEHTTLVVIAHRlstiveadtilVLHRGQAVEQGTHQQLL 562
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1204-1427 |
2.73e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVLKG---ISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG----LKD 1276
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRAlfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1277 LRMKLSIIPQEP--TLFRGCIRTNL----DPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFC 1350
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafgpQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSG-------GQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1351 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE-EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLME 1427
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1204-1397 |
3.39e-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: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKiGLKDLRMKLSI 1283
Cdd:cd03265 1 IEVENLVKKYGDF--EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEPTLfrgcirtnldplgvysdDEIWKALEKCQLKTTISNLPNKLDSSVSDE-------GE-------NWSVGQRQLF 1349
Cdd:cd03265 78 VFQDLSV-----------------DDELTGWENLYIHARLYGVPGAERRERIDElldfvglLEaadrlvkTYSGGMRRRL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 334185504 1350 CLGRVLLKRNKILVLDEATASIDSATDAIIQRIIR---EEFaDCTVITVAH 1397
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEklkEEF-GMTILLTTH 190
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
609-807 |
3.60e-11 |
|
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: 65.53 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 609 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSL---LHAVLgeIPKvSGTVKVFGSIAYVSQTSW-------------- 671
Cdd:TIGR04520 11 PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLL--LPT-SGKVTVDGLDTLDEENLWeirkkvgmvfqnpd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 672 --IQSGTIRDNILYGkpMES---------RRYNAAIKACaldkDMNGFGHgdlteigQRGINLSGGQKQRIQLARAVYAD 740
Cdd:TIGR04520 88 nqFVGATVEDDVAFG--LENlgvpreemrKRVDEALKLV----GMEDFRD-------REPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 741 ADVYLLDDPFSAVDAhtagvlfhKCVED------SLKE---KTVILVTHQ-----------VMEEGTITQSGKYEELLMM 800
Cdd:TIGR04520 155 PDIIILDEATSMLDP--------KGRKEvletirKLNKeegITVISITHDmeeavladrviVMNKGKIVAEGTPREIFSQ 226
|
....*..
gi 334185504 801 GTAFQQL 807
Cdd:TIGR04520 227 VELLKEI 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1220-1425 |
4.28e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.06 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEpASGCILIDG--------IDISKIGLKDLRMKLSIIPQEPTLF 1291
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNLNRLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1292 rgcirtnldPLGVYS-----------------DDEIWKALEKCQLKTTISNlpnKLDSSVSDegenWSVGQRQLFCLGRV 1354
Cdd:PRK14258 101 ---------PMSVYDnvaygvkivgwrpkleiDDIVESALKDADLWDEIKH---KIHKSALD----LSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1355 LLKRNKILVLDEATASIDSATDAIIQRIIREEF--ADCTVITVAHRVPTVID-SDMVMVLS-----FGDLVEYNEPSKL 1425
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRlSDFTAFFKgnenrIGQLVEFGLTKKI 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
616-781 |
5.23e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPK--VSGTVKVfgsiayvSQTSWIQSGTIRDNILYGKPMesrryN 693
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGtpVAGCVDV-------PDNQFGREASLIDAIGRKGDF-----K 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 694 AAIKAcaldkdMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKcVEDSLKE- 772
Cdd:COG2401 114 DAVEL------LNAVGLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN-LQKLARRa 186
|
170
....*....|
gi 334185504 773 -KTVILVTHQ 781
Cdd:COG2401 187 gITLVVATHH 196
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
607-780 |
5.65e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 63.99 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 607 WEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLhAVLG--EIPKvSGTVKVFG-----------------SIAYVS 667
Cdd:COG4181 19 GTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLL-GLLAglDRPT-SGTVRLAGqdlfaldedararlrarHVGFVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 668 QTS-WIQSGTIRDNILYgkPMESRRY-NAAIKACALDKDMnGFGHgdltEIGQRGINLSGGQKQRIQLARAVYADADVYL 745
Cdd:COG4181 97 QSFqLLPTLTALENVML--PLELAGRrDARARARALLERV-GLGH----RLDHYPAQLSGGEQQRVALARAFATEPAILF 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334185504 746 LDDPFSAVDAHT----AGVLFhkcvedSLKEK---TVILVTH 780
Cdd:COG4181 170 ADEPTGNLDAATgeqiIDLLF------ELNRErgtTLVLVTH 205
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1221-1436 |
9.78e-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: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRlVEPA---SGCILIDGIDISKIGLKDLRMK-LSIIPQEPTL------ 1290
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLvpelsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1291 ----FRGCIRTNldPLGVYSDDEIWKALEKCQLKTTISNLPNKLdsSVSDEGenwsVGQRQLFCLGRVLLKRNKILVLDE 1366
Cdd:TIGR02633 96 aeniFLGNEITL--PGGRMAYNAMYLRAKNLLRELQLDADNVTR--PVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 1367 ATASIDSATDAIIQRIIREEFA-DCTVITVAHRVPTVID-SDMVMVLSFGDLVEyNEPSKLMETDSYFSKLV 1436
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHVA-TKDMSTMSEDDIITMMV 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1204-1427 |
1.04e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.38 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPL---VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG----LKD 1276
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1277 LRMKLSIIPQ--EPTLFRGCIRTNL----DPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFC 1350
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVafgpQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSG-------GQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1351 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFAD-CTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLME 1427
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
616-796 |
1.07e-10 |
|
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: 63.22 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQTSWI-QSGTIRDN 680
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLfPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 ILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIG------QRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 754
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREARERAEELLERVGladladRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 755 ----AHTAGVLfhkcveDSLKEK--TVILVTHQ------------VMEEGTITQSGKYEE 796
Cdd:cd03219 176 peetEELAELI------RELRERgiTVLLVEHDmdvvmsladrvtVLDQGRVIAEGTPDE 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
626-781 |
1.13e-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: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 626 GQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGsiayvsQTSWIQSGTIRDNILYG----------KPMESRRYNAA 695
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG------GPLDFQRDSIARGLLYLghapgikttlSVLENLRFWHA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 696 IKAC-----ALDK-DMNGFGHgdlTEIGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDS 769
Cdd:cd03231 100 DHSDeqveeALARvGLNGFED---RPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHC 172
|
170
....*....|..
gi 334185504 770 LKEKTVILVTHQ 781
Cdd:cd03231 173 ARGGMVVLTTHQ 184
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
617-797 |
1.27e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.05 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 617 RNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG--EI----------------PKVSGTVKVFGSIAYVSQTSwiqsgtIR 678
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleDItsgdlfigekrmndvpPAERGVGMVFQSYALYPHLS------VA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 679 DNILYG-------KPMESRRYNAAIKACALDKdmngfghgdLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFS 751
Cdd:PRK11000 94 ENMSFGlklagakKEEINQRVNQVAEVLQLAH---------LLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 752 AVDahtAGVLFHKCVEDSLKEK----TVILVTHQ------------VMEEGTITQSGKYEEL 797
Cdd:PRK11000 163 NLD---AALRVQMRIEISRLHKrlgrTMIYVTHDqveamtladkivVLDAGRVAQVGKPLEL 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1220-1434 |
1.38e-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: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRL--VEPASGCIL---------------------------------I 1264
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1265 DGIDISKIGLKDLRMKLSIIPQ-------EPTLFRGCIRTnLDPLGVYSDDEIWKA---LEKCQLKTTISNLPNKLdssv 1334
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQrtfalygDDTVLDNVLEA-LEEIGYEGKEAVGRAvdlIEMVQLSHRITHIARDL---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1335 sdegenwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHrVPTVID--SDMVMV 1410
Cdd:TIGR03269 170 -------SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSH-WPEVIEdlSDKAIW 241
|
250 260
....*....|....*....|....*...
gi 334185504 1411 LSFGDLVEYNEP----SKLMETDSYFSK 1434
Cdd:TIGR03269 242 LENGEIKEEGTPdevvAVFMEGVSEVEK 269
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1220-1426 |
1.39e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD-LRMKLSIIPQEPTLFRgcirtn 1298
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFR------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1299 ldPLGVYSDD----EIWKALEKCQLKTTISNLPNKLD-SSVSDE-GENWSVGQRQLFCLGRVLLKRNKILVLDEATASID 1372
Cdd:PRK10895 92 --RLSVYDNLmavlQIRDDLSAEQREDRANELMEEFHiEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1373 SATDAIIQRIIrEEFAD--CTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLM 1426
Cdd:PRK10895 170 PISVIDIKRII-EHLRDsgLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1221-1418 |
1.45e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.66 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDISKIGLKDLRMKLsiIPQEPT--------- 1289
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRSQRIRM--IFQDPStslnprqri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1290 --LFRGCIRTNLDPLGVYSDDEIWKALEKCQLKTTISN-LPNKLDSsvsdegenwsvGQRQLFCLGRVLLKRNKILVLDE 1366
Cdd:PRK15112 107 sqILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASyYPHMLAP-----------GQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1367 ATASID-SATDAIIQRIIR-EEFADCTVITVAHRVPTVID-SDMVMVLSFGDLVE 1418
Cdd:PRK15112 176 ALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVE 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1220-1411 |
2.06e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCIlidgidiskigLKDLRMKLSIIPQ----EPTLFRGCI 1295
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQklylDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1296 R-TNLDPlGVYSDDeIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATASID-- 1372
Cdd:PRK09544 88 RfLRLRP-GTKKED-ILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDvn 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334185504 1373 ---SATDAIIQriIREEFaDCTVITVAHRVPTVI-DSDMVMVL 1411
Cdd:PRK09544 155 gqvALYDLIDQ--LRREL-DCAVLMVSHDLHLVMaKTDEVLCL 194
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
616-784 |
2.66e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.20 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS---------IAYVSQTSwiqsG-----TIRDNI 681
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpldpedrrrIGYLPEER----GlypkmKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 LY-----GkpMESRRYNAAIKAcALDKdmngFGhgdLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA 755
Cdd:COG4152 93 VYlarlkG--LSKAEAKRRADE-WLER----LG---LGDRANKKVeELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP 162
|
170 180 190
....*....|....*....|....*....|....
gi 334185504 756 HTAGVLfhkcvEDSLKE-----KTVILVTHQvME 784
Cdd:COG4152 163 VNVELL-----KDVIRElaakgTTVIFSSHQ-ME 190
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1204-1429 |
3.15e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1283
Cdd:PRK13647 5 IEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEP-------TLFR----GCIRTNLDPLGVysDDEIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLG 1352
Cdd:PRK13647 84 VFQDPddqvfssTVWDdvafGPVNMGLDKDEV--ERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1353 RVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVA-HRVPTVID-SDMVMVLSFGDLVEYNEPSKLMETD 1429
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1199-1380 |
3.70e-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: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1199 PSNGTIHLQELKIRY-RPNAPL-VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKI---G 1273
Cdd:COG4181 4 SSAPIIELRGLTKTVgTGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1274 LKDLR-MKLSIIPQE----PTLfrgcirTNLD----PLGVYSDDEIWK----ALEKCQLKTTISNLPNKLdssvsdegen 1340
Cdd:COG4181 84 RARLRaRHVGFVFQSfqllPTL------TALEnvmlPLELAGRRDARAraraLLERVGLGHRLDHYPAQL---------- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 334185504 1341 wSVGQRQLFCLGRVLLKRNKILVLDEATASIDSAT-DAIIQ 1380
Cdd:COG4181 148 -SGGEQQRVALARAFATEPAILFADEPTGNLDAATgEQIID 187
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1221-1435 |
3.79e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.49 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI-SKIG---LKDLRMKLSIIPQ--EPTLFRGC 1294
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKdkyIRPVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1295 I-----------RTNLDPLGVYSDDEIwkaLEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILV 1363
Cdd:PRK13646 103 VereiifgpknfKMNLDEVKNYAHRLL---MDLGFSRDVMSQSPFQM-----------SGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1364 LDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMETDSYFSKL 1435
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1229-1374 |
3.90e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.52 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1229 REGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIglKDLRMKLSIIPQEPTLF-----RGCIRTNLDPlG 1303
Cdd:PRK10771 23 ERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT--PPSRRPVSMLFQENNLFshltvAQNIGLGLNP-G 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 1304 VYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLDEATASIDSA 1374
Cdd:PRK10771 100 LKLNAAQREKLHAIARQMGIEDLLARLPGQLSG-------GQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
616-797 |
4.66e-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: 64.05 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG--EIPKVSGtvKVFGSIAYVSQTSWIQ-------------------- 673
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSG--RIIYHVALCEKCGYVErpskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 674 ------SGTIRDNI-------------LYG---------KPMESRRYNA--AIKACALDKDMNGFGHgDLTEIGQrgiNL 723
Cdd:TIGR03269 94 vdfwnlSDKLRRRIrkriaimlqrtfaLYGddtvldnvlEALEEIGYEGkeAVGRAVDLIEMVQLSH-RITHIAR---DL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 724 SGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGvLFHKCVEDSLKEK--TVILVTH--QVMEE----------GTIT 789
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASgiSMVLTSHwpEVIEDlsdkaiwlenGEIK 248
|
....*...
gi 334185504 790 QSGKYEEL 797
Cdd:TIGR03269 249 EEGTPDEV 256
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
625-786 |
5.09e-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: 59.31 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 625 HGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQSGTIrdnilygkpmesrrynaaikacaldkd 704
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 705 mngfghgdlteIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEK------TVILV 778
Cdd:smart00382 54 -----------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLkseknlTVILT 122
|
....*...
gi 334185504 779 THQVMEEG 786
Cdd:smart00382 123 TNDEKDLG 130
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1220-1418 |
5.17e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.01 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKI---GLKDLRMKLSIIPQE-PTLF--RG 1293
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDsISAVnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1294 CIR----------TNLDPlgvysDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILV 1363
Cdd:PRK10419 107 TVReiireplrhlLSLDK-----AERLARASEMLRAVDLDDSVLDKRPPQLSG-------GQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1364 LDEATASIDSATDA-IIQRI--IREEFAD-CTVIT--------VAHRvptvidsdmVMVLSFGDLVE 1418
Cdd:PRK10419 175 LDEAVSNLDLVLQAgVIRLLkkLQQQFGTaCLFIThdlrlverFCQR---------VMVMDNGQIVE 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1211-1417 |
5.43e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 61.71 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1211 IRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTL 1290
Cdd:PRK13548 8 LSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1291 -F----RGCIRTNLDPLGVYS---DDEIWKALEKCQLkttiSNLPNKLDSSVSdeGenwsvGQRQLFCLGRVLL------ 1356
Cdd:PRK13548 88 sFpftvEEVVAMGRAPHGLSRaedDALVAAALAQVDL----AHLAGRDYPQLS--G-----GEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 1357 KRNKILVLDEATASIDSATDAIIQRIIReEFAD---CTVITVAHrvptviD-------SDMVMVLSFGDLV 1417
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLAR-QLAHergLAVIVVLH------DlnlaaryADRIVLLHQGRLV 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
618-754 |
6.21e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.45 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 618 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTV--------------KVFGSIAYVSQTSWI-QSGTIRDNIL 682
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplhaRARRGIGYLPQEASIfRRLSVYDNLM 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 683 ygKPMESRR-YNAAIKACALDKDMNGFGHGDLTE-IGQrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 754
Cdd:PRK10895 101 --AVLQIRDdLSAEQREDRANELMEEFHIEHLRDsMGQ---SLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1218-1418 |
6.65e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.42 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1218 PLVLK---GISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMK---LSIIPQEPtLF 1291
Cdd:PRK15079 31 PKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDP-LA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1292 RGCIRTNL-----DPLGVY----SDDEIWKALEKCQLKTTIsnLPNKLDSSVSDegenWSVGQRQLFCLGRVLLKRNKIL 1362
Cdd:PRK15079 110 SLNPRMTIgeiiaEPLRTYhpklSRQEVKDRVKAMMLKVGL--LPNLINRYPHE----FSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 1363 VLDEATASIDSATDA----IIQRIIREefADCTVITVAHRVPTV--IdSDMVMVLSFGDLVE 1418
Cdd:PRK15079 184 ICDEPVSALDVSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVkhI-SDRVLVMYLGHAVE 242
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1220-1419 |
8.68e-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: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLK-DLRMKLSIIpqEPTLFRGCIrtn 1298
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGgGFNPELTGR--ENIYLNGRL--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1299 ldpLGVySDDEIWKALEKCQlktTISNLPNKLDSSVSdegeNWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAI 1378
Cdd:cd03220 112 ---LGL-SRKEIDEKIDEII---EFSELGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334185504 1379 IQRIIREEFADC-TVITVAHRVPTVID-SDMVMVLSFGDLVEY 1419
Cdd:cd03220 181 CQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFD 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
614-784 |
8.93e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.32 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSW----------IQSG------T 676
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGeNIPAMSRSRLytvrkrmsmlFQSGalftdmN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 677 IRDNILYGKPMESRRYNAAIKACALDKdmngfghgdLTEIGQRGI------NLSGGQKQRIQLARAVYADADVYLLDDPF 750
Cdd:PRK11831 101 VFDNVAYPLREHTQLPAPLLHSTVMMK---------LEAVGLRGAaklmpsELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 334185504 751 SAVDAHTAGVLFhKCVeDSLKEK---TVILVTHQVME 784
Cdd:PRK11831 172 VGQDPITMGVLV-KLI-SELNSAlgvTCVVVSHDVPE 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
666-798 |
9.15e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 666 VSQTSWIQSGTIRDNILYGKPMESRR-YNAAIKACALDKDMNGFGHGDLTEIGQRGINLSGGQKQRIQLARAVYADADVY 744
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKEDATREdVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 745 LLDDPFSAVDAHTAGVLFHKCVEDSLK-EKTVILVTHQVM---------------EEGTITQS-GKYEELL 798
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIITIAHRIAsikrsdkivvfnnpdRTGSFVQAhGTHEELL 1451
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1227-1424 |
1.02e-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: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1227 TFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKdlrmklsIIPQEPTLFRGCIRTNLDPLGVYS 1306
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY-------IKADYEGTVRDLLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1307 ddeiwkalekcQLKTTISNlPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIReE 1386
Cdd:cd03237 94 -----------YFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR-R 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 334185504 1387 FADCTVITVahrvpTVIDSDMVMVLSFGD--LVEYNEPSK 1424
Cdd:cd03237 161 FAENNEKTA-----FVVEHDIIMIDYLADrlIVFEGEPSV 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
614-760 |
1.25e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.34 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVS----QTSWIQSG 675
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDNI------------LYGKPMESRRYNAAIKAcaldkdmngFG---HGDLTEIGqrgiNLSGGQKQRIQLARAVYAD 740
Cdd:COG1129 346 SIRENItlasldrlsrggLLDRRRERALAEEYIKR---------LRiktPSPEQPVG----NLSGGNQQKVVLAKWLATD 412
|
170 180
....*....|....*....|
gi 334185504 741 ADVYLLDDPfsavdahTAGV 760
Cdd:COG1129 413 PKVLILDEP-------TRGI 425
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
616-784 |
1.43e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.46 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGeIPKVSGTVKVFGSiAYVSQTS--------------WiqsGTIRDNI 681
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGT-APLAEARedtrlmfqdarllpW---KKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 ---LYGKPMESRRynAAIKACALDKDMNGFGHGdlteigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTA 758
Cdd:PRK11247 103 glgLKGQWRDAAL--QALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180
....*....|....*....|....*....
gi 334185504 759 gVLFHKCVEdSLKEK---TVILVTHQVME 784
Cdd:PRK11247 170 -IEMQDLIE-SLWQQhgfTVLLVTHDVSE 196
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1204-1434 |
1.44e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.59 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPlVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSI 1283
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1284 IPQEP--TLFRGCIRTNL--DPLGVYSDDE-----IWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRV 1354
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIafGPINLGLDEEtvahrVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1355 LLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMETDSY 1431
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
...
gi 334185504 1432 FSK 1434
Cdd:PRK13652 232 LAR 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
629-818 |
1.90e-09 |
|
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: 61.28 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 629 VAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------------SIAYVSQ-TSWIQSGTIRDNILYGKpmesR 690
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQeARLFPHLSVRGNLRYGM----K 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 691 RYNAAIKACALDK--DMNGFGHgdlteIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVD-AHTAGVL-FHKC 765
Cdd:TIGR02142 102 RARPSERRISFERviELLGIGH-----LLGRLPGrLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdPRKYEILpYLER 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 766 VEDSLKeKTVILVTHQ------------VMEEGTITQSGKYEEllMMGTAFQQLVnAHNDAVTVL 818
Cdd:TIGR02142 177 LHAEFG-IPILYVSHSlqevlrladrvvVLEDGRVAAAGPIAE--VWASPDLPWL-AREDQGSLI 237
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1220-1417 |
2.03e-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: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFrgcirTNL 1299
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLW-----WDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1300 DPLGVY---------SDDEIWKALEKCqlkTTISNLPNKLDSSVsdegENWSVGQRQLFCLGRVLLKRNKILVLDEATAS 1370
Cdd:cd03267 111 PVIDSFyllaaiydlPPARFKKRLDEL---SELLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 334185504 1371 IDSATDAIIQRIIREEFAD--CTVITVAHRVPTVID-SDMVMVLSFGDLV 1417
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1220-1266 |
2.05e-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: 2.05e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG 1266
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
616-872 |
2.22e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.20 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------------SIAYVSQT-SWIQSGTI 677
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 678 RDNILYGK-----PMESRRYNA--AIKACALDKdmngFGHGDLTEigqrginLSGGQKQRIQLARAVYADADVYLLDDPF 750
Cdd:PRK10070 124 LDNTAFGMelagiNAEERREKAldALRQVGLEN----YAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 751 SAVDAHTAGVLFHKCVEDSLK-EKTVILVTH---QVMEEG---TITQSGkyeELLMMGTAFQQLVNAHNDAVTV----LP 819
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhQRTIVFISHdldEAMRIGdriAIMQNG---EVVQVGTPDEILNNPANDYVRTffrgVD 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 820 LASNESLGDLRKEGKDREIRNMtvvekieeeiektdiPG------VQLTQEEEKESGYV 872
Cdd:PRK10070 270 ISQVFSAKDIARRTPNGLIRKT---------------PGfgprsaLKLLQDEDREYGYV 313
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1220-1438 |
2.36e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.49 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDgidiskiglkdlrMKLSIIPQEPTLFRGCIRTNL 1299
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1300 dplgVYSDDE----IWKALEKCQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATasidSAT 1375
Cdd:PTZ00243 742 ----LFFDEEdaarLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL----SAL 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 1376 DAII-QRIIREEF----ADCTVITVAHRVPTVIDSDMVMVLSFGDLVEYNEPSKLMETdSYFSKLVAE 1438
Cdd:PTZ00243 814 DAHVgERVVEECFlgalAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT-SLYATLAAE 880
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
616-785 |
2.66e-09 |
|
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: 58.92 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGsIAYVSQTSWIQSG--------------TIRDNI 681
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-FDVVKEPAEARRRlgfvsdstglydrlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 -----LYGkpMESRRYNAAIKACALDKDMNGFghgdlteIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 756
Cdd:cd03266 100 eyfagLYG--LKGDELTARLEELADRLGMEEL-------LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190
....*....|....*....|....*....|....
gi 334185504 757 TAGVLFhkcveDSLKE-----KTVILVTHqVMEE 785
Cdd:cd03266 171 ATRALR-----EFIRQlralgKCILFSTH-IMQE 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1173-1416 |
2.72e-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: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1173 ERIKQYMNIPEEPPAIID---DKRPPSSWPSngtIHLQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLIS 1249
Cdd:TIGR01257 898 EPLTEEMEDPEHPEGINDsffERELPGLVPG---VCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLS 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1250 ALFRLVEPASGCILIDGIDIsKIGLKDLRMKLSIIPQEPTLFRGCirTNLDPLGVYSDDEiWKALEKCQLKTTISNLPNK 1329
Cdd:TIGR01257 975 ILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHL--TVAEHILFYAQLK-GRSWEEAQLEMEAMLEDTG 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1330 LDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTV-IDSDMV 1408
Cdd:TIGR01257 1051 LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRI 1130
|
....*...
gi 334185504 1409 MVLSFGDL 1416
Cdd:TIGR01257 1131 AIISQGRL 1138
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
616-792 |
2.80e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 58.31 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG-EIPKVSGtvkvfGSIAYVSQtswiqsgtirdNILyGKPMESR---- 690
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhPKYEVTE-----GEILFKGE-----------DIT-DLPPEERarlg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 691 -----RYNAAIKacaldkdmnGFGHGDLTeigqRGIN--LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAhTAGVLFH 763
Cdd:cd03217 79 iflafQYPPEIP---------GVKNADFL----RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DALRLVA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334185504 764 KCVEDSLKEKT-VILVTH-------------QVMEEGTITQSG 792
Cdd:cd03217 145 EVINKLREEGKsVLIITHyqrlldyikpdrvHVLYDGRIVKSG 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1220-1402 |
2.89e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIG-LKDLRMKLSIIPQEPTLFrgcirTN 1298
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLF-----PN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1299 LDPLgvysdDEIWKALEKCQ-----LKTTISNLPNKLDSSVSdeGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDS 1373
Cdd:PRK15439 101 LSVK-----ENILFGLPKRQasmqkMKQLLAALGCQLDLDSS--AGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190
....*....|....*....|....*....|
gi 334185504 1374 A-TDAIIQRIIREEFADCTVITVAHRVPTV 1402
Cdd:PRK15439 174 AeTERLFSRIRELLAQGVGIVFISHKLPEI 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
616-785 |
4.00e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.80 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQ-TSWIQSGTIRDN 680
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQeLNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 ILYGKPMESR---RYNAAIKACA--LDKdmngFG-HGDL-TEIGqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAV 753
Cdd:COG1129 100 IFLGREPRRGgliDWRAMRRRARelLAR----LGlDIDPdTPVG----DLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190
....*....|....*....|....*....|....
gi 334185504 754 DAHTAGVLFhKCVEDsLKEK--TVILVTHQvMEE 785
Cdd:COG1129 172 TEREVERLF-RIIRR-LKAQgvAIIYISHR-LDE 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1220-1372 |
6.10e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.84 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPT---------- 1289
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATtpgditvqel 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1290 LFRGciRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKldsSVsdegENWSVGQRQLFCLGRVLLKRNKILVLDEATA 1369
Cdd:PRK10253 102 VARG--RYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQ---SV----DTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
...
gi 334185504 1370 SID 1372
Cdd:PRK10253 173 WLD 175
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
604-780 |
7.46e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.59 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 604 NFGWEPETKIPT--LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVfGSIAYVSQTSWIQSGTIRDN- 680
Cdd:PRK13643 8 NYTYQPNSPFASraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIKPVRKKv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 -ILYGKPMESRRYNAAIKACALDKDMNGFGHGDLTEIGQRGI---------------NLSGGQKQRIQLARAVYADADVY 744
Cdd:PRK13643 87 gVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLemvgladefwekspfELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 334185504 745 LLDDPFSAVDAhTAGVLFHKCVEDSLKE-KTVILVTH 780
Cdd:PRK13643 167 VLDEPTAGLDP-KARIEMMQLFESIHQSgQTVVLVTH 202
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1201-1293 |
7.69e-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: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1201 NGTIHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGL-KDLRM 1279
Cdd:COG1137 1 MMTLEAENLVKSYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhKRARL 78
|
90
....*....|....
gi 334185504 1280 KLSIIPQEPTLFRG 1293
Cdd:COG1137 79 GIGYLPQEASIFRK 92
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
610-796 |
8.70e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.52 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 610 ETKipTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG---------------SIAYVSQTSWIQ- 673
Cdd:PRK13637 19 EKK--ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPEYQl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 674 -SGTIRDNILYGkPME--------SRRYNAAIKACALD----KDMNGFghgdlteigqrgiNLSGGQKQRIQLARAVYAD 740
Cdd:PRK13637 97 fEETIEKDIAFG-PINlglseeeiENRVKRAMNIVGLDyedyKDKSPF-------------ELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 741 ADVYLLDDPFSAVDAHTAGVLFHKCVEdsLKEK---TVILVTHQ------------VMEEGTITQSGKYEE 796
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKE--LHKEynmTIILVSHSmedvakladriiVMNKGKCELQGTPRE 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1220-1379 |
1.03e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVePASGCILIDGIDISKIGLKDL---RMKLSIIPQEPTlfrgcir 1296
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1297 TNLDP-----------LGVYS--------DDEIWKALEKCQLK-TTISNLPNKldssvsdegenWSVGQRQLFCLGRVLL 1356
Cdd:PRK15134 373 SSLNPrlnvlqiieegLRVHQptlsaaqrEQQVIAVMEEVGLDpETRHRYPAE-----------FSGGQRQRIAIARALI 441
|
170 180
....*....|....*....|...
gi 334185504 1357 KRNKILVLDEATASIDSATDAII 1379
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQI 464
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
612-796 |
1.07e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 58.66 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV-LGEIPKvSGTVKVFG----------------SIAYVSQT-SWIQ 673
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInLLERPT-SGRVLVDGqdltalsekelrkarrQIGMIFQHfNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 674 SGTIRDNI-----LYGKPmesrryNAAIKACALDK-DMNGfghgdLTEIGQR-GINLSGGQKQRIQLARAVYADADVYLL 746
Cdd:PRK11153 96 SRTVFDNValpleLAGTP------KAEIKARVTELlELVG-----LSDKADRyPAQLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 747 DDPFSAVD-AHTAGVLfhkcveDSLKE------KTVILVTHQ------------VMEEGTITQSGKYEE 796
Cdd:PRK11153 165 DEATSALDpATTRSIL------ELLKDinrelgLTIVLITHEmdvvkricdrvaVIDAGRLVEQGTVSE 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1221-1417 |
1.09e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.19 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD---LRMKLSIIPQEPTLFRGciRT 1297
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMD--RT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1298 NLD----PL---GVYSDD---EIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEA 1367
Cdd:PRK10908 96 VYDnvaiPLiiaGASGDDirrRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1368 TASIDSATDAIIQRIIrEEF--ADCTVITVAHRVPTVIDSDM-VMVLSFGDLV 1417
Cdd:PRK10908 165 TGNLDDALSEGILRLF-EEFnrVGVTVLMATHDIGLISRRSYrMLTLSDGHLH 216
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1125-1366 |
1.13e-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: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1125 ALLLILIpkG---YIAPGLVGLSLS----YALTLTqtqvFLTR-------WYCTLSNSIISVERIKQY---MNIPEEPPA 1187
Cdd:COG4615 241 LLFFALI--GlilFLLPALGWADPAvlsgFVLVLL----FLRGplsqlvgALPTLSRANVALRKIEELelaLAAAEPAAA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1188 IIDDKRPPSSWpsnGTIHLQELKIRYRP---NAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILI 1264
Cdd:COG4615 315 DAAAPPAPADF---QTLELRGVTYRYPGedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1265 DGIDISKIGLKDLRMKLSIIPQEPTLFrgciRTNLDPLGVYSDDEIWKALEKCQL--KTTISNlpNKLdSSVsdegeNWS 1342
Cdd:COG4615 392 DGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLERLELdhKVSVED--GRF-STT-----DLS 459
|
250 260
....*....|....*....|....*....
gi 334185504 1343 VGQRQlfclgRV-----LLKRNKILVLDE 1366
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 ... |
1220-1414 |
1.17e-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: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKiglkdlrmklsiipQEPTLFRGC----- 1294
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF--------------QRDSIARGLlylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1295 ---IRTNLDPL-------GVYSDDEIWKALEKCQLkTTISNLP-NKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILV 1363
Cdd:cd03231 81 apgIKTTLSVLenlrfwhADHSDEQVEEALARVGL-NGFEDRPvAQL-----------SAGQQRRVALARLLLSGRPLWI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 334185504 1364 LDEATASIDSATDAIIQRIIREEFADCTVITVAHRVPTVIDSDMVMVLSFG 1414
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1221-1428 |
1.22e-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: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDlrMKLSIIPQEPTLFRG-CIRTNL 1299
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1300 dPLGV--------YSDDEIWKA----LEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEA 1367
Cdd:cd03296 96 -AFGLrvkprserPPEAEIRAKvhelLKLVQLDWLADRYPAQL-----------SGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 1368 TASIDSATDAIIQRIIREEFADCTVIT--VAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMET 1428
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDELHVTTvfVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1204-1399 |
1.27e-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: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGC---IL---IDGIDI----SKIG 1273
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLFgerRGGEDVwelrKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1274 LKDLRMKLSIIPQEPTL------FRGCIrtnldplGVY---SDDEIWKALEkcQLKTT-ISNLPNKLDSSVSDegenwsv 1343
Cdd:COG1119 82 LVSPALQLRFPRDETVLdvvlsgFFDSI-------GLYrepTDEQRERARE--LLELLgLAHLADRPFGTLSQ------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1344 GQRQLFCLGRVLLKRNKILVLDEATASID-SATDAIIQRIirEEFA---DCTVITVAHRV 1399
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDlGARELLLALL--DKLAaegAPTLVLVTHHV 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
610-803 |
1.29e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 610 ETKIPT--LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSiaYVSQTSWIQSGTIRDN------- 680
Cdd:PRK11629 17 EGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAELRNQklgfiyq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 -----------------ILYG--KPMES-RRYNAAIKACALDKDMNgfghgdlteigQRGINLSGGQKQRIQLARAVYAD 740
Cdd:PRK11629 95 fhhllpdftalenvampLLIGkkKPAEInSRALEMLAAVGLEHRAN-----------HRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 741 ADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVIL-VTHQV-----------MEEGTITQsgkyeELLMMGTA 803
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLvVTHDLqlakrmsrqleMRDGRLTA-----ELSLMGAE 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
616-797 |
1.41e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 57.72 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVfGSIAYVSQTSWIQSGTIRD---------------- 679
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLKPLRKkvgivfqfpehqlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 680 ----NILYGkPME--------SRRYNAAIKACALDKDMngfghgdlteIGQRGINLSGGQKQRIQLARAVYADADVYLLD 747
Cdd:PRK13634 102 tvekDICFG-PMNfgvseedaKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 748 DPfsavdahTAGV----------LFHKCvedsLKEK--TVILVTHQ------------VMEEGTITQSGKYEEL 797
Cdd:PRK13634 171 EP-------TAGLdpkgrkemmeMFYKL----HKEKglTTVLVTHSmedaaryadqivVMHKGTVFLQGTPREI 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1221-1418 |
1.54e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.05 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI---SKIGLKDLRMKLSIIPQEP--TLF-RGC 1294
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPygSLNpRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1295 IRTNL-DPLGVYSD-------DEIWKALEKCQLKTTISN-LPNKldssvsdegenWSVGQRQLFCLGRVLLKRNKILVLD 1365
Cdd:PRK11308 111 VGQILeEPLLINTSlsaaerrEKALAMMAKVGLRPEHYDrYPHM-----------FSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 1366 EATasidSATDAIIQRIIREEFAD------CTVITVAHRVPTV--IdSDMVMVLSFGDLVE 1418
Cdd:PRK11308 180 EPV----SALDVSVQAQVLNLMMDlqqelgLSYVFISHDLSVVehI-ADEVMVMYLGRCVE 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
614-798 |
1.88e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 57.30 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSL---LHAVL--------------GEIPKVSGTVKVFGSIAYVSQTSWIQSgT 676
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLrpqkgkvlvsgidtGDFSKLQGIRKLVGIVFQNPETQFVGR-T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 677 IRDNILYG------KPMESR-RYNAAIKACALDKdmngFGHgdlteigQRGINLSGGQKQRIQLARAVYADADVYLLDDP 749
Cdd:PRK13644 95 VEEDLAFGpenlclPPIEIRkRVDRALAEIGLEK----YRH-------RSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 750 FSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQ-----------VMEEGTITQSGKYEELL 798
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNleelhdadriiVMDRGKIVLEGEPENVL 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1200-1426 |
2.67e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.52 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1200 SNGTIHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRM 1279
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1280 KLSIIPQEPTLfrgciRTNLDPlgVYSDDEIWK----------------ALEKCQLKTTISNLPNKLDSSVSDEGE---N 1340
Cdd:PRK10619 80 KVADKNQLRLL-----RTRLTM--VFQHFNLWShmtvlenvmeapiqvlGLSKQEARERAVKYLAKVGIDERAQGKypvH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1341 WSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADC-TVITVAHRVPTVID-SDMVMVLSFGDLVE 1418
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGkTMVVVTHEMGFARHvSSHVIFLHQGKIEE 232
|
....*...
gi 334185504 1419 YNEPSKLM 1426
Cdd:PRK10619 233 EGAPEQLF 240
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
616-754 |
2.71e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.66 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--IAYVSQTSWIQS--------------GTIRD 679
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYLDTtlpltvnrflrlrpGTKKE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 680 NILygkPMeSRRYNAaikACALDKDMNgfghgdlteigqrgiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 754
Cdd:PRK09544 100 DIL---PA-LKRVQA---GHLIDAPMQ---------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1224-1416 |
2.77e-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: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1224 ISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPA-SGCILIDG--IDIsKIGLKDLRMKLSIIPQE------------- 1287
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDI-RNPAQAIRAGIAMVPEDrkrhgivpilgvg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1288 -----PTLFRGCIRTNLDPLGvySDDEIWKALEKCQLKTTISNLP-NKLdssvsdegenwSVGQRQLFCLGRVLLKRNKI 1361
Cdd:TIGR02633 358 knitlSVLKSFCFKMRIDAAA--ELQIIGSAIQRLKVKTASPFLPiGRL-----------SGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1362 LVLDEATASIDSATDAIIQRIIREEFAD-CTVITVAHRVPTVID-SDMVMVLSFGDL 1416
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1219-1385 |
2.77e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.65 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1219 LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDISK-------IGLKDLrMKLSIIPQEPT 1289
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdIDDPDvaeachyLGHRNA-MKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1290 LFRGCIRtNLDPLGVYSddeiwkALEKCQLKtTISNLPNKldssvsdegeNWSVGQRQLFCLGRVLLKRNKILVLDEATA 1369
Cdd:PRK13539 95 EFWAAFL-GGEELDIAA------ALEAVGLA-PLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170
....*....|....*.
gi 334185504 1370 SIDSATDAIIQRIIRE 1385
Cdd:PRK13539 157 ALDAAAVALFAELIRA 172
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
616-780 |
3.03e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYV--------------------SQTSWIQSG 675
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgkdifqidaiklrkevgmvfQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDNILYgkPMES------RRYNAAIKACALDKDMNGFGHGDLTEIGQRginLSGGQKQRIQLARAVYADADVYLLDDP 749
Cdd:PRK14246 106 SIYDNIAY--PLKShgikekREIKKIVEECLRKVGLWKEVYDRLNSPASQ---LSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190
....*....|....*....|....*....|.
gi 334185504 750 FSAVDAHTAGVLfHKCVEDSLKEKTVILVTH 780
Cdd:PRK14246 181 TSMIDIVNSQAI-EKLITELKNEIAIVIVSH 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1221-1399 |
3.62e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD-LRMKLSIIPQE----------PT 1289
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQElsvideltvlEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1290 LFRGCIRTNlDPLGVYSDDeiWKAL-EKCQLKTTISNLPNKLDSSVsdegENWSVGQRQLFCLGRVLLKRNKILVLDEAT 1368
Cdd:PRK09700 101 LYIGRHLTK-KVCGVNIID--WREMrVRAAMMLLRVGLKVDLDEKV----ANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190
....*....|....*....|....*....|....*
gi 334185504 1369 ASI-DSATD---AIIQRIIREEFAdctVITVAHRV 1399
Cdd:PRK09700 174 SSLtNKEVDylfLIMNQLRKEGTA---IVYISHKL 205
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
613-797 |
3.93e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 613 IPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQTSWI-QSGTI 677
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLfPNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 678 RDNILYGKPME---SRRYNAAIKA--CALDKDMNGfghGDLtEIGQRginlsggqkQRIQLARAVYADADVYLLDDPFSA 752
Cdd:PRK15439 104 KENILFGLPKRqasMQKMKQLLAAlgCQLDLDSSA---GSL-EVADR---------QIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 753 VDAHTAGVLFHKCveDSLKEKTV--ILVTHQ------------VMEEGTITQSGKYEEL 797
Cdd:PRK15439 171 LTPAETERLFSRI--RELLAQGVgiVFISHKlpeirqladrisVMRDGTIALSGKTADL 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1199-1418 |
4.93e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1199 PSNGTIHLQELKIRYRPNAPLV--LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI-------------L 1263
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1264 IDGIDISKIGLKDLR-MKLSIIPQEPTlfrgcirTNLDPL---------------GVYSDDEIWKA---LEKCQL---KT 1321
Cdd:PRK10261 88 IELSEQSAAQMRHVRgADMAMIFQEPM-------TSLNPVftvgeqiaesirlhqGASREEAMVEAkrmLDQVRIpeaQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1322 TISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIR--EEFADCTVITVAHRV 1399
Cdd:PRK10261 161 ILSRYPHQL-----------SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDM 229
|
250 260
....*....|....*....|
gi 334185504 1400 PTVID-SDMVMVLSFGDLVE 1418
Cdd:PRK10261 230 GVVAEiADRVLVMYQGEAVE 249
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
589-819 |
5.04e-08 |
|
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: 55.97 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 589 SGLDASGTAVDIQVGNFGWEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG------- 661
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLFGAKQRA-PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqld 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 662 ---------SIAYVSQTSWIQ---SGTIRDNIlyGKPMES----------RRYNAAIKACALDKDmngfgHGDlteigQR 719
Cdd:TIGR02769 80 rkqrrafrrDVQLVFQDSPSAvnpRMTVRQII--GEPLRHltsldeseqkARIAELLDMVGLRSE-----DAD-----KL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 720 GINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEdsLKEK---TVILVTHQ------------VME 784
Cdd:TIGR02769 148 PRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRK--LQQAfgtAYLFITHDlrlvqsfcqrvaVMD 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 334185504 785 EGTITQSGKYEELLMMGT-AFQQLVNAhndavtVLP 819
Cdd:TIGR02769 226 KGQIVEECDVAQLLSFKHpAGRNLQSA------VLP 255
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
610-780 |
5.91e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.43 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 610 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHaVLGEIPK-VSGTVKV--------------------FGSI----A 664
Cdd:PRK10535 18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVagqdvatldadalaqlrrehFGFIfqryH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 665 YVSQTSWIQSGTIrDNILYGKPMESRRYnaaiKACALdkdMNGFGHGDltEIGQRGINLSGGQKQRIQLARAVYADADVY 744
Cdd:PRK10535 97 LLSHLTAAQNVEV-PAVYAGLERKQRLL----RAQEL---LQRLGLED--RVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 334185504 745 LLDDPFSAVDAHTAGVLFhkCVEDSLKEK--TVILVTH 780
Cdd:PRK10535 167 LADEPTGALDSHSGEEVM--AILHQLRDRghTVIIVTH 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1220-1386 |
6.20e-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: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGL-KDLRMKLSIIPQEPTLF-RGCIRT 1297
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFsRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1298 NLDPLGVYSDDEIWKalekcQLKTTISNLPNKLDSSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIdsaTDA 1377
Cdd:PRK11614 100 NLAMGGFFAERDQFQ-----ERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---API 171
|
170
....*....|....*
gi 334185504 1378 IIQRI------IREE 1386
Cdd:PRK11614 172 IIQQIfdtieqLREQ 186
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
622-782 |
6.48e-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: 55.11 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 622 EIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQT-SWIQSGTIRDnILYGKP---MESRRYNAAI 696
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYiKADYEGTVRD-LLSSITkdfYTHPYFKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 697 kacaldkdMNGFGHGDLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA----HTAGVLFHKCVEdslKE 772
Cdd:cd03237 100 --------AKPLQIEQILD--REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFAEN---NE 166
|
170
....*....|
gi 334185504 773 KTVILVTHQV 782
Cdd:cd03237 167 KTAFVVEHDI 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
629-780 |
6.78e-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: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 629 VAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVfGS---IAYVSQ---------TSW--IQSGTirDNILYGK-PMESRRYN 693
Cdd:TIGR03719 351 VGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GEtvkLAYVDQsrdaldpnkTVWeeISGGL--DIIKLGKrEIPSRAYV 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 694 AAIkacaldkdmnGFGHGDLTE-IGQrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLfhkcvEDSLKE 772
Cdd:TIGR03719 428 GRF----------NFKGSDQQKkVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL-----EEALLN 488
|
170
....*....|
gi 334185504 773 --KTVILVTH 780
Cdd:TIGR03719 489 faGCAVVISH 498
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
717-798 |
7.37e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.36 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 717 GQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQV------------ME 784
Cdd:PRK10619 147 GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMgfarhvsshvifLH 226
|
90
....*....|....
gi 334185504 785 EGTITQSGKYEELL 798
Cdd:PRK10619 227 QGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
600-807 |
8.47e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.51 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 600 IQVGN--FGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IA 664
Cdd:PRK13650 5 IEVKNltFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwdirhkIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 665 YVSQTSWIQ--SGTIRDNILYG--------KPMESRrynaaikacaLDKDMNGFGHGDLTEigQRGINLSGGQKQRIQLA 734
Cdd:PRK13650 85 MVFQNPDNQfvGATVEDDVAFGlenkgiphEEMKER----------VNEALELVGMQDFKE--REPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 735 RAVYADADVYLLDDPFSAVDAHTAGVLFhKCVEdSLKEK---TVILVTHQ-----------VMEEGTITQSGKYEELLMM 800
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELI-KTIK-GIRDDyqmTVISITHDldevalsdrvlVMKNGQVESTSTPRELFSR 230
|
....*..
gi 334185504 801 GTAFQQL 807
Cdd:PRK13650 231 GNDLLQL 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
616-798 |
8.51e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.98 E-value: 8.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPK---VSGTVKVFGSI----------AYVSQTS-WIQSGTIRDNI 681
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPidakemraisAYVQQDDlFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 LYGKPME-SRRYNAAIKACALDK--DMNGFGHGDLTEIGQRGI--NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH 756
Cdd:TIGR00955 121 MFQAHLRmPRRVTKKEKRERVDEvlQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 757 TAGVLFHKCVEDSLKEKTVILVTHQ-------------VMEEGTITQSGKYEELL 798
Cdd:TIGR00955 201 MAYSVVQVLKGLAQKGKTIICTIHQpsselfelfdkiiLMAEGRVAYLGSPDQAV 255
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1220-1397 |
9.02e-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: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDlrMKLSIIPQEPTLF-RGCIRTN 1298
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYpHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1299 LD-PLGV--YSDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLDEATasidSAT 1375
Cdd:cd03301 93 IAfGLKLrkVPKDEIDERVREVAELLQIEHLLDRKPKQLSG-------GQRQRVALGRAIVREPKVFLMDEPL----SNL 161
|
170 180
....*....|....*....|....*...
gi 334185504 1376 DAIIQRIIREEFA------DCTVITVAH 1397
Cdd:cd03301 162 DAKLRVQMRAELKrlqqrlGTTTIYVTH 189
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
600-780 |
9.70e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.48 E-value: 9.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 600 IQVGNFGWEPETKIPT----LRNIHLEIKHGQKVAVCGPVGAGKSSL---LHAVL----GEI---------PKVSGTVKV 659
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLlpdtGTIewifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 660 FGS---------------------IAYVSQTSWIQ--SGTIRDNILYG-------KPMESRRYNAAIKACALDKdmngfg 709
Cdd:PRK13651 83 VLEklviqktrfkkikkikeirrrVGVVFQFAEYQlfEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGLDE------ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 710 hgdltEIGQRG-INLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHtaGV-----LFHKCVEdslKEKTVILVTH 780
Cdd:PRK13651 157 -----SYLQRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQ--GVkeileIFDNLNK---QGKTIILVTH 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1206-1291 |
1.32e-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: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1206 LQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDgidiskiglKDLRMklSIIP 1285
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLRI--GYLP 67
|
....*.
gi 334185504 1286 QEPTLF 1291
Cdd:COG0488 68 QEPPLD 73
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1221-1411 |
1.41e-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: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDIS--------KIGlkdlrMklsiIPQEPTL 1290
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRsprdaialGIG-----M----VHQHFML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1291 FRgcirtNL------------DPLGVYSDDEIWKALEKcqlkttIS---NLPNKLDSSVSDegenWSVGQRQlfclgRV- 1354
Cdd:COG3845 92 VP-----NLtvaenivlglepTKGGRLDRKAARARIRE------LSeryGLDVDPDAKVED----LSVGEQQ-----RVe 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1355 ----LLKRNKILVLDEATASI-DSATDAIIqRIIReEFAD--CTVITVAHRVPTVID-SDMVMVL 1411
Cdd:COG3845 152 ilkaLYRGARILILDEPTAVLtPQEADELF-EILR-RLAAegKSIIFITHKLREVMAiADRVTVL 214
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
614-781 |
1.51e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS------IAYVSQTSWI--QSG-----TIRDN 680
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVghRSGinpylTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 ILYGKPMESrrynaaiKACALDKDMNGFGHGDLTEIgQRGInLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGV 760
Cdd:PRK13540 95 CLYDIHFSP-------GAVGITELCRLFSLEHLIDY-PCGL-LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|.
gi 334185504 761 LFHKCVEDSLKEKTVILVTHQ 781
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQ 186
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1212-1399 |
1.67e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.30 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1212 RYRPNAPLVLKGISCTFRE-------------GTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIgLKDLR 1278
Cdd:PRK11247 6 RLNQGTPLLLNAVSKRYGErtvlnqldlhipaGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-REDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1279 MKLsiipQEPTLFRGciRTNLD--PLGVYSD--DEIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRV 1354
Cdd:PRK11247 85 LMF----QDARLLPW--KKVIDnvGLGLKGQwrDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALARA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 334185504 1355 LLKRNKILVLDEATASIDSATDAIIQRII-----REEFadcTVITVAHRV 1399
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIeslwqQHGF---TVLLVTHDV 194
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
616-780 |
1.86e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.15 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAV--LGEI---PKVSGTVKVFGS-------------IAYVSQT-SWIQSGT 676
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELypeARVSGEVYLDGQdifkmdvielrrrVQMVFQIpNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 677 IRDNILYG----------KPMESRRYNAAIKACALDKDMNgfghgdltEIGQRGINLSGGQKQRIQLARAVYADADVYLL 746
Cdd:PRK14247 99 IFENVALGlklnrlvkskKELQERVRWALEKAQLWDEVKD--------RLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190
....*....|....*....|....*....|....
gi 334185504 747 DDPFSAVDAHTAGVLFHKCVEDSlKEKTVILVTH 780
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELK-KDMTIVLVTH 203
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1193-1372 |
2.09e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1193 RPPSSWPsngTIHLQELKIRYrPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKI 1272
Cdd:PRK10522 315 QAFPDWQ---TLELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1273 GLKDLRMKLSIIPQEPTLFRgciRTnLDPLGVYSDDEI---WKALEKCQLKTTISnlpnklDSSVSDegENWSVGQRQLF 1349
Cdd:PRK10522 391 QPEDYRKLFSAVFTDFHLFD---QL-LGPEGKPANPALvekWLERLKMAHKLELE------DGRISN--LKLSKGQKKRL 458
|
170 180
....*....|....*....|...
gi 334185504 1350 CLGRVLLKRNKILVLDEATASID 1372
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQD 481
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1220-1372 |
2.23e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 53.56 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI--SKIGLKDLRMKLSIIPQEPTLFR----- 1292
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFYLFPhltal 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1293 -----GCIRTNldplGVYSDDEIWKALE---KCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVL 1364
Cdd:PRK09493 96 envmfGPLRVR----GASKEEAEKQAREllaKVGLAERAHHYPSEL-----------SGGQQQRVAIARALAVKPKLMLF 160
|
....*...
gi 334185504 1365 DEATASID 1372
Cdd:PRK09493 161 DEPTSALD 168
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
629-772 |
2.23e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 629 VAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVfGS---IAYVSQ---------TSW--IQSGTirDNILYGK-PMESRRYN 693
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvkLAYVDQsrdaldpnkTVWeeISGGL--DIIKVGNrEIPSRAYV 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 694 AAIkacaldkdmnGFGHGDlteigQRGI--NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLfhkcvEDSLK 771
Cdd:PRK11819 430 GRF----------NFKGGD-----QQKKvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRAL-----EEALL 489
|
.
gi 334185504 772 E 772
Cdd:PRK11819 490 E 490
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1220-1397 |
2.24e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.50 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDL----RMKLSIIPQEPTLFRG-C 1294
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1295 IRTNLDPLGVYSDDEIWKALEKCQ-------LKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLDEA 1367
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQellqrlgLEDRVEYQPSQL-----------SGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190
....*....|....*....|....*....|.
gi 334185504 1368 TASIDSATDAIIQRIIRE-EFADCTVITVAH 1397
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQlRDRGHTVIIVTH 202
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1201-1435 |
2.50e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.24 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1201 NGTIHLQELKIRYRPNAPLVLKGI---SCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG----IDISKIG 1273
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTPFEFKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1274 -LKDLRMKLSIIPQEP--TLFRGCIRTNL--DPLGVYSDDEiwKALEKCQLKTTISNLPNKLDSSVSDEgenWSVGQRQL 1348
Cdd:PRK13645 84 eVKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENKQ--EAYKKVPELLKLVQLPEDYVKRSPFE---LSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1349 FCLGRVLLKRNKILVLDEATASIDSATDA----IIQRIIREEFAdcTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPS 1423
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEdfinLFERLNKEYKK--RIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPF 236
|
250
....*....|..
gi 334185504 1424 KLMETDSYFSKL 1435
Cdd:PRK13645 237 EIFSNQELLTKI 248
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
616-797 |
2.55e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.02 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVfGSIAYVSQTSWIQSGTIRDNI--LYGKPmESRRYN 693
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-DDITITHKTKDKYIRPVRKRIgmVFQFP-ESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 694 AAI--------KACALD-KDMNGFGHGDLTEIG-------QRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA-- 755
Cdd:PRK13646 101 DTVereiifgpKNFKMNlDEVKNYAHRLLMDLGfsrdvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPqs 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 756 -HTAGVLFHKCVEDslKEKTVILVTHQ------------VMEEGTITQSGKYEEL 797
Cdd:PRK13646 181 kRQVMRLLKSLQTD--ENKTIILVSHDmnevaryadeviVMKEGSIVSQTSPKEL 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
607-788 |
2.86e-07 |
|
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: 55.79 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 607 WEPETKiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQSG----------- 675
Cdd:TIGR01257 938 FEPSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLgmcpqhnilfh 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 --TIRDNILYGKPMESRRYN-AAIKACALDKDmNGFGHgdltEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSA 752
Cdd:TIGR01257 1017 hlTVAEHILFYAQLKGRSWEeAQLEMEAMLED-TGLHH----KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 334185504 753 VDAHTagvlfHKCVEDSLKE----KTVILVTHQvMEEGTI 788
Cdd:TIGR01257 1092 VDPYS-----RRSIWDLLLKyrsgRTIIMSTHH-MDEADL 1125
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1206-1372 |
3.21e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.04 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1206 LQELKIRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGlKDLRMKLSIIP 1285
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1286 QEPTL---FrgCIRTNLDPLGVYSDDEIWKALEKCQLKTTISNLPNKLDSSVSDegenWSVGQRQLFCLGRVLLKRNKIL 1362
Cdd:PRK13537 87 QFDNLdpdF--TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVL 160
|
170
....*....|
gi 334185504 1363 VLDEATASID 1372
Cdd:PRK13537 161 VLDEPTTGLD 170
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1204-1397 |
3.55e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.55 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1204 IHLQELKIRYRPNAPLVLK---GISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCI------------------ 1262
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1263 LIDGIDISKI------GLKDLRMKLSIIPQ--EPTLFRGCIRTNL--DPLGVYSDDEiwKALEKCQLKTTISNLP-NKLD 1331
Cdd:PRK13651 83 VLEKLVIQKTrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSKE--EAKKRAAKYIELVGLDeSYLQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1332 SSVSdegeNWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADC-TVITVAH 1397
Cdd:PRK13651 161 RSPF----ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTH 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
611-760 |
3.85e-07 |
|
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: 52.82 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 611 TKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIpKVSGtvkvfGSIAYVSQTSWIQSGTI---------RDNI 681
Cdd:COG4778 22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNY-LPDS-----GSILVRHDGGWVDLAQAspreilalrRRTI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 682 ------LYGKP--------MESRRYNAAIKACALDKDMNGFGHGDLTEigqrgiNL--------SGGQKQRIQLARAVYA 739
Cdd:COG4778 96 gyvsqfLRVIPrvsaldvvAEPLLERGVDREEARARARELLARLNLPE------RLwdlppatfSGGEQQRVNIARGFIA 169
|
170 180
....*....|....*....|.
gi 334185504 740 DADVYLLDDPFSAVDAHTAGV 760
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAV 190
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1211-1418 |
4.12e-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: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1211 IRYRPNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVE--PASGCILIDGIDiskiglkdlrmklsiIPQEP 1288
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ---------------FGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1289 TLfrgcirtnLDPLGVYSD-DEIWKALEKCQLKTTISNL--PNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLD 1365
Cdd:COG2401 101 SL--------IDAIGRKGDfKDAVELLNAVGLSDAVLWLrrFKEL-----------STGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 1366 EATASIDSATDAIIQRIIREEF--ADCTVITVAHRvPTVIDS---DMVMVLSFGDLVE 1418
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLArrAGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1174-1397 |
4.13e-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: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1174 RIKQYMNIPEEPPAIIDDK----RPPSSWPSNGTIHLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLIS 1249
Cdd:COG0488 282 RIKALEKLEREEPPRRDKTveirFPPPERLGKKVLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1250 ALFRLVEPASGCIlidgidisKIGLKdlrMKLSIIPQEptlfrgciRTNLDP-LGVYsdDEIWKALEKCQlKTTISNL-- 1326
Cdd:COG0488 360 LLAGELEPDSGTV--------KLGET---VKIGYFDQH--------QEELDPdKTVL--DELRDGAPGGT-EQEVRGYlg 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1327 -----PNKLDSSVSDegenWSVGQRQLFCLGRVLLKRNKILVLDEAT-----ASIDSATDAIiqriirEEFaDCTVITVA 1396
Cdd:COG0488 418 rflfsGDDAFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTnhldiETLEALEEAL------DDF-PGTVLLVS 486
|
.
gi 334185504 1397 H 1397
Cdd:COG0488 487 H 487
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
600-799 |
4.67e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.27 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 600 IQVGNFGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYV 666
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 667 SQTS--WIQSGTIRDNILYGkPME--------SRRYNAAIKACALDKDMNGFGHgdlteigqrgiNLSGGQKQRIQLARA 736
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFG-PINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 737 VYADADVYLLDDPFSAVDAHTAGVLFhKCVEDSLKE--KTVILVTHQ------------VMEEGTITQSGKYEELLM 799
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETygMTVIFSTHQldlvpemadyiyVMDKGRIVAYGTVEEIFL 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
605-835 |
4.75e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.17 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 605 FGWEPETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-------------IAYVSQTSW 671
Cdd:PRK13642 12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwnlrrkIGMVFQNPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 672 IQ--SGTIRDNILYGKPMESRRYNAAIKAcaLDKDMNGFGHGDLTEigQRGINLSGGQKQRIQLARAVYADADVYLLDDP 749
Cdd:PRK13642 92 NQfvGATVEDDVAFGMENQGIPREEMIKR--VDEALLAVNMLDFKT--REPARLSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 750 FSAVDAHTAGVLFHkcVEDSLKEK---TVILVTHQVMEEGT-----ITQSGKyeelLMMGTAFQQLVNAHNDAVTV---L 818
Cdd:PRK13642 168 TSMLDPTGRQEIMR--VIHEIKEKyqlTVLSITHDLDEAASsdrilVMKAGE----IIKEAAPSELFATSEDMVEIgldV 241
|
250
....*....|....*..
gi 334185504 819 PLASNeSLGDLRKEGKD 835
Cdd:PRK13642 242 PFSSN-LMKDLRKNGFD 257
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
618-797 |
5.13e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.69 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 618 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQ-----TSWIQS------GTIRDNILYGK 685
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPPyqrpiNMMFQSyalfphMTVEQNIAFGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 686 PmESRRYNAAIKACAldKDMNGFGHgdLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHK 764
Cdd:PRK11607 117 K-QDKLPKAEIASRV--NEMLGLVH--MQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 334185504 765 CVeDSLKE--KTVILVTHQ------------VMEEGTITQSGKYEEL 797
Cdd:PRK11607 192 VV-DILERvgVTCVMVTHDqeeamtmagriaIMNRGKFVQIGEPEEI 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1204-1270 |
5.38e-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: 5.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 1204 IHLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASG-CILIDGIDIS 1270
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGiVTWGSTVKIG 66
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
618-785 |
6.22e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.89 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 618 NIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS------------IAYVSQTSWIQSG-TIRDNILyg 684
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQFDNLDPDfTVRENLL-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 685 kpMESRRYNAAIKAC-ALDKDMNGFGHGDLTEIGQRGiNLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFH 763
Cdd:PRK13537 103 --VFGRYFGLSAAAArALVPPLLEFAKLENKADAKVG-ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170 180
....*....|....*....|..
gi 334185504 764 KCVEDSLKEKTVILVTHqVMEE 785
Cdd:PRK13537 180 RLRSLLARGKTILLTTH-FMEE 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
622-783 |
7.67e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 622 EIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQtsWI---QSGTIRDnILY--GKPMESRRYNAAI 696
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVED-LLRsiTDDLGSSYYKSEI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 697 kacaldkdMNGFGhgdLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPfSAvdahtagvlfHKCVEDSL----- 770
Cdd:PRK13409 438 --------IKPLQ---LERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEP-SA----------HLDVEQRLavaka 495
|
170 180
....*....|....*....|
gi 334185504 771 -------KEKTVILVTHQVM 783
Cdd:PRK13409 496 irriaeeREATALVVDHDIY 515
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
616-780 |
8.72e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.40 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSI--AYVSQTSWI-QSGTIRDNILYG---KPMES 689
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIkvGYLPQEPQLdPTKTVRENVEEGvaeIKDAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 690 RRYNA-AIKACALDKDMNGFG--HGDLTEIGQRG-------------------------INLSGGQKQRIQLARAVYADA 741
Cdd:TIGR03719 101 DRFNEiSAKYAEPDADFDKLAaeQAELQEIIDAAdawdldsqleiamdalrcppwdadvTKLSGGERRRVALCRLLLSKP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 334185504 742 DVYLLDDPFSAVDAHTAGVLfhkcvEDSLKE--KTVILVTH 780
Cdd:TIGR03719 181 DMLLLDEPTNHLDAESVAWL-----ERHLQEypGTVVAVTH 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1219-1385 |
1.28e-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: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1219 LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLR-MKLSIIPQEPtLFRGCIRT 1297
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDR-LGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1298 -----NLDpLGVYSDDEI-------WKALE------------KCQ-LKTTISNLpnkldssvsdegenwSVGQRQLFCLG 1352
Cdd:COG3845 351 msvaeNLI-LGRYRRPPFsrggfldRKAIRafaeelieefdvRTPgPDTPARSL---------------SGGNQQKVILA 414
|
170 180 190
....*....|....*....|....*....|....
gi 334185504 1353 RVLLKRNKILVLDEATASID-SATDAIIQRIIRE 1385
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDvGAIEFIHQRLLEL 448
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1220-1425 |
1.34e-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: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDI--------SKIGLKDLRMKLSIIPQEPTLF 1291
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1292 RGciRTNLD-----PL---GVYSDDEIWKA---LEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNK 1360
Cdd:PRK11264 98 PH--RTVLEniiegPVivkGEPKEEATARArelLAKVGLAGKETSYPRRL-----------SGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 1361 ILVLDEATASIDSATDAIIQRIIR---EEfaDCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKL 1425
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRqlaQE--KRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1221-1418 |
1.47e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKD-LRMKLSIIPQE----PTLfrgCI 1295
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1296 RTNL------DPLGVysddeiwkaLEKCQLKTTISNLPNKLDSSVSDEG--ENWSVGQRQLFCLGRVLLKRNKILVLDEA 1367
Cdd:PRK11288 97 AENLylgqlpHKGGI---------VNRRLLNYEAREQLEHLGVDIDPDTplKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1368 TASIDSATDAIIQRIIREEFADCTVIT-VAHRVPTVID-SDMVMVLSFGDLVE 1418
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
597-798 |
1.53e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 597 AVDIQVGNFGWEPEtkiPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKvfgsiayvsqtsWIQsgt 676
Cdd:PRK15064 319 ALEVENLTKGFDNG---PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------------WSE--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 677 irdnilygkpmesrryNAAIKACALD------KDMNGF---------GHGDLT-------------EIGQRGINLSGGQK 728
Cdd:PRK15064 381 ----------------NANIGYYAQDhaydfeNDLTLFdwmsqwrqeGDDEQAvrgtlgrllfsqdDIKKSVKVLSGGEK 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 729 QRIQLARAVYADADVYLLDDPFSAVDAHTAGVLfhkcvEDSLK--EKTVILVTH-------------QVMEEGTITQSGK 793
Cdd:PRK15064 445 GRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL-----NMALEkyEGTLIFVSHdrefvsslatriiEITPDGVVDFSGT 519
|
....*
gi 334185504 794 YEELL 798
Cdd:PRK15064 520 YEEYL 524
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1209-1302 |
1.56e-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: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1209 LKIRYRPNAPL--VLKGISCTFREGTRVGVVGRTGSGKS-TLISALfRLVEP----ASGCILIDGIDISKIGLKDLR--- 1278
Cdd:COG4172 12 LSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLLGLSERELRrir 90
|
90 100
....*....|....*....|....*
gi 334185504 1279 -MKLSIIPQEPTlfrgcirTNLDPL 1302
Cdd:COG4172 91 gNRIAMIFQEPM-------TSLNPL 108
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
622-783 |
1.87e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.48 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 622 EIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQ-TSWIQSGTIRDNI--LYGKPMESRRYNAAIka 698
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQyISPDYDGTVEEFLrsANTDDFGSSYYKTEI-- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 699 caldkdMNGFGhgdLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPfSAvdahtagvlfHKCVEDSL------- 770
Cdd:COG1245 440 ------IKPLG---LEKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEP-SA----------HLDVEQRLavakair 499
|
170
....*....|....*...
gi 334185504 771 -----KEKTVILVTHQVM 783
Cdd:COG1245 500 rfaenRGKTAMVVDHDIY 517
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
626-781 |
1.97e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.57 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 626 GQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGSIAYVSQTSWIQSGTI-RDNILY--------------------- 683
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVtQDDILYphltvretlvfcsllrlpksl 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 684 GKPMESRRYNAAIKACALDKDMNgfghgdlTEIGQ---RGInlSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGV 760
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCEN-------TIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180
....*....|....*....|.
gi 334185504 761 LFHKCVEDSLKEKTVILVTHQ 781
Cdd:PLN03211 245 LVLTLGSLAQKGKTIVTSMHQ 265
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1220-1417 |
2.06e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.94 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--IDIS--------KIGL--KDlRMKLSIIPQE 1287
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRsprdairaGIAYvpED-RKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1288 PtlfrgcIRTN--------LDPLGVYSDDEIWKALE--------KCQ-LKTTISNLpnkldssvsdegenwSVGQRQLFC 1350
Cdd:COG1129 346 S------IRENitlasldrLSRGGLLDRRRERALAEeyikrlriKTPsPEQPVGNL---------------SGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185504 1351 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIReEFAD--CTVItvahrvptVIDSDM---------VMVLSFGDLV 1417
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIR-ELAAegKAVI--------VISSELpellglsdrILVMREGRIV 473
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
612-755 |
2.11e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.77 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLG--EIpkVSGTVKVFGS-----------IAYVSQT-SWIQSGTI 677
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleRI--TSGEIWIGGRvvnelepadrdIAMVFQNyALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 678 RDNILYG-------KPMESRRYNAAIKacaldkdmngfghgdLTEIGQ----RGINLSGGQKQRIQLARAVYADADVYLL 746
Cdd:PRK11650 94 RENMAYGlkirgmpKAEIEERVAEAAR---------------ILELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
....*....
gi 334185504 747 DDPFSAVDA 755
Cdd:PRK11650 159 DEPLSNLDA 167
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
630-789 |
2.16e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.25 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 630 AVCGPVGAGKSSLLHAVLGEIPKVSGtVKVFGSIAYVSQTSWIQSGTI----RDNILYGKP-------MESRRYNAAIKA 698
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRSIFNYRDVLefrrRVGMLFQRPnpfpmsiMDNVLAGVRAHK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 699 CALDKDMNGFGHGDLTEIG----------QRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVL--FHKCV 766
Cdd:PRK14271 130 LVPRKEFRGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIeeFIRSL 209
|
170 180
....*....|....*....|...
gi 334185504 767 EDSLkekTVILVTHQVMEEGTIT 789
Cdd:PRK14271 210 ADRL---TVIIVTHNLAQAARIS 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1219-1417 |
2.18e-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: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1219 LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPA---SGCILIDGidiskiglkdlrmklsiIPQEPTLFRGCI 1295
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG-----------------QPRKPDQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1296 R------TNLDPLGVYsddEIWkalekcqLKTTISNLPNKLDSSVSDEG-------------------ENWSVGQRQLFC 1350
Cdd:cd03234 84 AyvrqddILLPGLTVR---ETL-------TYTAILRLPRKSSDAIRKKRvedvllrdlaltriggnlvKGISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 1351 LGRVLLKRNKILVLDEATASIDSATDAIIQRIIReEFA--DCTVITVAHRvPTvidSDM------VMVLSFGDLV 1417
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLS-QLArrNRIVILTIHQ-PR---SDLfrlfdrILLLSSGEIV 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1215-1397 |
2.97e-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: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1215 PNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISalfrlvepasgciLIDGIDISKIG--LKDLRMKLSIIPQEPTL-- 1290
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAGVDKDFNGeaRPQPGIKVGYLPQEPQLdp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1291 --------FRGC--IRTNLDPL----GVYSD-DEIWKAL--EKCQLKTTIS-----NLPNKL------------DSSVsd 1336
Cdd:TIGR03719 82 tktvrenvEEGVaeIKDALDRFneisAKYAEpDADFDKLaaEQAELQEIIDaadawDLDSQLeiamdalrcppwDADV-- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 1337 egENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIReEFADcTVITVAH 1397
Cdd:TIGR03719 160 --TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ-EYPG-TVVAVTH 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1171-1372 |
3.22e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 50.98 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1171 SVERIKQYMNIPEEPPAIIDDKRPPSSWPSNGTIHLQELKIRYRPNAplVLKGISCTFREGTRVGVVGRTGSGKSTLISA 1250
Cdd:PRK13536 9 EAPRRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1251 LFRLVEPASGCILIDGIDI-SKIGLKdlRMKLSIIPQEPTLFRG-CIRTNLDPLGVY---SDDEIWKALEKCqlkTTISN 1325
Cdd:PRK13536 87 ILGMTSPDAGKITVLGVPVpARARLA--RARIGVVPQFDNLDLEfTVRENLLVFGRYfgmSTREIEAVIPSL---LEFAR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 334185504 1326 LPNKLDSSVSDegenWSVGQRQLFCLGRVLLKRNKILVLDEATASID 1372
Cdd:PRK13536 162 LESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
610-780 |
3.60e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.78 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 610 ETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-----------------SIAYVSQT-SW 671
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakHVGFVFQSfML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 672 IQSGTIRDNI-----LYGKPMESRRYNAAikacALDKDMNgfghgdlteIGQR----GINLSGGQKQRIQLARAVYADAD 742
Cdd:PRK10584 100 IPTLNALENVelpalLRGESSRQSRNGAK----ALLEQLG---------LGKRldhlPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 334185504 743 VYLLDDPFSAVDAHT----AGVLFhkcvedSLKEK---TVILVTH 780
Cdd:PRK10584 167 VLFADEPTGNLDRQTgdkiADLLF------SLNREhgtTLILVTH 205
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1220-1422 |
3.99e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.85 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDlrMKLSIIPQEPTLFRGciRTNL 1299
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRH--MTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1300 D--------------PLGVYSDDEIWKALEKCQLkttiSNLPNKLDSSVSDegenwsvGQRQLFCLGRVLLKRNKILVLD 1365
Cdd:PRK10851 93 DniafgltvlprrerPNAAAIKAKVTQLLEMVQL----AHLADRYPAQLSG-------GQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 1366 EATASIDSATDAIIQRIIR---EEFaDCTVITVAHRVPTVID-SDMVMVLSFGDLVEYNEP 1422
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRqlhEEL-KFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTP 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1231-1437 |
4.28e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1231 GTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDG--ID-ISKIGLKDLRMKLSIIPQEPTlfrgcirTNLDPLGV--Y 1305
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDtLSPGKLQALRRDIQFIFQDPY-------ASLDPRQTvgD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1306 SDDEIWKALEKCQLKTTISNLPNKLDSSVSDEGENW------SVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAII 1379
Cdd:PRK10261 423 SIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWryphefSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1380 QRIIREEFADCTV--ITVAHRVPTVID-SDMVMVLSFGDLVEYNEPSKLMETDS--YFSKLVA 1437
Cdd:PRK10261 503 INLLLDLQRDFGIayLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQhpYTRKLMA 565
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1231-1413 |
4.48e-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: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1231 GTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLRMKLSIIPQEPTLFRGcirtnldplgvysddei 1310
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1311 wkalekcqlkttisnlpnkldssvsdegenwsVGQRQLFclGRVLLKRNKILVLDEATASIDSATDAIIQRIIR------ 1384
Cdd:smart00382 65 --------------------------------LRLRLAL--ALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180 190
....*....|....*....|....*....|
gi 334185504 1385 -EEFADCTVITVAHRVPTVIDSDMVMVLSF 1413
Cdd:smart00382 111 lKSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
616-785 |
6.14e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWIQSG--------------TIRDN 680
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqEMRFASTTAALAAGvaiiyqelhlvpemTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 ILYGK-PMesrrynaaiKACALD-KDMNGFGHGDLTEIG------QRGINLSGGQKQRIQLARAVYADADVYLLDDPFSA 752
Cdd:PRK11288 100 LYLGQlPH---------KGGIVNrRLLNYEAREQLEHLGvdidpdTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190
....*....|....*....|....*....|....
gi 334185504 753 VDAHTAGVLFhKCVEDSLKEKTVIL-VTHQvMEE 785
Cdd:PRK11288 171 LSAREIEQLF-RVIRELRAEGRVILyVSHR-MEE 202
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
924-1175 |
8.01e-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: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 924 MLIGVYSIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAFIF 1003
Cdd:cd07346 40 WIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1004 VVAPAVELTAALLIMTYVTWQVIIIALLALAATKVVQDYYLASARELIRINGTTKAPVMNYAAETSLGVVTIRAFGTAER 1083
Cdd:cd07346 120 LLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEER 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1084 FFKNYLNLVDADAVLFFLSNAAMEWVILRIETLQNvtLFTCALLLI---LIPKGYIAPGLVGLSLSYALTLTQTQVFLTR 1160
Cdd:cd07346 200 EIERFREANRDLRDANLRAARLSALFSPLIGLLTA--LGTALVLLYggyLVLQGSLTIGELVAFLAYLGMLFGPIQRLAN 277
|
250
....*....|....*
gi 334185504 1161 WYCTLSNSIISVERI 1175
Cdd:cd07346 278 LYNQLQQALASLERI 292
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1199-1398 |
8.51e-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: 50.52 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1199 PSNGTIHLQELKIRYR------PNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLisalFRLVE---PASGCILIdgidi 1269
Cdd:TIGR00954 440 PGRGIVEYQDNGIKFEniplvtPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSL----FRILGelwPVYGGRLT----- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1270 skiglKDLRMKLSIIPQEPTLFRGCIRTNLdplgVY---SDDEIWKALEKCQLKTTISNLpnKLDSSVSDEG-----ENW 1341
Cdd:TIGR00954 511 -----KPAKGKLFYVPQRPYMTLGTLRDQI----IYpdsSEDMKRRGLSDKDLEQILDNV--QLTHILEREGgwsavQDW 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185504 1342 ----SVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREefADCTVITVAHR 1398
Cdd:TIGR00954 580 mdvlSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1199-1433 |
9.23e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.01 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1199 PSNGT---IHLQELKIRYRPNapLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFR---LVEP--ASGCILIDGIDI- 1269
Cdd:PRK14243 3 TLNGTetvLRTENLNVYYGSF--LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1270 -SKIGLKDLRMKLSIIPQEPTLFRGCIRTNL----DPLGVYSD-DE-IWKALEKCQLKTTISNlpnKLDSSvsdeGENWS 1342
Cdd:PRK14243 81 aPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIaygaRINGYKGDmDElVERSLRQAALWDEVKD---KLKQS----GLSLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1343 VGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFADCTVITVAH------RVptvidSDMVMVLS---- 1412
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRV-----SDMTAFFNvelt 228
|
250 260 270
....*....|....*....|....*....|..
gi 334185504 1413 -----FGDLVEYNEPSKLM------ETDSYFS 1433
Cdd:PRK14243 229 egggrYGYLVEFDRTEKIFnspqqqATRDYVS 260
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
614-793 |
1.72e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.20 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 614 PTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWIQSgtIRDNI-LYGKPMESRR 691
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtLITSTSKNKDIKQ--IRKKVgLVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 692 YNAAI-KACALDKDMNGFGHGDLTEIGQR-----GIN----------LSGGQKQRIQLARAVYADADVYLLDDPfsavda 755
Cdd:PRK13649 99 FEETVlKDVAFGPQNFGVSQEEAEALAREklalvGISeslfeknpfeLSGGQMRRVAIAGILAMEPKILVLDEP------ 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 756 hTAGV----------LFHKCVEDSLkekTVILVTH------------QVMEEGTITQSGK 793
Cdd:PRK13649 173 -TAGLdpkgrkelmtLFKKLHQSGM---TIVLVTHlmddvanyadfvYVLEKGKLVLSGK 228
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1155-1379 |
1.78e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1155 QVFLTRWYCTLSNSIISVERIKQYMNIPEEPPAIIDDK-----RPPSSWPsNGTIHLQELKIRYrpNAPLVLKGISCTFR 1229
Cdd:PRK10636 260 QSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPfhfsfRAPESLP-NPLLKMEKVSAGY--GDRIILDSIKLNLV 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1230 EGTRVGVVGRTGSGKSTLISALFRLVEPASGCI-LIDGIdiskiglkdlrmKLSIIPQEPTLFrgcIRTNLDPLGVYSDD 1308
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI------------KLGYFAQHQLEF---LRADESPLQHLARL 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 1309 EIwKALEKcQLKTTISNLPNKLDsSVSDEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASID-----SATDAII 1379
Cdd:PRK10636 402 AP-QELEQ-KLRDYLGGFGFQGD-KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDldmrqALTEALI 474
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1204-1270 |
2.65e-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: 2.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 1204 IHLQELKIRYrpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIS 1270
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT 70
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
612-749 |
2.97e-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: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 612 KIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEiPKVSGtvkvfGSIAYVSQ--TSWIQSGTIRDNILY---GKP 686
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATS-----GRIVFDGKdiTDWQTAKIMREAVAIvpeGRR 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 687 MESR---RYNAAIKACALDKDMNGFGHGDLTEI--------GQRGINLSGGQKQRIQLARAVYADADVYLLDDP 749
Cdd:PRK11614 91 VFSRmtvEENLAMGGFFAERDQFQERIKWVYELfprlherrIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
617-790 |
3.04e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 617 RNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS--------------IAYVSQ----TSWIQSGTIR 678
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITEsrrdNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 679 DNILYGKPMESRRYNAAI----------KACALDKDMNGFGHgdltEIGQRGINLSGGQKQRIQLARAVYADADVYLLDD 748
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMglfhevdeqrTAENQRELLALKCH----SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185504 749 PFSAVDAHTAGVLFHkcVEDSLKE--KTVILVTHQ------------VMEEGTITQ 790
Cdd:PRK09700 436 PTRGIDVGAKAEIYK--VMRQLADdgKVILMVSSElpeiitvcdriaVFCEGRLTQ 489
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1220-1293 |
3.88e-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: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISAL--FRLVEPASGCILIDGIDIskiglKDL------RMKLSIIPQEPTLF 1291
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDI-----TDLppeeraRLGIFLAFQYPPEI 89
|
..
gi 334185504 1292 RG 1293
Cdd:cd03217 90 PG 91
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
609-797 |
3.99e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.10 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 609 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSS---LLHAVL--GEIPKVSGTVKvfgSIAYVSQTSW---------IQS 674
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLlpDDNPNSKITVD---GITLTAKTVWdirekvgivFQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 675 -------GTIRDNILYGkpMESRRYNAAIKACALDKDMNGFGHGDLteIGQRGINLSGGQKQRIQLARAVYADADVYLLD 747
Cdd:PRK13640 93 pdnqfvgATVGDDVAFG--LENRAVPRPEMIKIVRDVLADVGMLDY--IDSEPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 748 DPFSAVD-AHTAGVLfhKCVEDSLKEK--TVILVTHQ-----------VMEEGTITQSGKYEEL 797
Cdd:PRK13640 169 ESTSMLDpAGKEQIL--KLIRKLKKKNnlTVISITHDideanmadqvlVLDDGKLLAQGSPVEI 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
581-780 |
4.19e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 581 LKMDEIERSGldasgtAVDIQVGNFGWEPETKIpTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVf 660
Cdd:PRK11147 307 MQVEEASRSG------KIVFEMENVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 661 GS---IAYVSQTSWI--QSGTIRDNILYGK----------------------PMESRrynAAIKAcaldkdmngfghgdl 713
Cdd:PRK11147 379 GTkleVAYFDQHRAEldPEKTVMDNLAEGKqevmvngrprhvlgylqdflfhPKRAM---TPVKA--------------- 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 714 teigqrginLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLfhkcvEDSLKE--KTVILVTH 780
Cdd:PRK11147 441 ---------LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELL-----EELLDSyqGTVLLVSH 495
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
283-572 |
4.63e-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: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 283 IFIAVFAFLRTFAVVSLPLMLYVFVDYANSdHRDLRNGFFNLACLVMLKLVESLT--MRHWYFAsrRSGMRIRSALMVAA 360
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIP-AGDLSLLLWIALLLLLLALLRALLsyLRRYLAA--RLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 361 YKKQLKLSSLGRKRHSSGEIVNYIAVDAYRMGEFLWW-FHSGWSLSLQLLLSTAVLF------GVVGAGAFPGLILLLLC 433
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILFylnwklTLVALLLLPLYVLILRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 434 gllnlpFAKMLQNCQTQFMIAQDKRLRSTSEILNSMKVIKLQSWEDEFKKKIESCRDDEFTWLAKAQLTKAFGSFLYWMS 513
Cdd:cd07346 159 ------FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 514 PTIVSSVVFL-GCALLKSAPLNASTIFTVLATLRVMSEPVKIIPDAISAIIQGNVSFQRL 572
Cdd:cd07346 233 TALGTALVLLyGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
723-812 |
5.31e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 46.75 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 723 LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLFHKCVEdsLKEK---TVILVTHQ------------VMEEGT 787
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLE--LQEKlgiSYIYVSQHlgivkhisdkvlVMHQGE 227
|
90 100
....*....|....*....|....*....
gi 334185504 788 ITQSGKYEELLM----MGTafQQLVNAHN 812
Cdd:COG4167 228 VVEYGKTAEVFAnpqhEVT--KRLIESHF 254
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
723-807 |
5.40e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 46.67 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 723 LSGGQKQRIQLARAVYADADVYLLDDPFSAVDAHTAGVLF---HKCVEDslKEKTVILVTHQ-----------VMEEGTI 788
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLdlvRKVKSE--HNITIISITHDlseameadhviVMNKGTV 220
|
90
....*....|....*....
gi 334185504 789 TQSGKYEELLMMGTAFQQL 807
Cdd:PRK13648 221 YKEGTPTEIFDHAEELTRI 239
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
616-787 |
5.98e-05 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 46.97 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPK---VSGTVKVFGS-----------------IAYVSQ---TS-- 670
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEdllklsekelrkirgreIQMIFQdpmTSln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 671 --WiqsgTIRDNIlygkpMESRRYnaaikacaldkdmngfgHGDLT--EIGQR--------GIN------------LSGG 726
Cdd:COG0444 101 pvM----TVGDQI-----AEPLRI-----------------HGGLSkaEARERaiellervGLPdperrldrypheLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 727 QKQRIQLARAVYADADVYLLDDPFSAVDAHT-AGV--LFHKcvedsLKEK---TVILVTH------------------QV 782
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIqAQIlnLLKD-----LQRElglAILFITHdlgvvaeiadrvavmyagRI 229
|
....*
gi 334185504 783 MEEGT 787
Cdd:COG0444 230 VEEGP 234
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
721-783 |
6.53e-05 |
|
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: 45.26 E-value: 6.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 721 INLSGGQKQRIQLARAVYADADVYLLDDPFSAVDA----HTAGVLFHKCVEDslkEKTVILVTHQVM 783
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEEG---KKTALVVEHDLA 133
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1219-1423 |
7.28e-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: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1219 LVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIskIGLKDLRMKLSIIPQEPTLFrgcirtn 1298
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALF------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1299 ldP-LGVY------------SDDEIWK----ALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKI 1361
Cdd:cd03300 85 --PhLTVFeniafglrlkklPKAEIKErvaeALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1362 LVLDEATasidSATDAIIQRIIREEFAD------CTVITVAHrvptviD-------SDMVMVLSFGDLVE-------YNE 1421
Cdd:cd03300 152 LLLDEPL----GALDLKLRKDMQLELKRlqkelgITFVFVTH------DqeealtmSDRIAVMNKGKIQQigtpeeiYEE 221
|
..
gi 334185504 1422 PS 1423
Cdd:cd03300 222 PA 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1200-1402 |
7.65e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.41 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1200 SNGTIHLQELKIRYRpNAPLVLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLKDLrm 1279
Cdd:PRK15056 3 QQAGIVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1280 kLSIIPQE-------PTLFRGCIRtnldpLGVYSDD---EIWKALEKCQLKTTISNLpNKLDSSVSDEGEnWSVGQRQLF 1349
Cdd:PRK15056 80 -VAYVPQSeevdwsfPVLVEDVVM-----MGRYGHMgwlRRAKKRDRQIVTAALARV-DMVEFRHRQIGE-LSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 334185504 1350 CLGRVLLKRNKILVLDEATASIDSATDAIIQRIIREEFAD-CTVITVAHRVPTV 1402
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSV 205
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1229-1410 |
1.14e-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: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1229 REGTRVGVVGRTGSGKSTLISALFRLVEPASGCIlidgidiskiglkDLRMKLSIIPQ--EP-------TLFRGCIRTNL 1299
Cdd:COG1245 364 REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQyiSPdydgtveEFLRSANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1300 DplGVYSDDEIWKALekcqlkttisNLPNKLDSSVSDegenWSVGQRQLFCLGRVLLKRNKILVLDEATASIDS----AT 1375
Cdd:COG1245 431 G--SSYYKTEIIKPL----------GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAV 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 334185504 1376 DAIIQRIIREEfaDCTVITVAHRVpTVID--SDMVMV 1410
Cdd:COG1245 495 AKAIRRFAENR--GKTAMVVDHDI-YLIDyiSDRLMV 528
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
631-782 |
1.24e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.55 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 631 VCGPVG---AGKSSLL------------HAVLGEIPKVSGTVKVFG-SIAYVSQTSWIQSG-TIRDNILYGK-PMESR-- 690
Cdd:PRK10575 39 VTGLIGhngSGKSTLLkmlgrhqppsegEILLDAQPLESWSSKAFArKVAYLPQQLPAAEGmTVRELVAIGRyPWHGAlg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 691 RYNAAIKAcALDKDMNGFGhgdLTEIGQRGIN-LSGGQKQRIQLARAVYADADVYLLDDPFSAVD-AHTAGVLfhKCVED 768
Cdd:PRK10575 119 RFGAADRE-KVEEAISLVG---LKPLAHRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVL--ALVHR 192
|
170
....*....|....*.
gi 334185504 769 SLKEK--TVILVTHQV 782
Cdd:PRK10575 193 LSQERglTVIAVLHDI 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1206-1428 |
1.27e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1206 LQELKIRYRPNAPL--VLKGISCTFREGTRVGVVGRTGSGKS-TLISALFRLVEPA----SGCILIDGIDISKIGLKDLR 1278
Cdd:PRK15134 8 IENLSVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1279 M----KLSIIPQEPTLfrgcirtNLDPL---------------GVYSD---DEIWKALEKC---QLKTTISNLPNKLdss 1333
Cdd:PRK15134 88 GvrgnKIAMIFQEPMV-------SLNPLhtlekqlyevlslhrGMRREaarGEILNCLDRVgirQAAKRLTDYPHQL--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1334 vsdegenwSVGQRQLFCLGRVLLKRNKILVLDEATASIDSATDAIIQRIIRE--EFADCTVITVAHRVPTVID-SDMVMV 1410
Cdd:PRK15134 158 --------SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqQELNMGLLFITHNLSIVRKlADRVAV 229
|
250
....*....|....*...
gi 334185504 1411 LSFGDLVEYNEPSKLMET 1428
Cdd:PRK15134 230 MQNGRCVEQNRAATLFSA 247
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
903-1088 |
1.49e-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: 45.61 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 903 FQAASTYWLAFAIGIPKITNTMLI-GVYSIISTLSAGF-VYARAITTAHLGLKASKAFFSgftnAVFKAPMLFFDSTPVG 980
Cdd:cd18572 18 YTGAVIDAVVADGSREAFYRAVLLlLLLSVLSGLFSGLrGGCFSYAGTRLVRRLRRDLFR----SLLRQDIAFFDATKTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 981 RILTRASSDLNVLDYDVPFAFIFVVAPAVELTAALLIMTYVTWQ----VIIIALLALAATKVVQDYYlasaRELIRINGT 1056
Cdd:cd18572 94 ELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRltllAFITVPVIALITKVYGRYY----RKLSKEIQD 169
|
170 180 190
....*....|....*....|....*....|...
gi 334185504 1057 TKApVMNYAAETSLGVV-TIRAFGTAERFFKNY 1088
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) ... |
712-780 |
1.74e-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: 1.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 712 DLTEIGQRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSAVDAH---TAGVLFHKCVEDslkEKTVILVTH 780
Cdd:cd03236 128 ELRHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAED---DNYVLVVEH 197
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
922-1091 |
1.79e-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: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 922 NTMLIGVYsIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTRASSDLNVLDYDVPFAf 1001
Cdd:cd18568 42 NLILIGLL-IVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSA- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1002 IFVVAPAVELTAALLIMTYVTWQ----VIIIALLALAATKVVQDYYLASARELIRingtTKAPVMNYAAETSLGVVTIRA 1077
Cdd:cd18568 120 LTTILDLLMVFIYLGLMFYYNLQltliVLAFIPLYVLLTLLSSPKLKRNSREIFQ----ANAEQQSFLVEALTGIATIKA 195
|
170
....*....|....
gi 334185504 1078 FGTAERFFKNYLNL 1091
Cdd:cd18568 196 LAAERPIRWRWENK 209
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1232-1253 |
1.84e-04 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 45.14 E-value: 1.84e-04
10 20
....*....|....*....|..
gi 334185504 1232 TRVGVVGRTGSGKSTLISALFR 1253
Cdd:COG3596 40 PVIALVGKTGAGKSSLINALFG 61
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
924-1175 |
1.97e-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: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 924 MLIGVYSIISTLSAGFVYARAITTAHLGLKA-----SKAFfsgftNAVFKAPMLFFDSTPVGRILTRASSD--------- 989
Cdd:cd18544 42 LLALLYLGLLLLSFLLQYLQTYLLQKLGQRIiydlrRDLF-----SHIQRLPLSFFDRTPVGRLVTRVTNDtealnelft 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 990 ---LNVLDYDVPFAFIFVVAPAVELTAALL------IMTYVTWqviiiallalAATKVVQDYYLAsARELI-RINGttka 1059
Cdd:cd18544 117 sglVTLIGDLLLLIGILIAMFLLNWRLALIsllvlpLLLLATY----------LFRKKSRKAYRE-VREKLsRLNA---- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1060 pvmnYAAETSLGVVTIRAFGTAERFFKNYLNLVDAdavlFFLSNAAMEWV--ILR--IETLQNVTLftcALLL----ILI 1131
Cdd:cd18544 182 ----FLQESISGMSVIQLFNREKREFEEFDEINQE----YRKANLKSIKLfaLFRplVELLSSLAL---ALVLwyggGQV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 334185504 1132 PKGYIAPGLVglslsYALTLTQTQVF-----LTRWYCTLSNSIISVERI 1175
Cdd:cd18544 251 LSGAVTLGVL-----YAFIQYIQRFFrpirdLAEKFNILQSAMASAERI 294
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1221-1436 |
1.98e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDIS-KIGLKDLRMKLSIIPQEPTLFRGciRTNL 1299
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQ--RSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1300 DP--LGVYSDDEIWKALEKCQLKTtiSNLPNKLDSSVS--DEGENWSVGQRQLFCLGRVLLKRNKILVLDEATASIDSAT 1375
Cdd:PRK10982 92 DNmwLGRYPTKGMFVDQDKMYRDT--KAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 1376 DAIIQRIIRE-EFADCTVITVAHRVPTVID-SDMVMVLSFGDLVEyNEPSKLMETDSYFSKLV 1436
Cdd:PRK10982 170 VNHLFTIIRKlKERGCGIVYISHKMEEIFQlCDEITILRDGQWIA-TQPLAGLTMDKIIAMMV 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
676-799 |
2.26e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.23 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 TIRDNILYGK-PMESRRYNAAIKAcalDKDMNGFGHGDlTEIGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 754
Cdd:PRK13631 133 TIEKDIMFGPvALGVKKSEAKKLA---KFYLNKMGLDD-SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185504 755 AHTAGVLFHKCVEDSLKEKTVILVTHQ------------VMEEGTITQSGKYEELLM 799
Cdd:PRK13631 209 PKGEHEMMQLILDAKANNKTVFVITHTmehvlevadeviVMDKGKILKTGTPYEIFT 265
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1220-1380 |
2.54e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 44.42 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKIGLK---DLR-MKLSIIPQEPTLFRGCi 1295
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRnQKLGFIYQFHHLLPDF- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1296 rTNLD----PL---GVYSDDEIWKALEKCQ---LKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNKILVLD 1365
Cdd:PRK11629 103 -TALEnvamPLligKKKPAEINSRALEMLAavgLEHRANHRPSEL-----------SGGERQRVAIARALVNNPRLVLAD 170
|
170
....*....|....*.
gi 334185504 1366 EATASIDSAT-DAIIQ 1380
Cdd:PRK11629 171 EPTGNLDARNaDSIFQ 186
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
723-781 |
3.03e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 3.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185504 723 LSGGQKQRIQLARAV----YADADVYLLDDPFSAVDAHTAGVLFHKCVEDSLKEKTVILVTHQ 781
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
616-794 |
3.21e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 616 LRNIHLEIKHGQKVAVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFG-SIAYVSQTSWIQSG--------------TIRDN 680
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkEIDFKSSKEALENGismvhqelnlvlqrSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 681 ILYGK-PM------ESRRYNAAIKACA-LDKDMNGfghgdlteiGQRGINLSGGQKQRIQLARAVYADADVYLLDDPFSA 752
Cdd:PRK10982 94 MWLGRyPTkgmfvdQDKMYRDTKAIFDeLDIDIDP---------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 334185504 753 VDAHTAGVLFHkcVEDSLKEK--TVILVTH------QVMEEGTITQSGKY 794
Cdd:PRK10982 165 LTEKEVNHLFT--IIRKLKERgcGIVYISHkmeeifQLCDEITILRDGQW 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
724-754 |
3.36e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.57 E-value: 3.36e-04
10 20 30
....*....|....*....|....*....|.
gi 334185504 724 SGGQKQRIQLARAVYADADVYLLDDPFSAVD 754
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1220-1397 |
4.47e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 43.61 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGIDISKI---GLKDLRMK--------LSIIP--- 1285
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhvgfvfqsFMLIPtln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1286 -----QEPTLFRGCIRTNldplgvySDDEIWKALEKCQLKTTISNLPNKLdssvsdegenwSVGQRQLFCLGRVLLKRNK 1360
Cdd:PRK10584 105 alenvELPALLRGESSRQ-------SRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 334185504 1361 ILVLDEATASIDSAT-DAIIQRI--IREEFAdCTVITVAH 1397
Cdd:PRK10584 167 VLFADEPTGNLDRQTgDKIADLLfsLNREHG-TTLILVTH 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
623-780 |
5.83e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 623 IKHGQKVAVCGPVGAGKSSLLHAVLGE-IP----------------KVSGT-------------VKVFGSIAYVSQTSWI 672
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGElIPnlgdyeeepswdevlkRFRGTelqnyfkklyngeIKVVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 673 QSGTIRDniLYGKPMESRRYNAAIKACALDKDMNgfghgdlteigqRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFS 751
Cdd:PRK13409 176 FKGKVRE--LLKKVDERGKLDEVVERLGLENILD------------RDIsELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|....*.
gi 334185504 752 AVD-------AhtagvlfhKCVEDSLKEKTVILVTH 780
Cdd:PRK13409 242 YLDirqrlnvA--------RLIRELAEGKYVLVVEH 269
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
724-780 |
7.13e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 7.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 334185504 724 SGGQKQRIQLARAVYADADVYLLDDPFSAVDAHtaGVLFhkcVEDSLKE--KTVILVTH 780
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLH--AVLW---LETYLLKwpKTFIVVSH 399
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1221-1435 |
1.28e-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: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1221 LKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPA---SGCILIDGIdisKIGLKDLRMKLSIIPQE----PTL--- 1290
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM---PIDAKEMRAISAYVQQDdlfiPTLtvr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1291 ----FRGCIRTnldPLGVYSD------DEIWKA--LEKCQlkTTISNLPNKLDSsvsdegenWSVGQRQLFCLGRVLLKR 1358
Cdd:TIGR00955 118 ehlmFQAHLRM---PRRVTKKekrervDEVLQAlgLRKCA--NTRIGVPGRVKG--------LSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 1359 NKILVLDEATASIDSATDAIIQRIIReEFAD--CTVITVAHRVPTVIDS--DMVMVLSFGDLVEYNEPSKLMEtdsYFSK 1434
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLK-GLAQkgKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVP---FFSD 260
|
.
gi 334185504 1435 L 1435
Cdd:TIGR00955 261 L 261
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
673-826 |
1.76e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.41 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 673 QSGTIRDNI-LYGKPMESRRYNAAIKAcalDKDMNGFghgDLTEI-GQRGINLSGGQKQRIQLARAVYADADVYLLDDPF 750
Cdd:NF000106 99 ESFSGRENLyMIGR*LDLSRKDARARA---DELLERF---SLTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 751 SAVDAHTAGVLFHKcVEDSLKEKTVILVTHQVMEE-------------GTITQSGKYEEL-------------------- 797
Cdd:NF000106 173 TGLDPRTRNEVWDE-VRSMVRDGATVLLTTQYMEEaeqlaheltvidrGRVIADGKVDELktkvggrtlqirpahaaeld 251
|
170 180 190
....*....|....*....|....*....|....*.
gi 334185504 798 LMMGTAFQQLVNA-------HNDAVTVLPLASNESL 826
Cdd:NF000106 252 RMVGAIAQAGLDGiagatadHEDGVVNVPIVSDEQL 287
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1220-1268 |
1.91e-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: 1.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASGCILIDGID 1268
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD 65
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1233-1253 |
2.35e-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: 2.35e-03
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
609-800 |
2.93e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 609 PETKIPTLRNIHLEIKHGQKVAVCGPVGAGKSSLLHA---------VLGEIpKVSGTVKV---FGSIA-YVSQTSwIQSG 675
Cdd:PLN03140 889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVlagrktggyIEGDI-RISGFPKKqetFARISgYCEQND-IHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 676 --TIRDNILYGK----PMESRRYNaaiKACALDKDMNGFGHGDLTE--IGQRGIN-LSGGQKQRIQLARAVYADADVYLL 746
Cdd:PLN03140 967 qvTVRESLIYSAflrlPKEVSKEE---KMMFVDEVMELVELDNLKDaiVGLPGVTgLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334185504 747 DDPFSAVDAHTAGVLFhKCVEDSLKE-KTVILVTHQvmeeGTITQSGKYEELLMM 800
Cdd:PLN03140 1044 DEPTSGLDARAAAIVM-RTVRNTVDTgRTVVCTIHQ----PSIDIFEAFDELLLM 1093
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1220-1290 |
4.65e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 4.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185504 1220 VLKGISCTFREGTRVGVVGRTGSGKSTLISALFRLVEPASG-CILIDGIdisKIGlkdlrmklsIIPQEPTL 1290
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGI---KVG---------YLPQEPQL 81
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
624-754 |
4.76e-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: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 624 KHGQKVAVCGPVGAGKSSLLHAVLGE-IP----------------------------KVS-GTVKVFGSIAYVSQTSWIQ 673
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGElKPnlgdydeepswdevlkrfrgtelqdyfkKLAnGEIKVAHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 674 SGTIRDniLYGKPMESRRYNAAIKACALDKDMNgfghgdlteigqRGI-NLSGGQKQRIQLARAVYADADVYLLDDPFSA 752
Cdd:COG1245 177 KGTVRE--LLEKVDERGKLDELAEKLGLENILD------------RDIsELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
..
gi 334185504 753 VD 754
Cdd:COG1245 243 LD 244
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
1235-1254 |
6.26e-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: 6.26e-03
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
912-988 |
6.80e-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: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 912 AFAIGIPKIT-----NTMLIGVYSIISTLSAG----------FVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDS 976
Cdd:cd18555 16 LLTLLIPILTqyvidNVIVPGNLNLLNVLGIGililfllyglFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFEN 95
|
90
....*....|..
gi 334185504 977 TPVGRILTRASS 988
Cdd:cd18555 96 RSSGDLLFRANS 107
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
630-754 |
6.98e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 40.63 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185504 630 AVCGPVGAGKSSLLHAVLGEIPKVSGTVKVFGS-----------------IAYVSQTSWI-QSGTIRDNILYG-KPMESR 690
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDARLfPHYKVRGNLRYGmAKSMVA 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 691 RYNAAIKACALDKDMNGFGhgdlteigqrgINLSGGQKQRIQLARAVYADADVYLLDDPFSAVD 754
Cdd:PRK11144 108 QFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
922-985 |
9.51e-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: 9.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185504 922 NTMLIGVySIISTLSAGFVYARAITTAHLGLKASKAFFSGFTNAVFKAPMLFFDSTPVGRILTR 985
Cdd:cd18570 42 NIISIGL-ILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISR 104
|
|
| |
